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2-aminobutyrate + H2O + NADP+
2-oxobutyrate + NH3 + NADPH
-
3% of activity with L-glutamate
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
2-oxoglutarate + NH3 + NAD(P)H + H+
L-glutamate + H2O + NAD(P)+
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADPH
L-glutamate + H2O + NADP+
-
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
homocysteinesulfinate + H2O + NAD(P)+
?
-
-
-
-
?
L-glutamate + H2O + 2-azido-NAD+
2-oxoglutarate + NH3 + 2-azido-NADH
-
-
-
?
L-glutamate + H2O + N6-(2-aminoethyl)-NAD(P)+
2-oxoglutarate + NH3 + N6-(2-aminoethyl)-NAD(P)H
-
-
-
?
L-glutamate + H2O + N6-(2-aminoethyl)-NAD+
2-oxoglutarate + NH3 + N6-(2-aminoethyl)-NADH + H+
-
-
-
-
r
L-glutamate + H2O + N6-(2-hydroxy-3-trimethylammoniumpropyl)-NAD+
2-oxoglutarate + NH3 + N6-(2-hydroxy-3-trimethylammoniumpropyl)-NADH
-
-
-
?
L-glutamate + H2O + N6-(2-hydroxy-3-trimethylammoniumpropyl)-NAD+
2-oxoglutarate + NH3 + N6-(2-hydroxy-3-trimethylammoniumpropyl)-NADH + H+
-
-
-
-
r
L-glutamate + H2O + N6-(3-sulfonatopropyl)-NAD+
2-oxoglutarate + NH3 + N6-(2-sulfonatopropyl)-NADH
-
-
-
?
L-glutamate + H2O + N6-poly(ethyleneglycol)-N6-(2-aminoethyl)-NAD+
2-oxoglutarate + NH3 + )poly(ethyleneglycol)-N6-(2-aminoethyl)-NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + poly(ethyleneglycol)-N6-(2-aminoethyl)-NADP+
2-oxoglutarate + NH3 + poly(ethyleneglycol)-N6-(2-aminoethyl)-NADPH + H+
-
-
-
-
r
L-glutamate + H2O + polyethylenglycol-N6-(2-aminoethyl)-NAD(P)+
2-oxoglutarate + NH3 + polyethylenglycol-N6-(2-aminoethyl)-NAD(P)H
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
norvaline + H2O + NAD(P)+
2-oxopentanoate + NH3 + NAD(P)H
-
-
-
-
?
norvaline + H2O + NADP+
2-oxovalerate + NH3 + NADPH
-
activity is 20% of that observed in the presence of 2-oxoglutarate and L-glutamate
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
-
r
valine + H2O + NADP+
2-oxovalerate + NH3 + NADPH
-
3% of activity with L-glutamate
-
?
additional information
?
-
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
no activity with NAD+ as cofactor
-
-
ir
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
?
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
specific activity in the presence of NADH is about 30% of that with NADPH
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
r
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
highly specific for 2-oxoglutarate and glutamate
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
enzyme for the main route for ammonia assimilation at low concentrations of ammonia
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
very low activity with: leucine, alpha-aminobutyrate, valine, isoleucine and methionine
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
rate of glutamate synthesis is several-fold higher than the rate for the reverse reaction
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
dogfish
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
highly specific for 2-oxoglutarate and glutamate
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
ir
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
ir
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
r
additional information
?
-
-
the similarity in relative activation when both cofactors are present, combined with consistently greater GDH product formation from equimolar NADH than with NADPH, does not support the idea that there is a preferential utilization of NADPH by bovine GDH
-
-
?
additional information
?
-
-
the glutamate formation activity is 3fold higher than the glutamate deamination activity
-
-
?
additional information
?
-
in vitro, the thermodynamic equilibrium of mammalian GDH favors glutamate synthesis. Because the GDH-catalyzed reaction is reversible, its direction is expected to depend on the concentration of the substrates and the affinity of the enzyme (Km value) for these substrates. In addition to substrate concentrations, the GDH catalysis is affected by the pH, the ionic strength and the composition of the buffer
-
-
-
additional information
?
-
in vitro, the thermodynamic equilibrium of mammalian GDH favors glutamate synthesis. Because the GDH-catalyzed reaction is reversible, its direction is expected to depend on the concentration of the substrates and the affinity of the enzyme (Km value) for these substrates. In addition to substrate concentrations, the GDH catalysis is affected by the pH, the ionic strength and the composition of the buffer
-
-
-
additional information
?
-
-
in vitro, the thermodynamic equilibrium of mammalian GDH favors glutamate synthesis. Because the GDH-catalyzed reaction is reversible, its direction is expected to depend on the concentration of the substrates and the affinity of the enzyme (Km value) for these substrates. In addition to substrate concentrations, the GDH catalysis is affected by the pH, the ionic strength and the composition of the buffer
-
-
-
additional information
?
-
the binding affinity of L-glutamate is lower than that of 2-oxoglutarate. Hence, L-glutamate has a weaker affinity than 2-oxoglutarate in binding to the active site of GDH. A comparison of binding site in 2-oxoglutarate and L-glutamate indicate three residues which include Arg401, Trp88, and Arg12 that have important role in interaction between these ligands with active site of GDH
-
-
-
additional information
?
-
-
no activity in the amination reaction direction with NADH or NADPH, 2-oxoglutarate and ammonia
-
-
?
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2-Azido-NAD+
-
0.1 mM, 60% inhibition after 3 min of photolabeling
4-iodoacetamidosalicylic acid
-
-
8-azidoguanosine 5'-triphosphate
-
used for affinity photolabeling, 0.1 mM, 95% inhibition
alanine
-
weak inhibition at pH 8.5, strong inhibition at pH 10.0
AlCl3
-
increase in sensitivity to aluminium as pH decreases, inhibitory effect is predominant below pH 7.0, no effect above pH 8.5. Completely inactivated enzyme contains 2 mol of aluminum per mol of subunit. Citrate, NaF, N-(2-hydroxyethyl) ethylenediaminetriacetic acid or EDTA efficiently protects against inactivation. Citrate and NaF release aluminum from the completely inactivated aluminum-enzyme complex and fully recover enzyme activity. Binding of aluminum induces a decrease in alpha helices and beta sheets and an increase in random coil
alpha-Ketoglutarate oxime
-
-
alpha-Monofluoroglutarate
-
-
Aminooxyacetate
-
5 mM, weak inhibition of isozymes 1-3
AMP
-
inhibits only NADPH-linked activity
Chloroquine
-
potent inhibitor of isozymes GDH1 and GDH2 at a dose-dependent manner, the inhibitory effect of chloroquine on GDH2 is abolished by the presence of ADP and L-leucine, whereas GTP does not change the sensitivity to chloroquine inhibition, shows a non-competitive inhibition against 2-oxoglutarate and an uncompetitive inhibition against NADH
citrate
-
10 mM, 60% inhibition of oxidative deamination
GDP
strong allosteric inhibitor of GDH1 leading to a 90% reduction of activity. Addition of increasing concentrations of pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm) leads to an increasing protection from GDP inhibition
histidine
-
weak inhibition at pH 8.5, strong inhibition at pH 10.0
KCN
-
50 mM, strong inhibition of isozymes 1-3
L-aspartate
-
inhibition of NADPH linked reaction, activation of NAD(H) linked reaction
lysine
-
weak inhibition at pH 8.5, strong inhibition at pH 10.0
malate
-
5 mM, complete inhibition of NADH-linked activity
Methylacetimidate
-
100 mM, moderate inhibition of isozymes 1-3
methylglyoxal
with 1 mM methylglyoxal, GDH activity significantly decreases at 30 min of incubation, and markedly drops by 37% within 5 h compared to control
Mg2+
at 1.0-2.0 mM; at 1.0-2.0 mM
N-(N'-acetyl-4-sulfamoylphenyl)maleimide
-
-
Ni2+
-
1 mM, moderate inhibition of isozymes 1-3
o-phenanthroline
-
5 mM, strong inhibition of isozymes 1-3
o-phthalaldehyde
-
0.1 mM, 98% inhibition after 5 min at 60°C, competitive vs. 2-oxoglutarate and NADH
oxalylglycine
-
competitive vs. 2-oxoglutarate, uncompetitive vs. NADPH, noncompetitive vs. NH4+
p-chloromercuribenzoic acid
-
progressive decrease in enzyme activity of both isoenzymes, inhibition is not affected by addition of GTP or ADP
p-hydroxymercuribenzoate
-
5 mM, moderate inhibition of isozymes 1-3
Phenylglyoxal
-
4 mM, 75% inhibition, uncompetitive vs. 2-oxoglutarate, noncompetitive vs. NADH
phosphate
-
pH 8.0-9.0: activation, pH 6.0-7.6: almost complete inhibition with 400 mM
phosphatidylserine
-
assumed to be a simple non-competitive inhibition
pyridoxal
-
NADH and NADPH protect from inactivation
Sodium acetate
-
at 5°C only
sodium dodecylsulfate
-
time-dependent irreversible inhibition, 0.2 mM, 37% inhibition, 0.15 mM, 50% inhibition after 30 min, in the presence of 2-oxoglutarate after 370 min
succinate
-
5 mM, complete inhibition of NADH-linked activity
Zn2+
-
1 mM, strong inhibition of isozymes 1-3
2-oxoglutarate
-
-
ADP
-
-
ADP
-
above pH 7.0: allosteric activation, pH 6.0-7.0: strong inhibition
ATP
-
-
ATP
-
strong inhibition at 37°C, no inhibition at 5°C
ATP
-
wild-type: inhibition at 0.1 mM and between 0.5-1.0 mM and above, activation at 1 mM, H454Y and S448P mutant enzyme: activation between 0.1-1 mM, inhibition above, R463A mutant enzyme: progressive inhibition between 0.01 and 10 mM
ATP
-
1 mM, 65% inhibition of NADH reaction due to chelating properties of ATP
ATP
-
membrane-bound enzyme form, inhibition of microtubule-binding activity
ATP
-
strong inhibition at 37°C, no inhibition at 5°C
D-glutamate
-
10 mM, 57% inhibition of NADP+-linked activity, 30% inhibition of NADPH-linked activity
D-glutamate
-
2 mM, 11% inhibition, 6 mM, 34% inhibition
diethylstilbestrol
-
-
EDTA
-
5 mM, 80-90% inhibition of isozymes 1-3
EDTA
-
complete loss of NADH and NAD+ activities, NADPH activity unaffected
fumarate
-
-
glutamate
-
weak inhibition at pH 8.5, strong inhibition at pH 10.0
Glutarate
-
-
Glutarate
-
shows no affinity for N6-linked NAD+ but is biospecifically adsorbed to S6-linked NAD+ derivatives in the presence of its soluble kinetic-based enzyme capture ligand glutarate
Glyoxal
-
-
Glyoxal
67% inhibition at 1 mM
GTP
-
-
GTP
-
inhibition at pH 9.0, activation in presence of electrolytes at pH 6.0
GTP
-
0.06 mM, 95% inhibition
GTP
-
GTP inhibition is attenuated to some extent by the proteolysis with TLCK-treated chymotrypsin
GTP
-
allosteric regulation, low inhibition of the deamination reaction and strong inhibition of the amination reaction
GTP
-
little inhibition of H454Y mutant enzyme
GTP
inhibition of wild-type enzyme and mutant enzymes r470H and N498S. No inhibition of mutant enzyme G456A. IC50 of wild-type enzyme is 0.00019 mM, IC50 of mutant enzyme G456A is 0.0028 mM, IC50 of mutant enzyme R470G is 0.00017 mM, IC50 of mutant enzyme N498S is 0.0002 mM
GTP
-
inhibits wild-type enzyme and mutant enzyme E279G
GTP
-
IC50 for wild-type GLUD1: 0.0122 mM, IC50 for mutant enzyme R443S: 0.0162 mM, IC50 for mutant enzyme M415L: 0.0147 mM, IC50 for mutant enzyme M370L: 0.0113 mM, IC50 for mutant enzyme S331T: 0.0108 mM
GTP
potent inhibitor. IC50 for wild-type enzyme is 0.00019 mM, IC50 for mutant enzyme G456A is 0.0028 mM. ADP renders the GLUD1-derived enzyme less sensitive to GTP inhibition; totally insensitive to, it becomes amenable to GTP inhibition in presence of ADP
GTP
-
inhibits isozyme GDH1
GTP
-
efective inhibitor: activity below 10% of its full activity; GDH2 is resistent to GTP inhibition
GTP
negative allosteric regulator
GTP
-
1 mM, 42% inhibition due to chelating properties of GTP
GTP
8.23% activity in the presence of 0.01 mM ATP
GTP
-
membrane-bound liver enzyme, complete inhibition
GTP
-
allosteric regulation, low inhibition of the deamination reaction and strong inhibition of the amination reaction
GTP
-
strong inhibition at 37°C, weak inhibition at 5°C
isophthalate
-
-
isophthalate
-
competitive vs. glutamate
L-glutamate
-
-
L-glutamate
a competitive inhibitor against GDH
NaCl
-
100 mM, 50% inhibition of NADH and NAD+ dependent reactions
NAD+
-
incubation with 0.1 mM for 60 min inhibits hGDH1 and hGDH2 by 75% and 70%, respectively, incubations for longer time periods up to 3 h, does not further increase the inhibition of hGDH isoenzymes, ADP-ribosylated hDGH isozymes are reactivated by Mg2+-dependent mitochondrial ADP-ribosylcysteine hydrolase
NADH
modeling of the NADH/ADP site for allosteric effects induced at a single site of binding inhibitor NADH versus activator ADP to GDH. ADP shows dissimilar binding conformations at each NADH/ADP site in the GDH trimer, while NADH shows similar inhibitory binding conformations at each NADH/ADP site
NADH
allosteric enzyme regulation
NADH
-
high concentration
oxaloacetate
-
5 mM, 79% inhibition of oxidative deamination
oxaloacetate
-
5 mM, 20-25% inhibition of NADH- and NAD+-dependent activities
palmitoyl-CoA
-
-
palmitoyl-CoA
-
concentration-dependent inhibition, GDH1 is less sensitive to palmitoyl-CoA inhibition than GDH2
pyridoxal 5'-phosphate
-
5 mM, 100% inhibition
pyridoxal 5'-phosphate
dogfish
-
NAD+ and NADP+ protect from inactivation in the presence of sodium glutarate
pyridoxal 5'-phosphate
-
2 mM, complete loss of activity
pyridoxal 5'-phosphate
-
0.11 mM, approx. 30% inactivation after 10 min, 0.78 mM, 80% inactivation, inactivation is completely reversed by dialysis
additional information
-
complex inhibition pattern for ATP, GTP, NaCl, KCl, sodium acetate, NaI, and potassium nitrate of forward and reverse reaction at 5°C and 37°C
-
additional information
-
GDH2 is resistant to GTP inhibition
-
additional information
the isozyme hGDH2 is resistant against GTP inhibition
-
additional information
the isozyme hGDH2 is resistant against GTP inhibition
-
additional information
-
the isozyme hGDH2 is resistant against GTP inhibition
-
additional information
-
no inhibition or activation in the presence of ADP, GTP and leucine
-
additional information
-
complex inhibition pattern for ATP, GTP, NaCl, KCl, sodium acetate, NaI, and potassium nitrate of forward and reverse reaction at 5°C and 37°C
-
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2-mercaptoethanol
-
2fold activation
8-azidoguanosine 5'-diphosphate
-
used for affinity photolabeling
APRTh
TTC1249 (APRTh), a 23-30 kDa protein, which is annotated as adenine phosphoribosyltransferase but lacks the enzymatic activity, forms a ternary complex with the enzyme heterodimer, heterocomplex formation and structure, interaction analysis and function, detailed overview. APRTh mediates the allosteric activation of GDH by AMP
-
chymotrypsin
-
0.2 mg/ml chymotrypsin cleaves glutamate dehydrogenase in such a fashion as to cause a rise in activity with NADP+ and NAD+ as coenzyme, over threefold activation in the NADP+ assay with TLCK-treated chymotrypsin, the distinguishing aspect with untreated chymotrypsin is that the activation is followed by a decrease in activity
-
glutathione
-
2fold activation
KCl
-
activates at 5°C and 37°C
L-aspartate
-
2fold activation of glutamate synthesis
L-His
-
activates in presence of 3 M NaCl, 3 M Kcl or in absence of salts
N6-(2-aminoethyl)-NAD+
-
-
N6-(2-aminoethyl)-NADP+
-
-
N6-(2-Hydroxy-3-trimethylammonium propyl)-NAD+
-
-
N6-(3-sulfonatopropyl)-NAD+
-
-
NaCl
-
activates at 37°C only
phosphate
-
activator at pH 8.0-9.0, inhibitor at pH 6.0-7.6
PMP-BCATm
pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm) accelerates the oxidative deamination reaction of GDH1in the presence of branched-chain amino acids (Leu, Ile, Val). Reductive amination reaction is not affected
-
Poly(ethylene glycol)-N6-(2-aminoethyl)-NAD+
-
-
-
Poly(ethylene glycol)-N6-(2-aminoethyl)-NADP+
-
-
-
Trypsin
-
limited trypsin proteolyis activates the purified enzyme 8fold if the peptide is absent from the assay mixture, the native enzyme is 3fold activated if the cleaved peptide is present, activation may therefore be induced by loss of the peptide from the subunit of the native enzyme
-
ADP
-
-
ADP
-
above pH 7.0: allosteric activation
ADP
-
pH 6.0-7.0: strong inhibition
ADP
-
activation only if concentrations of both NAD(P)+ and substrate are high
ADP
-
1.5fold activation, 0.08 mM NADH as cofactor
ADP
-
increases the activity up to 2.3fold
ADP
-
ADP activation is almost abolished after treatment with TLCK-treated chymotrypsin
ADP
-
allosteric activator, addition of ADP or leucine to the single cofactor assay results in a marked activation of NADPH oxidation, about 1100% activation by ADP. Relative activation by ADP of GDH-catalyzed NAD+reduction is 36%, compared with 198% for NADP+ reduction
ADP
modeling of the NADH/ADP site for allosteric effects induced at a single site of binding inhibitor NADH versus activator ADP to GDH. ADP shows dissimilar binding conformations at each NADH/ADP site in the GDH trimer, while NADH shows similar inhibitory binding conformations at each NADH/ADP site
ADP
-
allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
ADP
-
no activation of R463A mutant enzyme
ADP
-
0.1-1.0 mM, activates wild-type enzyme and mutant enzyme E279G
ADP
-
1 mM, pH 8.0, 3fold activation of wild-type enzyme, no significant actication of Tyr187 mutant enzymes
ADP
in absence of GTP the isoenzyme GLUD2 assumes a conformational state associated with little catalytic activity, it remains amenable to full activation by ADP and/or L-Leu
ADP
-
ADP displays a lower affinity for hGDH2 than for hGDH1
ADP
positive allosteric regulator
ADP
activation is markedly diminished at lower pH values
ADP
ADP is an activator of hGDH1 and hGDH2 which binds only to the open state
ADP
ADP is an activator of hGDH1 and hGDH2 which binds only to the open state. hGDH1mutant R443S/G456A exhibits a reduced ADP sensitivity compared both to hGDH1 and to hGDH2. The addition of the M415L and R470H mutations results in an even more pronounced drop in ADP affinity
ADP
the addition of FLAG tag to the C-terminus of GDH leaves the recombinant protein fivefold less sensitive to ADP activation
ADP
120.88% activity in the presence of 0.25 mM ATP
ADP
ADP induces an allosteric conformational change in GDH1, leading to a 2fold enhanced oxidative deamination
ADP
-
activates in presence of 3 M NaCl or 3 M KCl or in absence of salts
ADP
-
1 mM, approx. 2fold activation of membrane-bound liver enzyme
ADP
-
allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
AMP
-
-
AMP
-
activates NADH-linked glutamate synthesis, inhibits NADPH-linked activity
AMP
-
activation only in biosynthetic direction
AMP
-
1 mM, reaction velocity increases 15fold at saturating NAD+ and glutamate levels
AMP
AMP activated GDH activity of the ternary complex, but not the GdhA-GdhB binary complex. APRTh mediates the allosteric activation of GDH by AMP. Reductive amination and oxidative deamination activity is enhanced by up to 6.3 and 2.5fold, respectively, by the addition of 1 mM AMP.
ATP
-
-
ATP
-
4.8fold activation, cofactor 0.08 mM NADH
ATP
-
allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
ATP
-
wild-type: activation at 1 mM, inhibition below and above, H454Y and S448P mutant enzymes: progressive increase in activity until 10 mM, inhibition above
ATP
-
activates in presence of 3 M NaCl or in absence of salts, slight inhibition in presence of 3 M KCl
ATP
-
approx. 1.5fold activation of membrane-bound liver enzyme
ATP
-
allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
GTP
-
inhibition at pH 9.0, activation in presence of electrolytes at pH 6.0
L-Leu
0.3-10 mM stimulates isoenzyme GLUD2 to a greater extent than isoenzyme GLUD1
L-Leu
0.3-10 mM stimulates isoenzyme GLUD2 to a greater extent than isoenzyme GLUD1. In absence of GTP the isoenzyme GLUD2 assumes a conformational state associated with little catalytic activity, it remains amenable to full activation by ADP and/or L-Leu
L-Leu
-
activates in presence of 3 M NaCl, 3 M Kcl or in absence of salts
L-leucine
-
allosteric activator, addition of ADP or leucine to the single cofactor assay results in a marked activation of NADPH oxidation, about 725% activation by L-leucine, respectively. Activation of NAD+ and NADP+ reduction by 40% and 135%, respectively
L-leucine
-
L-leucine displays the same affinity for hGDH2 and hGDH1
L-leucine
the crystal structure of GdhA/GdhB in a complex with leucine and biochemical analysis reveals that leucine is bound to the pockets at the GdhA-GdhA, GdhA-GdhB, and GdhB-GdhB interfaces. leucine binding increases the turnover of the GDH reaction, possibly through acceleration of the open-close cycle of the active-site cleft between the catalytic domain and NAD-binding domains
leucine
-
wild-type, S448P, H454Y and R463A mutant enzymes
leucine
-
the enzyme is subject to allosteric activation by leucine invlving ARg134, and Asp185, structural mechanism, overview
leucine
with 10 mM the activity increases by 1.55fold after 240 min and by 1.24fold when the enzyme is preincubated with methylglyoxal
leucine
enhances the oxidative deamination reaction of GDH1
leucine
-
the enzyme is subject to allosteric activation by leucine, structural mechanism, overview
leucine
-
activates at 5°C only
additional information
-
not inhibited by trypsin
-
additional information
-
serum GLDH activity is elevated in alcohol abuse
-
additional information
in reductive amination, the influence of AMP and leucine on the Km for NADH, 2-oxoglutarate, and ammonium is not large, although approximately 4.5, 5.3, and 10.2fold increases in Km for 2-OG are observed with AMP, leucine, and the copresence of AMP and leucine, respectively. Activation profiles of GDH activity of the TtGDH-APRTh complex by leucine and AMP, overview
-
additional information
-
in reductive amination, the influence of AMP and leucine on the Km for NADH, 2-oxoglutarate, and ammonium is not large, although approximately 4.5, 5.3, and 10.2fold increases in Km for 2-OG are observed with AMP, leucine, and the copresence of AMP and leucine, respectively. Activation profiles of GDH activity of the TtGDH-APRTh complex by leucine and AMP, overview
-
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0.0051 - 14
2-oxoglutarate
0.00294
alpha-ketoglutarate
-
-
0.291
N6-(2-aminoethyl)-NAD+
-
-
0.273
N6-(2-aminoethyl)-NADP+
-
-
0.148
N6-(2-hydroxy-3-trimethylammoniumpropyl)-NAD+
-
-
0.052
N6-(3-sulfonatopropyl)-NAD+
-
-
0.444
poly(ethyleneglycol)-N6-(2-aminoethyl)-NAD+
-
-
-
0.425
poly(ethyleneglycol)-N6-(2-aminoethyl)-NADP+
-
-
-
additional information
additional information
-
0.0051
2-oxoglutarate
recombinant enzyme complex TtGDH-APRTh, pH and temperature not specified in the publication
0.0229
2-oxoglutarate
recombinant enzyme complex TtGDH-APRTh, with AMP, pH and temperature not specified in the publication
0.027
2-oxoglutarate
recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication
0.052
2-oxoglutarate
recombinant enzyme complex TtGDH-APRTh, with L-leucine and AMP, pH and temperature not specified in the publication
0.1
2-oxoglutarate
-
euthermic animal, assay at 37°C
0.14
2-oxoglutarate
-
NADP-linked reductive amination
0.18
2-oxoglutarate
-
reductive amination, low-activity form of the enzyme
0.2
2-oxoglutarate
-
cosubstrate NADPH
0.2
2-oxoglutarate
-
reductive amination, high-activity form of the enzyme
0.2
2-oxoglutarate
pH 7.6, 70°C, recombinent enzyme (unheated)
0.25
2-oxoglutarate
-
NADPH-dependent activity
0.25
2-oxoglutarate
-
concentration range: 0.3-4.0 mM
0.25
2-oxoglutarate
pH 7.6, 70°C, native enzyme
0.3
2-oxoglutarate
pH 7.6, 70°C, recombinent enzyme (heated)
0.36
2-oxoglutarate
-
NADH + NH4Cl
0.36
2-oxoglutarate
-
isozyme 1, amination activity, cofactor NADH
0.4
2-oxoglutarate
-
50 mM Tris-HCl, pH 7.2
0.43
2-oxoglutarate
-
hibernating animal, assay at 5°C
0.47
2-oxoglutarate
-
NADPH + NH4Cl
0.53
2-oxoglutarate
-
pH 7.6, 90°C
0.59
2-oxoglutarate
-
isozyme 3, amination activity, cofactor NADH
0.6
2-oxoglutarate
-
cosubstrate NADH
0.62
2-oxoglutarate
-
glutamate dehydrogenase 2, 0.1 mM NADH
0.63
2-oxoglutarate
-
NADPH-dependent amination
0.64
2-oxoglutarate
-
NADPH-dependent amination
0.7
2-oxoglutarate
-
cofactor NADH
0.7
2-oxoglutarate
-
NADPH-dependent amination
0.98
2-oxoglutarate
-
hibernating animal, assay at 37°C
1
2-oxoglutarate
-
liver enzyme
1.1
2-oxoglutarate
-
glutamate dehydrogenase 2, 80 mM NH4+
1.16
2-oxoglutarate
-
mutant C274G, hGDH1
1.2
2-oxoglutarate
-
500 mM Tris-HCl, pH 7.2
1.23
2-oxoglutarate
-
isozyme 2, amination activity, cofactor NADH
1.25
2-oxoglutarate
-
25°C, wild-type enzyme
1.25
2-oxoglutarate
-
pH 8.0, 25°C, wild-type enzyme
1.25
2-oxoglutarate
-
pH 8.0, 25°C, wild-type enzyme hGDH1
1.25
2-oxoglutarate
-
hGDH1, wild-type
1.25
2-oxoglutarate
-
wild-type, hGDH1
1.25
2-oxoglutarate
-
isozyme GDH1, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
1.25
2-oxoglutarate
-
wild type isozyme GDH1, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
1.27
2-oxoglutarate
-
mutant enzyme L415M/S443R/A456G, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
1.29
2-oxoglutarate
-
25°C, mutant enzyme K333L
1.29
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme Y187E
1.29
2-oxoglutarate
-
mutant enzyme M415L/R443S/G456A, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
1.31
2-oxoglutarate
-
25°C, mutant enzyme K344L
1.31
2-oxoglutarate
-
25°C, mutant enzyme K346L
1.31
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme Y187M
1.34
2-oxoglutarate
-
hGDH1, mutant C323L
1.34
2-oxoglutarate
-
mutant C59G, hGDH1
1.36
2-oxoglutarate
-
hGDH1, mutant C323Y
1.36
2-oxoglutarate
-
mutant C59Y, hGDH1
1.37
2-oxoglutarate
-
mutant C274Y, hGDH1
1.38
2-oxoglutarate
-
hGDH1, mutant C323M
1.39
2-oxoglutarate
-
pH 8.0, 25°C, wild-type enzyme hGDH2
1.39
2-oxoglutarate
-
hGDH1, mutant C323R
1.39
2-oxoglutarate
-
hGDH2, wild-type
1.39
2-oxoglutarate
-
wild-type, hGDH2
1.39
2-oxoglutarate
-
isozyme GDH1, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
1.39
2-oxoglutarate
-
wild type isozyme GDH2, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
1.4
2-oxoglutarate
-
assay at 37°C
1.4
2-oxoglutarate
-
pH 7.6, 60°C
1.4
2-oxoglutarate
-
hGDH1, mutant C323G
1.4
2-oxoglutarate
-
mutant C274A, hGDH1
1.4
2-oxoglutarate
-
mutant C59A, hGDH1
1.41
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme S443R hGDH2
1.41
2-oxoglutarate
-
hGDH2, mutant C323Y
1.44
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme Y187R
1.45
2-oxoglutarate
-
25°C, mutant enzyme K337L
1.45
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme Y187G
1.45
2-oxoglutarate
-
hGDH2, mutant C323L
1.45
2-oxoglutarate
-
hGDH2, mutant C323M
1.46
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme Y187S
1.47
2-oxoglutarate
-
25°C, mutant enzyme S445L
1.5
2-oxoglutarate
-
25°C, mutant enzyme G446D
1.5
2-oxoglutarate
-
hGDH2, mutant C323R
1.5
2-oxoglutarate
-
mutant enzyme R443S/G456A, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
1.5 - 2
2-oxoglutarate
-
hGDH2, mutant C323G
1.51
2-oxoglutarate
-
glutamate dehydrogenase 1, 400 mM NH4+
1.51
2-oxoglutarate
-
glutamate dehydrogenase 1, 0.1 mM NADH
1.54
2-oxoglutarate
-
isozyme 1, amination activity, cofactor NADPH
1.58
2-oxoglutarate
-
mutant C274G, hGDH2
1.58
2-oxoglutarate
-
mutant C59Y, hGDH2
1.59
2-oxoglutarate
-
mutant C274A, hGDH2
1.61
2-oxoglutarate
-
mutant C59A, hGDH2
1.66
2-oxoglutarate
-
mutant C274Y, hGDH2
1.67
2-oxoglutarate
-
mutant C59G, hGDH2
1.73
2-oxoglutarate
-
isozyme 3, amination activity, cofactor NADH
1.85
2-oxoglutarate
-
isozyme 2, amination activity, cofactor NADPH
1.86
2-oxoglutarate
-
mutant C119Y, hGDH1
1.9
2-oxoglutarate
-
mutant C119A, hGDH1
1.94
2-oxoglutarate
-
mutant C119G, hGDH1
2
2-oxoglutarate
-
wild type isozyme GDH1, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
2.1
2-oxoglutarate
-
cosubstrate NADPH
2.1
2-oxoglutarate
-
glutamate dehydrogenase 1, 40 mM NH4+
2.1
2-oxoglutarate
-
wild type isozyme GDH2, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
2.12
2-oxoglutarate
-
mutant C119A, hGDH2
2.18
2-oxoglutarate
-
mutant C119G, hGDH2
2.26
2-oxoglutarate
-
mutant C119Y, hGDH2
2.3
2-oxoglutarate
-
kidney enzyme
2.6
2-oxoglutarate
-
glutamate dehydrogenase 1, 0.2 mM NADPH
3.13
2-oxoglutarate
-
25°C, mutant enzyme H454Y
3.3
2-oxoglutarate
-
cosubstrate NADH
3.5
2-oxoglutarate
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
3.66
2-oxoglutarate
-
euthermic animal, assay at 5°C
3.7
2-oxoglutarate
-
glutamate dehydrogenase 1, 0.2 mM NADH
3.7
2-oxoglutarate
-
glutamate dehydrogenase 2, 0.2 mM NADPH
4
2-oxoglutarate
-
cofactor NADPH
4.5
2-oxoglutarate
-
cofactor NADH
5
2-oxoglutarate
-
NADH-dependent activity
6.3
2-oxoglutarate
-
cofactor NADPH
7.1
2-oxoglutarate
-
pH 8.0
7.1
2-oxoglutarate
-
NAD-linked reductive amination
10.5
2-oxoglutarate
-
assay at 5°C
14
2-oxoglutarate
-
500 mM Tris-HCl, pH 8.2
0.25
glutamate
-
hibernating animal, assay at 5°C
0.32
glutamate
-
concentration range: 0.05-1.0 mM
0.47
glutamate
-
assay at 5°C
0.5
glutamate
-
euthermic animal, assay at 5°C
2.03
glutamate
-
euthermic animal, assay at 37°C
2.6
glutamate
-
assay at 37°C
4.61
glutamate
-
mitochondrial enzyme, cofactor NAD+
5.2
glutamate
-
hibernating animal, assay at 37°C
5.5
glutamate
-
concentration range: 1.0-10.0 mM
5.93
glutamate
-
enzyme from rough ER, cofactor NAD+
12
glutamate
-
cosubstrate NAD+
20.7
glutamate
-
mitochondrial enzyme, cofactor NADP+
23.8
glutamate
-
enzyme from rough ER, cofactor NADP+
0.24
L-glutamate
-
at pH 8.5
0.27
L-glutamate
recombinant enzyme complex TtGDH-APRTh, low Glu concentration, with AMP, pH and temperature not specified in the publication
0.3
L-glutamate
-
cosubstrate NAD+
0.3
L-glutamate
-
pH 8.0, 70°C
0.4
L-glutamate
-
kidney enzyme
0.45
L-glutamate
recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication
0.6
L-glutamate
-
pH 7.6, 90°C
0.64
L-glutamate
-
isozyme 1, deamination activity
0.77
L-glutamate
recombinant enzyme complex TtGDH-APRTh, with L-leucine and AMP, pH and temperature not specified in the publication
1
L-glutamate
-
1 mM, NAD+
1.01
L-glutamate
-
at pH 7.4
1.1
L-glutamate
-
cosubstrate NADP+
1.2
L-glutamate
recombinant enzyme complex TtGDH-APRTh, low Glu concentration, pH and temperature not specified in the publication
1.6
L-glutamate
-
cofactor NADP+
1.66
L-glutamate
-
cofactor NAD+
1.7
L-glutamate
-
50 mM Tris-HCl, pH 7.2
1.77
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2D172Y
1.81
L-glutamate
-
pH 9.5, 25°C, wild-type enzyme hGDH2
2.4
L-glutamate
-
NADP-linked oxidative deamination
2.5
L-glutamate
-
pH 7.6, 60°C
2.98
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K130Y
3
L-glutamate
-
1 mM, NADP+
3
L-glutamate
-
isozyme 3, deamination activity
3
L-glutamate
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
3.44
L-glutamate
-
pH 9.5, 25°C, wild-type enzyme
3.44
L-glutamate
-
pH 9.5, 25°C, wild-type enzyme hGDH1
3.52
L-glutamate
-
isozyme 2, deamination activity
3.65
L-glutamate
-
oxidative deamination, low-activity form of the enzyme
3.71
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1D172Y
3.76
L-glutamate
-
pH 9.5, 25°C, mutant enzyme E279M
3.83
L-glutamate
-
oxidative deamination, high-activity form of the enzyme
3.94
L-glutamate
-
pH 9.5, 25°C, mutant enzyme E279Y
3.98
L-glutamate
-
pH 9.5, 25°C, mutant enzyme E279G
4.05
L-glutamate
-
pH 9.5, 25°C, mutant enzyme E279L
4.12
L-glutamate
-
pH 9.5, 25°C, mutant enzyme E279R
5.51
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K130Y
7.3
L-glutamate
-
NAD-linked oxidative deamination
7.99
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K94Y
10
L-glutamate
-
NADP+-dependent activity
10.41
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K118Y
10.7
L-glutamate
-
wild type isozyme GDH2, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
10.8
L-glutamate
-
mutant enzyme R443S/G456A, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
12.4
L-glutamate
-
wild type isozyme GDH1, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
17.75
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2G96Y
19
L-glutamate
recombinant enzyme complex TtGDH-APRTh, high Glu concentration, with AMP, pH and temperature not specified in the publication
19.5
L-glutamate
-
500 mM Tris-HCl, pH 9.4
21.82
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K94Y
25
L-glutamate
-
0.004 mM, NAD+
25.82
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K118Y
30.55
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1G96Y
31
L-glutamate
-
500 mM Tris-HCl, pH 7.2
52
L-glutamate
recombinant enzyme complex TtGDH-APRTh, high Glu concentration, pH and temperature not specified in the publication
0.014
NAD+
-
-
0.016
NAD+
-
50 mM Tris-HCl, pH 7.2
0.02
NAD+
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
0.024
NAD+
recombinant enzyme complex TtGDH-APRTh, pH and temperature not specified in the publication
0.032
NAD+
-
kidney enzyme
0.056
NAD+
recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication
0.063
NAD+
-
+ L-glutamate
0.1
NAD+
-
pH 8.0, 25°C, recombinant enzyme
0.11
NAD+
-
500 mM Tris-HCl, pH 9.4
0.11
NAD+
-
pH 8.0, 25°C, native enzyme
0.13
NAD+
recombinant enzyme complex TtGDH-APRTh, with AMP, pH and temperature not specified in the publication
0.15
NAD+
-
500 mM Tris-HCl, pH 7.2
0.16
NAD+
recombinant enzyme complex TtGDH-APRTh, with L-leucine and AMP, pH and temperature not specified in the publication
0.2
NAD+
-
isozyme 1, deamination activity
0.26
NAD+
-
isozyme 2, deamination activity
0.32
NAD+
-
isozyme 3, deamination activity
0.364
NAD+
-
mitochondrial enzyme
0.43
NAD+
-
oxidative deamination, low-activity form of the enzyme
0.53
NAD+
-
substrate L-glutamate
0.55
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K94Y
0.58
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2G96Y
0.59
NAD+
-
pH 9.5, 25°C, wild-type enzyme hGDH2
0.63
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2D172Y
0.65
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1G96Y
0.71
NAD+
-
pH 9.5, 25°C, wild-type enzyme
0.71
NAD+
-
pH 9.5, 25°C, wild-type enzyme hGDH1
0.75
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K130Y
0.76
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1D172Y
0.79
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K94Y
0.82
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K118Y
0.92
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K130Y
0.924
NAD+
-
enzyme from rough ER
0.94
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K118Y
2.44
NAD+
-
oxidative deamination, high-activity form of the enzyme
3
NAD+
-
NAD-linked oxidative deamination
6.94
NAD+
-
pH 9.5, 25°C, mutant enzyme E279G
7.6
NAD+
-
pH 9.5, 25°C, mutant enzyme E279R
8.35
NAD+
-
pH 9.5, 25°C, mutant enzyme E279Y
9.98
NAD+
-
pH 9.5, 25°C, mutant enzyme E279M
10.01
NAD+
-
pH 9.5, 25°C, mutant enzyme E279L
0.000175
NADH
-
-
0.003
NADH
recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication
0.004
NADH
-
50 mM Tris-HCl, pH 7.2
0.0053
NADH
recombinant enzyme complex TtGDH-APRTh, with L-leucine and AMP, pH and temperature not specified in the publication
0.0058
NADH
recombinant enzyme complex TtGDH-APRTh, with AMP, pH and temperature not specified in the publication
0.007
NADH
-
+ 2-oxoglutarate
0.008
NADH
recombinant enzyme complex TtGDH-APRTh, pH and temperature not specified in the publication
0.009
NADH
-
glutamate dehydrogenase 1, 5 mM 2-oxoglutarate
0.009
NADH
-
glutamate dehydrogenase 2, 5 mM 2-oxoglutarate
0.01
NADH
-
500 mM Tris-HCl, pH 8.2
0.012
NADH
-
glutamate dehydrogenase 2, 80 mM NH4+
0.012
NADH
-
500 mM Tris-HCl, pH 7.2
0.015
NADH
-
liver enzyme
0.02
NADH
-
glutamate dehydrogenase 1, 40 mM NH4+
0.022
NADH
-
kidney enzyme
0.04
NADH
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
0.048
NADH
-
glutamate dehydrogenase 1, 400 mM NH4+
0.05
NADH
-
glutamate dehydrogenase 1, 12.5 mM 2-oxoglutarate
0.07
NADH
-
isozyme 1, amination activity, cofactor NADH
0.075
NADH
-
mutant enzyme L415M/S443R/A456G, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
0.076
NADH
-
25°C, mutant enzyme K346L
0.079
NADH
-
25°C, mutant enzyme K333L
0.08
NADH
-
pH 8.0, 25°C, wild-type enzyme
0.08
NADH
-
mutant enzyme M415L/R443S/G456A, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
0.081
NADH
-
25°C, wild-type enzyme
0.081
NADH
-
pH 8.0, 25°C, wild-type enzyme hGDH1
0.081
NADH
-
hGDH1, wild-type
0.081
NADH
-
wild-type, hGDH1
0.081
NADH
-
isozyme GDH1, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
0.081
NADH
-
wild type isozyme GDH1, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
0.082
NADH
-
pH 8.0, 25°C, mutant enzyme Y187E
0.082
NADH
-
pH 8.0, 25°C, mutant enzyme Y187R
0.083
NADH
-
pH 7.6, 90°C
0.084
NADH
-
pH 8.0, 25°C, mutant enzyme Y187M
0.085
NADH
-
pH 8.0, 25°C, mutant enzyme Y187G
0.086
NADH
-
pH 8.0, 25°C, wild-type enzyme hGDH2
0.086
NADH
-
hGDH2, wild-type
0.086
NADH
-
wild-type, hGDH2
0.086
NADH
-
isozyme GDH2, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
0.086
NADH
-
wild type isozyme GDH2, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
0.088
NADH
-
25°C, mutant enzyme K337L
0.088
NADH
-
pH 8.0, 25°C, mutant enzyme S443R hGDH2
0.088
NADH
-
pH 8.0, 25°C, mutant enzyme Y187S
0.089
NADH
-
25°C, mutant enzyme G446D
0.09
NADH
-
isozyme 3, amination activity, cofactor NADH
0.09
NADH
-
concentration range: 0.04-0.1 mM
0.09
NADH
-
25°C, mutant enzyme K344L
0.09
NADH
-
mutant C119A, hGDH1
0.091
NADH
-
mutant C119Y, hGDH1
0.092
NADH
-
mutant C119G, hGDH1
0.094
NADH
-
mutant C59G, hGDH1
0.097
NADH
-
mutant C59A, hGDH1
0.098
NADH
-
25°C, mutant enzyme S445L
0.098
NADH
-
mutant C119G, hGDH2
0.099
NADH
-
mutant C59A, hGDH2
0.099
NADH
-
mutant C59Y, hGDH1
0.101
NADH
-
mutant C119A, hGDH2
0.102
NADH
-
mutant C59Y, hGDH2
0.106
NADH
-
mutant C59G, hGDH2
0.108
NADH
-
mutant C119Y, hGDH2
0.117
NADH
-
hGDH1, mutant C323L
0.119
NADH
-
hGDH1, mutant C323G
0.119
NADH
-
hGDH1, mutant C323M
0.119
NADH
-
hGDH2, mutant C323M
0.121
NADH
-
hGDH2, mutant C323L
0.122
NADH
-
25°C, mutant enzyme H454Y
0.122
NADH
-
hGDH1, mutant C323R
0.125
NADH
-
hGDH2, mutant C323R
0.128
NADH
-
hGDH2, mutant C323G
0.129
NADH
-
hGDH1, mutant C323Y
0.13
NADH
-
reductive amination, low-activity form of the enzyme
0.138
NADH
-
hGDH2, mutant C323Y
0.14
NADH
-
isozyme 2, amination activity, cofactor NADH
0.169
NADH
-
mutant C274A, hGDH2
0.175
NADH
-
mutant C274G, hGDH2
0.176
NADH
-
mutant C274Y, hGDH2
0.178
NADH
-
mutant C274Y, hGDH1
0.181
NADH
-
mutant C274G, hGDH1
0.189
NADH
-
mutant C274A, hGDH1
0.2
NADH
-
NAD-linked reductive amination
0.5
NADH
-
NADH-dependent activity
0.52
NADH
-
reductive amination, high-activity form of the enzyme
0.98
NADH
-
substrate 2-oxoglutarate
0.004
NADP+
-
NADP+-dependent activity
0.013
NADP+
-
oxidative deamination, low-activity form of the enzyme
0.019
NADP+
-
NADP-linked oxidative deamination
0.025
NADP+
-
+ L-glutamate
0.025
NADP+
-
pH 7.6, 90°C
0.028
NADP+
-
cosubstrate glutamate
0.029
NADP+
-
oxidative deamination, high-activity form of the enzyme
0.035
NADP+
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
0.08
NADP+
-
concentration range: 0.02-0.2 mM
0.18
NADP+
-
substrate L-glutamate
0.31
NADP+
-
cosubstrate norvaline
0.443
NADP+
-
enzyme from rough ER
0.637
NADP+
-
mitochondrial enzyme
0.006
NADPH
-
NADPH-dependent amination
0.01
NADPH
-
+ 2-oxoglutarate
0.01
NADPH
-
pH 7.6, 60°C
0.011
NADPH
-
reductive amination, low-activity form of the enzyme
0.013
NADPH
-
NADPH-dependent activity
0.013
NADPH
-
NADP-linked reductive amination
0.013
NADPH
-
reductive amination, high-activity form of the enzyme
0.018
NADPH
-
NADPH-dependent amination
0.02
NADPH
-
NADPH-dependent amination
0.028
NADPH
-
glutamate dehydrogenase 1, 10 mM 2-oxoglutarate
0.028
NADPH
-
glutamate dehydrogenase 2, 10 mM 2-oxoglutarate
0.037
NADPH
-
pH 7.6, 90°C
0.04
NADPH
-
concentration range: 0.002-0.1 mM
0.04
NADPH
pH 7.6, 70°C, native enzyme
0.05
NADPH
pH 7.6, 70°C, recombinent enzyme (heated)
0.069
NADPH
-
glutamate dehydrogenase 1, 40 mM NH4+
0.069
NADPH
-
glutamate dehydrogenase 2, 80 mM NH4+
0.1
NADPH
pH 7.6, 70°C, recombinent enzyme (unheated)
0.17
NADPH
-
50 mM Tris-HCl, pH 7.2
0.27
NADPH
-
isozyme 1, amination activity, cofactor NADPH
0.46
NADPH
-
isozyme 3, amination activity, cofactor NADPH
0.54
NADPH
-
500 mM Tris-HCl, pH 7.2
0.56
NADPH
-
substrate 2-oxoglutarate
0.56
NADPH
-
substrate NH3
0.75
NADPH
-
500 mM Tris-HCl, pH 8.2
0.78
NADPH
-
isozyme 2, amination activity, cofactor NADPH
0.38
NH3
-
biphasic Lineweaver-Burk plot suggests 2 Km values
1.25
NH3
-
reductive amination, high-activity form of the enzyme
1.31
NH3
-
reductive amination, low-activity form of the enzyme
1.5
NH3
-
NADPH-dependent amination
1.7
NH3
-
NADP-linked reductive amination
2.4
NH3
-
NADPH-dependent amination
2.5
NH3
pH 7.6, 70°C, recombinent enzyme (unheated)
2.9
NH3
-
NADPH-dependent amination
4.9
NH3
-
NAD-linked reductive amination
5.1
NH3
-
NADP-linked reductive amination
10
NH3
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
11.4
NH3
pH 7.6, 70°C, recombinent enzyme (heated)
12.8
NH3
-
hGDH1, pH 8.0, temperature not specified in the publication
13
NH3
pH 7.6, 70°C, native enzyme
13.4
NH3
-
wild type isozyme GDH1, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
14.7
NH3
-
hGDH2, pH 8.0, temperature not specified in the publication
17.1
NH3
-
wild type isozyme GDH2, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
22.2
NH3
-
mutant enzyme R443S/G456A, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
29
NH3
recombinant enzyme complex TtGDH-APRTh, pH and temperature not specified in the publication
33
NH3
-
hGDH2, pH 7.5, temperature not specified in the publication
33
NH3
recombinant enzyme complex TtGDH-APRTh, with L-leucine and AMP, pH and temperature not specified in the publication
35
NH3
-
hGDH1, pH 7.5, temperature not specified in the publication
43
NH3
recombinant enzyme complex TtGDH-APRTh, with AMP, pH and temperature not specified in the publication
44
NH3
-
NADPH + 2-oxoglutarate
46
NH3
recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication
50
NH3
-
NADH + 2-oxoglutarate
57.5
NH3
-
hGDH1, pH 7.0, temperature not specified in the publication
62.2
NH3
-
hGDH2, pH 7.0, temperature not specified in the publication
66
NH3
-
NADH-dependent activity
100
NH3
-
biphasic Lineweaver-Burk plot suggests 2 Km values
0.0424
NH4+
-
-
1.3
NH4+
-
concentration range: 0.2-5 mM
5.8
NH4+
-
glutamate dehydrogenase 1, 0.2 mM NADPH
7
NH4+
-
glutamate dehydrogenase 1, 0.2 mM NADPH
7
NH4+
-
euthermic animal, assay at 37°C
10.4
NH4+
-
glutamate dehydrogenase 1, 10 mM 2-oxoglutarate
12.1
NH4+
-
hibernating animal, assay at 5°C
12.9
NH4+
-
glutamate dehydrogenase 2, 5 mM 2-oxoglutarate
13
NH4+
-
isozyme 2, amination activity, cofactor NADH
13
NH4+
-
concentration range: 10-200 mM
15
NH4+
-
cosubstrates NADPH + 2-oxoglutarate
15.8
NH4+
-
glutamate dehydrogenase 1, 5 mM 2-oxoglutarate
15.8
NH4+
-
hibernating animal, assay at 37°C
17.8
NH4+
-
assay at 37°C
19
NH4+
-
glutamate dehydrogenase 1, 10 mM 2-oxoglutarate
21.7
NH4+
-
glutamate dehydrogenase 1, 0.1 mM NADH
22.8
NH4+
-
glutamate dehydrogenase 1, 0.1 mM NADH
24.7
NH4+
-
euthermic animal, assay at 5°C
27
NH4+
-
cosubstrates NADH + 2-oxoglutarate
30
NH4+
-
isozyme 1, amination activity, cofactor NADH
36
NH4+
-
isozyme 1, amination activity, cofactor NADPH
41
NH4+
-
isozyme 3, amination activity, cofactor NADPH
44
NH4+
-
isozyme 3, amination activity, cofactor NADH
53
NH4+
-
isozyme 2, amination activity, cofactor NADPH
58
NH4+
-
500 mM Tris-HCl, pH 8.2
77
NH4+
-
500 mM Tris-HCl, pH 7.2
106
NH4+
-
glutamate dehydrogenase 1, 12.5 mM 2-oxoglutarate
115.1
NH4+
-
glutamate dehydrogenase 1, 0.2 mM NADH
160
NH4+
-
50 mM Tris-HCl, pH 7.2
additional information
additional information
-
-
-
additional information
additional information
-
Km-values for 2-oxoglutaratefor mutant enzyme R443S, recombinant wild-type enzyme and wild-type enzyme from human liver
-
additional information
additional information
kinetic analysis in wild-type and transgenic overexpressing brain cell fractions, overview
-
additional information
additional information
-
kinetic analysis in wild-type and transgenic overexpressing brain cell fractions, overview
-
additional information
additional information
-
lowering the pH of the buffer from pH 8.0 to pH 7.0 increases the Km for ammonia substantially, i.e. for hGDH1 from 12.8 mM to 57.5 mM, and for hGDH2: from 14.7 mM to 62.2 mM, thus essentially precluding reductive amination
-
additional information
additional information
when assayed in triethanolamine buffer, pH 8.0, at 1.0 mM ADP, hGDH1 and hGDH2 show similar catalytic properties (Vmax and Kms for 2-oxoglutarate, ammonia and glutamate), kinetics, overview
-
additional information
additional information
when assayed in triethanolamine buffer, pH 8.0, at 1.0 mM ADP, hGDH1 and hGDH2 show similar catalytic properties (Vmax and Kms for 2-oxoglutarate, ammonia and glutamate), kinetics, overview
-
additional information
additional information
-
when assayed in triethanolamine buffer, pH 8.0, at 1.0 mM ADP, hGDH1 and hGDH2 show similar catalytic properties (Vmax and Kms for 2-oxoglutarate, ammonia and glutamate), kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.23 - 510
2-oxoglutarate
0.23
2-oxoglutarate
recombinant enzyme complex TtGDH-APRTh, pH and temperature not specified in the publication
0.66
2-oxoglutarate
recombinant enzyme complex TtGDH-APRTh, with AMP, pH and temperature not specified in the publication
14
2-oxoglutarate
-
hGDH1, mutant C323Y
15
2-oxoglutarate
-
hGDH1, mutant C323R
15
2-oxoglutarate
recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication
17
2-oxoglutarate
-
hGDH1, mutant C323G
17
2-oxoglutarate
-
hGDH1, mutant C323L
17
2-oxoglutarate
-
hGDH2, mutant C323Y
19
2-oxoglutarate
-
hGDH1, mutant C323M
19
2-oxoglutarate
-
hGDH2, mutant C323M
19
2-oxoglutarate
-
hGDH2, mutant C323R
20
2-oxoglutarate
-
hGDH2, mutant C323L
21
2-oxoglutarate
-
hGDH2, mutant C323G
37
2-oxoglutarate
recombinant enzyme complex TtGDH-APRTh, with L-leucine and AMP, pH and temperature not specified in the publication
104
2-oxoglutarate
-
pH 8.0, 25°C, wild-type enzyme hGDH1
104
2-oxoglutarate
-
hGDH1, wild-type
130
2-oxoglutarate
-
pH 8.0, 25°C, wild-type enzyme hGDH2
130
2-oxoglutarate
-
hGDH2, wild-type
134
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme S443R hGDH2
165.3
2-oxoglutarate
-
pH 7.6, 90°C
183
2-oxoglutarate
-
cofactor NADH
195
2-oxoglutarate
-
concentration range: 0.3-4.0 mM
510
2-oxoglutarate
-
reduction
25
glutamate
-
oxidation
40
glutamate
-
concentration range: 0.05-1.0 mM
61
glutamate
-
cofactor NADP+
162
glutamate
-
concentration range: 1.0-10.0 mM
714
glutamate
-
cofactor NADH, + 1 mM ADP
0.27
L-glutamate
recombinant enzyme complex TtGDH-APRTh, low Glu concentration, pH and temperature not specified in the publication
1.2
L-glutamate
recombinant enzyme complex TtGDH-APRTh, low Glu concentration, with AMP, pH and temperature not specified in the publication
1.5
L-glutamate
recombinant enzyme complex TtGDH-APRTh, high Glu concentration, pH and temperature not specified in the publication
2
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K130Y
3.33
L-glutamate
-
cofactor NAD+, value below 200.0
4
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K130Y
4.4
L-glutamate
recombinant enzyme complex TtGDH-APRTh, high Glu concentration, with AMP, pH and temperature not specified in the publication
4.5
L-glutamate
recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication
4.83
L-glutamate
-
cofactor NAD+
11
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K94Y
13
L-glutamate
recombinant enzyme complex TtGDH-APRTh, with L-leucine and AMP, pH and temperature not specified in the publication
14
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K94Y
42
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1G96Y
48
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K118Y
57
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1D172Y
57
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2D172Y
57
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2G96Y
59
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K118Y
65
L-glutamate
-
pH 9.5, 25°C, wild-type enzyme hGDH1
83
L-glutamate
-
pH 9.5, 25°C, wild-type enzyme hGDH2
121.2
L-glutamate
-
pH 7.6, 90°C
2
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K130Y
2.8
NAD+
recombinant enzyme complex TtGDH-APRTh, pH and temperature not specified in the publication
3.7
NAD+
recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication
4
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K130Y
9.1
NAD+
recombinant enzyme complex TtGDH-APRTh, with AMP, pH and temperature not specified in the publication
11
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K94Y
12
NAD+
recombinant enzyme complex TtGDH-APRTh, with L-leucine and AMP, pH and temperature not specified in the publication
14
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K94Y
42
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1G96Y
48
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K118Y
51
NAD+
-
pH 9.5, 25°C, mutant enzyme E279M
57
NAD+
-
pH 9.5, 25°C, mutant enzyme E279L
57
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1D172Y
57
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2D172Y
57
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2G96Y
59
NAD+
-
pH 9.5, 25°C, mutant enzyme E279G
59
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K118Y
61
NAD+
-
pH 9.5, 25°C, mutant enzyme E279R
65
NAD+
-
pH 9.5, 25°C, wild-type enzyme
65
NAD+
-
pH 9.5, 25°C, wild-type enzyme hGDH1
68
NAD+
-
pH 9.5, 25°C, mutant enzyme E279Y
83
NAD+
-
pH 9.5, 25°C, wild-type enzyme hGDH2
0.2
NADH
recombinant enzyme complex TtGDH-APRTh, pH and temperature not specified in the publication
0.72
NADH
recombinant enzyme complex TtGDH-APRTh, with AMP, pH and temperature not specified in the publication
9.1
NADH
recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication
29
NADH
recombinant enzyme complex TtGDH-APRTh, with L-leucine and AMP, pH and temperature not specified in the publication
77
NADH
-
mutant C119G, hGDH1
79
NADH
-
mutant C119Y, hGDH1
81
NADH
-
mutant C119A, hGDH1
85
NADH
-
mutant C59Y, hGDH1
88
NADH
-
mutant C274Y, hGDH1
90
NADH
-
concentration range: 0.04-0.1 mM
90
NADH
-
mutant C274A, hGDH1
90
NADH
-
mutant C59A, hGDH1
91
NADH
-
mutant C274G, hGDH1
91
NADH
-
mutant C59G, hGDH1
93
NADH
-
25°C, mutant enzyme K333L
95
NADH
-
25°C, mutant enzyme H454Y
98
NADH
-
25°C, mutant enzyme K337L
100
NADH
-
25°C, mutant enzyme K346L
100
NADH
-
mutant C274Y, hGDH2
101
NADH
-
mutant C119G, hGDH2
101
NADH
-
mutant enzyme M415L/R443S/G456A, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
102
NADH
-
25°C, mutant enzyme G446D
103
NADH
-
mutant C119Y, hGDH2
104
NADH
-
25°C, wild-type enzyme
104
NADH
-
pH 8.0, 25°C, wild-type enzyme hGDH1
104
NADH
-
wild-type, hGDH1
104
NADH
-
isozyme GDH1, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
104
NADH
-
wild type isozyme GDH1, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
105
NADH
-
25°C, mutant enzyme K344L
105
NADH
-
mutant C119A, hGDH2
108
NADH
-
mutant C59Y, hGDH2
109
NADH
-
mutant C274G, hGDH2
110
NADH
-
mutant C59G, hGDH2
111
NADH
-
25°C, mutant enzyme S445L
114
NADH
-
mutant C274A, hGDH2
117
NADH
-
mutant C59A, hGDH2
118
NADH
-
mutant enzyme L415M/S443R/A456G, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
130
NADH
-
pH 8.0, 25°C, wild-type enzyme hGDH2
130
NADH
-
wild-type, hGDH2
130
NADH
-
isozyme GDH2, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
130
NADH
-
wild type isozyme GDH2, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
134
NADH
-
pH 8.0, 25°C, mutant enzyme S443R hGDH2
374.5
NADH
-
pH 7.6, 90°C
102
NADP+
-
concentration range: 0.02-0.2 mM
399.6
NADP+
-
pH 7.6, 90°C
112
NADPH
-
concentration range: 0.002-0.1 mM
200
NADPH
-
NADPH-dependent activity
387.5
NADPH
-
pH 7.6, 90°C
0.31
NH3
recombinant enzyme complex TtGDH-APRTh, pH and temperature not specified in the publication
1.1
NH3
recombinant enzyme complex TtGDH-APRTh, with AMP, pH and temperature not specified in the publication
16
NH3
recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication
44
NH3
recombinant enzyme complex TtGDH-APRTh, with L-leucine and AMP, pH and temperature not specified in the publication
43.8
NH4+
-
pH 7.6, 90°C
63.3
NH4+
-
concentration range: 0.2-5 mM
168
NH4+
-
concentration range: 10-200 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0015 - 0.0692
17beta-estradiol
0.001 - 0.0032
corticosterone
0.0072 - 0.396
dehydroepiandrosterone
0.0494 - 0.814
dehydrotestosterone
0.001 - 0.008
diethylstilbestrol
0.0117 - 0.287
pregnenolone
0.0123 - 0.596
progesterone
0.0015
17beta-estradiol
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0151
17beta-estradiol
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.0269
17beta-estradiol
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0692
17beta-estradiol
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.05
Chloroquine
Homo sapiens
-
GDH1
0.14
Chloroquine
Homo sapiens
-
GDH2
0.001
corticosterone
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0021
corticosterone
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0025
corticosterone
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.0032
corticosterone
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.0072
dehydroepiandrosterone
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0294
dehydroepiandrosterone
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.216
dehydroepiandrosterone
Homo sapiens
pH 8.0, temperature not specified in the publication
0.396
dehydroepiandrosterone
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.0494
dehydrotestosterone
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0915
dehydrotestosterone
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.494
dehydrotestosterone
Homo sapiens
pH 8.0, temperature not specified in the publication
0.814
dehydrotestosterone
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.001
diethylstilbestrol
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.00167
diethylstilbestrol
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0071
diethylstilbestrol
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.008
diethylstilbestrol
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0113
estriol
Homo sapiens
pH 8.0, temperature not specified in the publication
0.145
estriol
Homo sapiens
pH 8.0, temperature not specified in the publication
0.189
estriol
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.316
estriol
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.00017
GTP
Homo sapiens
inhibition of wild-type enzyme and mutant enzymes r470H and N498S. No inhibition of mutant enzyme G456A. IC50 of mutant enzyme R470G is 0.00017 mM, IC50 of mutant enzyme N49
0.00019
GTP
Homo sapiens
potent inhibitor. IC50 for wild-type enzyme is 0.00019 mM
0.00019
GTP
Homo sapiens
inhibition of wild-type enzyme and mutant enzymes r470H and N498S. No inhibition of mutant enzyme G456A. IC50 of wild-type enzyme is 0.00019 mM
0.00031
GTP
Homo sapiens
-
in the absence of other modulators, pH 8.0
0.001
GTP
Homo sapiens
-
isozyme GDH1
0.00161
GTP
Homo sapiens
-
in the presence of 0.1 mM ADP, pH 8.0
0.0028
GTP
Homo sapiens
IC50 of mutant enzyme G456A is 0.0028 mM
0.0028
GTP
Homo sapiens
IC50 for mutant enzyme G456A is 0.0028 mM. ADP renders the GLUD1-derived enzyme less sensitive to GTP inhibition
0.0106
GTP
Mus musculus
C-terminally FLAG-tagged recombinant protein, pH 8.0, 23°C
0.0108
GTP
Homo sapiens
-
IC50 for mutant enzyme S331T: 0.0108 mM
0.0113
GTP
Homo sapiens
-
IC50 for mutant enzyme M370L: 0.0113 mM
0.0122
GTP
Homo sapiens
-
IC50 for wild-type GLUD1: 0.0122 mM
0.0147
GTP
Homo sapiens
-
IC50 for mutant enzyme M415L: 0.0147 mM
0.0162
GTP
Homo sapiens
-
IC50 for mutant enzyme R443S: 0.0162 mM
0.0185
GTP
Homo sapiens
-
in the presence of 1 mM ADP, pH 8.0
0.0196
GTP
Homo sapiens
His-tagged recombinant protein, pH 8.0, 23°C
0.0212
GTP
Homo sapiens
wild-type, pH 8.0, 23°C
0.0239
GTP
Homo sapiens
-
in the presence of 0.1 mM ADP, pH 8.0
0.0245
GTP
Mus musculus
wild-type, pH 8.0, 23°C
0.0271
GTP
Mus musculus
N-terminally FLAG-tagged recombinant protein, pH 8.0, 23°C
0.07
GTP
Homo sapiens
-
isozyme GDH2
0.0785
GTP
Homo sapiens
-
in the absence of other modulators, pH 8.0
0.1668
GTP
Homo sapiens
-
in the presence of 1 mM ADP, pH 8.0
0.186
GTP
Homo sapiens
-
mutant S448P, pH 8.0, 25°C
0.227
GTP
Homo sapiens
-
mutant Q441R, pH 8.0, 25°C
0.242
GTP
Homo sapiens
wild-type, pH 8.0, 23°C
0.25
GTP
Homo sapiens
His-tagged recombinant protein, pH 8.0, 23°C
0.2627
GTP
Homo sapiens
-
wild-type, pH 8.0, 25°C
0.31
GTP
Homo sapiens
-
GDH1, in the absence of ADP, in 50 mM triethanolamine pH 8.0 buffer
0.317
GTP
Homo sapiens
-
mutant S445L, pH 8.0, 25°C
2.921
GTP
Homo sapiens
-
mutant H454Y, pH 8.0, 25°C
18.5
GTP
Homo sapiens
-
GDH1, in the presence of 1 mM ADP, in 50 mM triethanolamine pH 8.0 buffer
78.5
GTP
Homo sapiens
-
GDH2, in the absence of ADP, in 50 mM triethanolamine pH 8.0 buffer in 50 mM TRA pH 8.0 buffer
139.4
GTP
Homo sapiens
-
mutant enzyme R443S/G456A, in the absence of ADP, in 50 mM triethanolamine pH 8.0 buffer
166.8
GTP
Homo sapiens
-
GDH2, in the presence of 1 mM ADP, in 50 mM triethanolamine pH 8.0 buffer
180
GTP
Homo sapiens
-
mutant K450E, pH 8.0, 25°C
622.4
GTP
Homo sapiens
-
mutant enzyme R443S/G456A, in the absence of ADP, in 50 mM triethanolamine pH 8.0 buffer
0.0117
pregnenolone
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0541
pregnenolone
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.104
pregnenolone
Homo sapiens
pH 8.0, temperature not specified in the publication
0.287
pregnenolone
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.0123
progesterone
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0589
progesterone
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
0.119
progesterone
Homo sapiens
pH 8.0, temperature not specified in the publication
0.596
progesterone
Homo sapiens
presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication
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drug target
the ADP-ribosylation of glutamate dehydrogenase is catalyzed by Sirt4, and downregulates the TCA cycle. In the ternary complex model of Sirt4-NAD+-GDH, the acetylated lysine 171 of GDH is located close to NAD+. This suggests a possible mechanism underlying the ADP-ribosylation at cysteine 172, which may occur through a transient intermediate with ADP-ribosylation at the acetylated lysine 171
evolution
-
while GDH in most mammals is encoded by a single GLUD1 gene, humans and other primates have acquired a GLUD2 gene with distinct tissue expression profile
evolution
GDH is a widely distributed enzyme among all domains of life. Mammalian GDH is regulated allosterically by multiple metabolites, in which the antenna helix plays a key role to transmit the allosteric signals. In contrast, bacterial GDH is believed not to be regulated allosterically because it lacks the antenna helix
evolution
hGDH2 emerged recently via retroposition during primate evolution, being only present in humans and some closely related great apes. Functional evolution of hGDH isoenzymes, overview. Reflecting the very recent emergence of hGDH2 from hGDH1, the two human proteins show very high amino acid sequence homology (about 97%), differing in only 15 of 505 amino acids in their mature forms. Despite this similarity, hGDH2 has unique enzymatic and regulatory properties. These include GTP resistance and low basal activity amenable to activation by ADP and/or L-leucine, lower optimal pH and relative sensitivity to thermal inactivation. These properties are to a large extent associated with only two of the 15 amino acid substitutions that occurred in the course of hGDH2 evolution. In particular, the Gly456 to Ala substitution confers GTP resistance, whereas the Arg443 to Ser change is associated with lower basal activity, though still permitting activation by ADP
evolution
reflecting the very recent emergence of hGDH2 from hGDH1, the two human proteins show very high amino acid sequence homology (about 97%), differing in only 15 of 505 amino acids in their mature forms. Despite this similarity, hGDH2 has unique enzymatic and regulatory properties
evolution
while most mammals possess a single GDH1 protein (hGDH1 in the human) that is highly expressed in the liver, humans and other primates have acquired, via duplication, an hGDH2 isoenzyme with distinct functional properties and tissue expression profile. hGDH2 underwent rapid evolutionary adaptation, acquiring unique properties that enable enhanced enzyme function under conditions inhibitory to its ancestor hGDH1. These are thought to provide a biological advantage to humans with hGDH2 evolution occurring concomitantly with human brain development
evolution
while most mammals possess a single GDH1 protein (hGDH1 in the human) that is highly expressed in the liver, humans and other primates have acquired, via duplication, an hGDH2 isoenzyme with distinct functional properties and tissue expression profile. hGDH2 underwent rapid evolutionary adaptation, acquiring unique properties that enable enhanced enzyme function under conditions inhibitory to its ancestor hGDH1. These are thought to provide a biological advantage to humans with hGDH2 evolution occurring concomitantly with human brain development. A major evolutionary adaptation of hGDH2 is the ability of the enzyme to downregulate its activity in the absence of allosteric effectors
malfunction
deregulation of hGDH1/2 is implicated in the pathogenesis of several human disorders
malfunction
deregulation of hGDH1/2 is implicated in the pathogenesis of several human disorders. Glioma cells with the R132H IDH1 mutation show selective inhibition of GLUD2 expression markedly slows cell growth. xpression of GLUD2 (but not GLUD1) promotes tumor expansion, suggesting that R132H IDH1 glioma cells proliferate by utilizing enhanced glutamate flux through the GLUD2 pathway
malfunction
growth analysis of the aprth knockout strain (Tt27DELTAAPRTh) and aprth-overexpressing strain (Tt27NStHisAPRTh) of Thermus thermophilus in minimal medium. The Tt27DELTAAPRTh strain exhibits delayed growth and requires approximately 36 h to reach the early stationary phase, whereas the wild-type strain reaches this phase after 21 h of cultivation. The overexpressing Tt27NStHisAPRTh strain exhibits better growth than even the wild-type strain
metabolism
GDH1 is the protein partner for pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm). Facilitating the recycling of BCATm to form metabolon, GDH1 acts as a catalytic machine
metabolism
glutamate dehydrogenase pathway and its roles in cell and tissue biology in health and disease, , glutamate dehydrogenase (GDH) pathway and the Krebs cycle function, oxidative deamination of glutamate by hGDH1 and hGDH2 generates 2-oxoglutarate, ammonia and NADH orNADPH, regulation of the isozymes, detailed overview
metabolism
glutamate dehydrogenase pathway and its roles in cell and tissue biology in health and disease, glutamate dehydrogenase (GDH) pathway and the Krebs cycle function, oxidative deamination of glutamate by hGDH1 and hGDH2 generates 2-oxoglutarate, ammonia and NADH orNADPH, regulation of the isozymes, detailed overview
metabolism
the enzyme is involved in the nitrogen distribution during primary assimilation, photorespiratory re-assimilation and translocation in Arabidopsis thaliana, overview. Traditional route of glutamate formation via the 2-oxoglutarate amination with NH4+ is persued by mitochondrial NADH-glutamate dehydrogenase
metabolism
the original published sequence of bovine GDH contains a few mistakes. Lysine is the correct amino acid identity of residue 387 in the allosteric NADH binding site, not asparagine. The thermodynamic impact of this mistake is shown to be +5 kcal/mol per NADH binding site. Four other residues are corrected in the bovine GDH sequence, specifically G47S, A248V, V271I, and A272T. Allostery at site R459 depends upon the expansion and contraction between subunits within the trimer as the catalytic site closes and opens, respectively
physiological function
-
influence of alcohol on leukocyte GLDH activity, its diagnostic value, influence on metabolism and cells toxicity is analysed. Examination is conducted in 238 alcoholics and in 244 healthy persons. A fast increase of leukocyte GLDH activity after break in alcohol consumption is found. After 24 hours, activity increases by 21.8% (median 31.6%), after seven days by 33% (median 52%), yet after a short interval since last alcohol intake (up to 48 hours), it increases by 32% (median 36%)
physiological function
the glutamate dehydrogenase catalyzes the reversible interconversion of glutamate to 2-oxoglutarate and ammonia using NADP(H) and NAD(H) as cofactors, thus interconnecting amino acid and carbohydrate metabolism. Mammalian GDH is allosterically regulated, with GTP and ADP being the main negative and positive modulators, respectively
physiological function
-
allosteric activation and inhibition is important for enzyme regulation, overview
physiological function
-
the enzyme provides a pathway for ammonium assimilation
physiological function
-
the enzyme provides a pathway for ammonium assimilation, although the activity for ammonium is low
physiological function
enzyme is able to complement an Escherichia coli glutamate auxotroph lacking glutamate dehydrogenase
physiological function
in a gene disruption strain of GDH, only threonine dehydrogenase activity is detected, indicating that activities toward Gln/Ala/Val/Cys are dependent on GDH. The disruption strain cannot grow in a medium in which growth is dependent on amino acid catabolism, GDH may be the only enzyme that can discharge the electrons (to NADP+/NAD+) released from amino acids in their oxidation to 2-oxoacids. In a medium containing excess pyruvate, the disprution strain displays normal growth, but higher degrees of amino acid catabolism are observed
physiological function
in transgenic Nicotiana tabacum the GDH protein accumulates in the mitochondria of mesophyll cells and in the mitochondria of the phloem companion cells. Overexpression induces major changes in carbon and nitrogen metabolite accumulation and a reduction in growth characterized by a decrease in the amount of sucrose, starch and glutamine in the leaves, and accompanied by an increase in the amount of nitrate and chlorophyl. There is an increase in the content of asparagine and a decrease in proline. Overexpressing the genes GDHA and GDHB individually or simultaneously induces a differential accumulation of glutamate and glutamine and a modification of the glutamate to glutamine ratio
physiological function
GDH catalyzes the synthesis and degradation of glutamate using NAD(P)(H). Bacterial GDH is believed not to be regulated allosterically because it lacks the antenna helix. TtGDH is activated by AMP in a complex with APRTh where APRTh is necessary for the AMP-mediated allosteric activation of TtGDH. L-Leucine is also required for allosteric regulation/activation of the enzyme
physiological function
in vitro, GDH catalyzes the reversible deamination of Glu to NH4 +, 2-oxoglutarate forming NADH. The reversible lethal phenotype of gltS mutants reveals that mitochondrial NADH-GDH is unable to re-assimilate photorespiratory NH3 produced within the same organelle although its amination activity. In vitro is several fold higher than the glutamate synthase isozyme Fd-GOGAT (EC 1.4.7.1) activity. The in vivo direction of reversible NADH-GDH reaction is controversial. NADH-GDH can exist as two homohexamers of either alpha subunit encoded by GDH1 or beta subunit encoded by GDH2 and five heterohexamers containing both alpha and beta subunits in Arabidopsis thaliana as observed in other plants
physiological function
isozyme hGDH2 is found in both human astrocytes and neurons, where it is thought to contribute to glutamate handling, both as a neurotransmitter and as a metabolic intermediate. It plays a putative role in early nervous system development, neurodegenerative processes, and oncogenesis. Regarding its role in cancer pathophysiology, hGDH2 promotes tumor cell survival especially under deprived conditions, such as glucose or glutamine depletion
physiological function
the enzyme catalyzes the reversible conversion of glutamate to 2-oxoglutarate and ammonia while reducing NAD(P)+ to NAD(P)H serving both catabolic and anabolic reactions. In mammalian tissues, oxidative deamination of glutamate via GDH generates 2-oxoglutarate, which is metabolized by the Krebs cycle, leading to the synthesis of ATP. In addition, the GDH pathway is linked to diverse cellular processes, including ammonia metabolism, acid-base equilibrium, redox homeostasis (via formation of fumarate), lipid biosynthesis (via oxidative generation of citrate), and lactate production. hGDH2 is co-expressed with hGDH1 in human brain, kidney, testis and steroidogenic organs, but not in the liver. In human cerebral cortex, hGDH1 and hGDH2 are expressed in astrocytes, the cells responsible for removing and metabolizing transmitter glutamate, and for supplying neurons with glutamine and lactate. In human testis, hGDH2 (but not hGDH1) is densely expressed in the Sertoli cells, known to provide the spermatids with lactate and other nutrients. In steroid producing cells, hGDH1/2 is thought to generate reducing equivalents (NADPH) in the mitochondria for the biosynthesis of steroidal hormones. Lastly, up-regulation of hGDH1/2 expression occurs in cancer, permitting neoplastic cells to utilize glutamine/glutamate for their growth. In addition to contributing to Krebs cycle anaplerosis and energy production, GDH function is linked to redox homeostasis and cell signaling processes. By regulating bioenergetics and redox homeostasis human GDH1/2 have emerged as key players in the pathogenesis of human neoplasias and as therapeutic targets for halting tumor development and expansion
physiological function
the enzyme catalyzes the reversible conversion of glutamate to 2-oxoglutarate and ammonia while reducing NAD(P)+ to NAD(P)H serving both catabolic and anabolic reactions. In mammalian tissues, oxidative deamination of glutamate via GDH generates 2-oxoglutarate, which is metabolized by the Krebs cycle, leading to the synthesis of ATP. In addition, the GDH pathway is linked to diverse cellular processes, including ammonia metabolism, acid-base equilibrium, redox homeostasis (via formation of fumarate), lipid biosynthesis (via oxidative generation of citrate), and lactate production. hGDH2 is co-expressed with hGDH1 in human brain, kidney, testis and steroidogenic organs, but not in the liver. In human cerebral cortex, hGDH1 and hGDH2 are expressed in astrocytes, the cells responsible for removing and metabolizing transmitter glutamate, and for supplying neurons with glutamine and lactate. In human testis, hGDH2 (but not hGDH1) is densely expressed in the Sertoli cells, known to provide the spermatids with lactate and other nutrients. In steroid producing cells, hGDH1/2 is thought to generate reducing equivalents (NADPH) in the mitochondria for the biosynthesis of steroidal hormones. Lastly, upregulation of hGDH1/2 expression occurs in cancer, permitting neoplastic cells to utilize glutamine/glutamate for their growth. In addition to contributing to Krebs cycle anaplerosis and energy production, GDH function is linked to redox homeostasis and cell signaling processes. By regulating bioenergetics and redox homeostasis human GDH1/2 have emerged as key players in the pathogenesis of human neoplasias and as therapeutic targets for halting tumor development and expansion
additional information
transgenic mice overexpressing the enzyme in brain have decreases in MAP2A labeling of dendrites and in synaptophysin labeling of presynaptic terminals, increasing in neuronal numbers and dendrite and presynaptic terminal labeling with advancing age, and show decreases in long-term potentiation of synaptic activity and in spine density in dendrites of CA1 neurons. Despite overexpression of Glud1 in all neurons of the central nervous system, the Tg mice suffer neuronal losses in select brain regions, e.g., the CA1 but not the CA3 region, dendrite structure and neuronal numbers in brains of transgenic mice, overview. The transgenic mice are significantly more resistant than wild-type mice to induction and duration of anesthesia produced by anesthetics that suppress Glu neurotransmission, phenotype, overview
additional information
-
transgenic mice overexpressing the enzyme in brain have decreases in MAP2A labeling of dendrites and in synaptophysin labeling of presynaptic terminals, increasing in neuronal numbers and dendrite and presynaptic terminal labeling with advancing age, and show decreases in long-term potentiation of synaptic activity and in spine density in dendrites of CA1 neurons. Despite overexpression of Glud1 in all neurons of the central nervous system, the Tg mice suffer neuronal losses in select brain regions, e.g., the CA1 but not the CA3 region, dendrite structure and neuronal numbers in brains of transgenic mice, overview. The transgenic mice are significantly more resistant than wild-type mice to induction and duration of anesthesia produced by anesthetics that suppress Glu neurotransmission, phenotype, overview
additional information
-
glutamate is bound to the active site of GdhB, the GdhB-Glu complex takes an open-like structure. No substrate is found in the active site of the GdhAGdhB-Leu complex, while six leucine molecules are found at the interfaces of three subunits
additional information
GDH1 has an advanced structure that also encompasses the antenna showing that the entire hexamer undergoes substantial conformational changes during each catalytic cycle. As the catalytic cleft opens the NAD+ domain moves away from the glutamate binding domain, twisting around the antenna in a clockwise direction along with concomitant clockwise rotation of the ascending alpha-helix of the antenna. In addition, the small alpha-helix of the antenna (at the end of its descending random coil) undergoes striking conformational changes as the catalytic mouth opens. The importance of this small helix is underscored by observations showing that mutation of amino acids located in this helix in hGDH1 attenuate GTP inhibition leading to hyperinsulinemia/hyperammonemia (HI/HA) syndrome
additional information
GDH1 has an advanced structure that also encompasses the antenna showing that the entire hexamer undergoes substantial conformational changes during each catalytic cycle. As the catalytic cleft opens the NAD+ domain moves away from the glutamate binding domain, twisting around the antenna in a clockwise direction along with concomitant clockwise rotation of the ascending alpha-helix of the antenna. In addition, the small alpha-helix of the antenna (at the end of its descending random coil) undergoes striking conformational changes as the catalytic mouth opens. The importance of this small helix is underscored by observations showing that mutation of amino acids located in this helix in hGDH1 attenuate GTP inhibition leading to hyperinsulinemia/hyperammonemia (HI/HA) syndrome
additional information
-
GDH1 has an advanced structure that also encompasses the antenna showing that the entire hexamer undergoes substantial conformational changes during each catalytic cycle. As the catalytic cleft opens the NAD+ domain moves away from the glutamate binding domain, twisting around the antenna in a clockwise direction along with concomitant clockwise rotation of the ascending alpha-helix of the antenna. In addition, the small alpha-helix of the antenna (at the end of its descending random coil) undergoes striking conformational changes as the catalytic mouth opens. The importance of this small helix is underscored by observations showing that mutation of amino acids located in this helix in hGDH1 attenuate GTP inhibition leading to hyperinsulinemia/hyperammonemia (HI/HA) syndrome
additional information
glutamate dehydrogenase (GDH) from Thermus thermophilus is composed of two heterologous subunits, GdhA and GdhB. In the heterocomplex, GdhB acts as the catalytic subunit, whereas GdhA lacks enzymatic activity and acts as the regulatory subunit for activation by leucine. TTC1249 (APRTh), which is annotated as adenine phosphoribosyltransferase but lacks the enzymatic activity, forms a ternary complex with the enzyme heterodimer. The ternary complex exhibits GDH activity that is activated by leucine, as observed for the GdhA-GdhB binary complex
additional information
-
glutamate dehydrogenase (GDH) from Thermus thermophilus is composed of two heterologous subunits, GdhA and GdhB. In the heterocomplex, GdhB acts as the catalytic subunit, whereas GdhA lacks enzymatic activity and acts as the regulatory subunit for activation by leucine. TTC1249 (APRTh), which is annotated as adenine phosphoribosyltransferase but lacks the enzymatic activity, forms a ternary complex with the enzyme heterodimer. The ternary complex exhibits GDH activity that is activated by leucine, as observed for the GdhA-GdhB binary complex
additional information
sequence comparisons and GDH structure homology modeling studies and docking analyses of NADPH, NADH, 2-oxoglutarate, and L-glutamate into the predictive model of GDH, loop modeling, overview
additional information
structure-function analysis, overview. Structure comparison with isozyme hGDH1, comparison of open, semi-closed and closed conformations from apo-hGDH1 (PDB ID 1L1F) and hGDH2 (PDB ID 6G2U)
additional information
structure-function analysis, overview. Structure comparison with isozyme hGDH1, comparison of open, semi-closed and closed conformations from apo-hGDH1 (PDB ID 1L1F) and hGDH2 (PDB ID 6G2U)
additional information
-
structure-function analysis, overview. Structure comparison with isozyme hGDH1, comparison of open, semi-closed and closed conformations from apo-hGDH1 (PDB ID 1L1F) and hGDH2 (PDB ID 6G2U)
additional information
structure-function analysis, overview. Structure comparison with isozyme hGDH2, comparison of open, semi-closed and closed conformations from apo-hGDH1 (PDB ID 1L1F) and hGDH2 (PDB ID 6G2U)
additional information
structure-function analysis, overview. Structure comparison with isozyme hGDH2, comparison of open, semi-closed and closed conformations from apo-hGDH1 (PDB ID 1L1F) and hGDH2 (PDB ID 6G2U)
additional information
-
structure-function analysis, overview. Structure comparison with isozyme hGDH2, comparison of open, semi-closed and closed conformations from apo-hGDH1 (PDB ID 1L1F) and hGDH2 (PDB ID 6G2U)
additional information
-
transgenic mice overexpressing the enzyme in brain have decreases in MAP2A labeling of dendrites and in synaptophysin labeling of presynaptic terminals, increasing in neuronal numbers and dendrite and presynaptic terminal labeling with advancing age, and show decreases in long-term potentiation of synaptic activity and in spine density in dendrites of CA1 neurons. Despite overexpression of Glud1 in all neurons of the central nervous system, the Tg mice suffer neuronal losses in select brain regions, e.g., the CA1 but not the CA3 region, dendrite structure and neuronal numbers in brains of transgenic mice, overview. The transgenic mice are significantly more resistant than wild-type mice to induction and duration of anesthesia produced by anesthetics that suppress Glu neurotransmission, phenotype, overview
-
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heterohexamer
3 * 46328, GdhA, + 3 * 46112, GdhB, sequence calculation and SDS-PAGE
monomer
-
at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml
octamer
-
8 * 61000, or aggregate of two tetramers, SDS-PAGE
oligomer
-
at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml
tetramer
-
4 * 52000, SDS-PAGE
?
-
x * 57000, SDS-PAGE
?
-
x * 57000, SDS-PAGE
-
?
-
x * 57500, recombinant enzyme, SDS-PAGE
?
x * 47122, calculated from sequence
?
-
x * 56000, enzymes from mitochondria and endoplasmic reticulum
?
x * 46078, calculated from sequence
?
-
x * 46078, calculated from sequence
-
dimer
-
the GdhA-GdhB-Leu complex is crystallized as a heterohexamer composed of four GdhA subunits and two GdhB subunits. In this complex, six leucine molecules are bound at subunit interfaces identified as glutamate-binding sites in the GdhB-Glu complex
dimer
-
the GdhA-GdhB-Leu complex is crystallized as a heterohexamer composed of four GdhA subunits and two GdhB subunits. In this complex, six leucine molecules are bound at subunit interfaces identified as glutamate-binding sites in the GdhB-Glu complex
hexamer
-
6 * 54000, SDS-PAGE
hexamer
-
6 * 48000, SDS-PAGE
hexamer
-
6 * 49000, SDS-PAGE
hexamer
-
4 * 44000 + 2 * 46000, isoenzyme GDH2, SDS-PAGE
hexamer
-
isoenzyme GDH1, SDS-PAGE
hexamer
-
6 * 56000, wild-type enzyme and mutant enzymes K333L, K337L, K344L, K346L, S445L and G446L
hexamer
-
6 * 56500, hGDH1, SDS-PAGE
hexamer
-
6 * 56500, hGDH2, SDS-PAGE
hexamer
-
native gradient polyacryamide gel electrophoresis, 6 * 60000 Da
hexamer
-
the GdhB-Glu complex is a hexamer that binds 12 glutamate molecules: six molecules are bound at the substrate-binding sites, and the remaining six are bound at subunit interfaces, each composed of three subunits
hexamer
-
6 * 47300, recombinant enzyme, second peak in gel filtration corresponding to catalytically inactive monomer, SDS-PAGE
hexamer
-
6 * 46000, SDS-PAGE
hexamer
-
6 * 46000, recombinant enzyme, SDS-PAGE
hexamer
electrostatic interactions play a key role in the relevant stability of Pyrococcus furiosus hlutamate dehydrogenase quaternary assembly at low pH although there may be other contributions involved in the complex mechanism of subunit association required for protein function
hexamer
-
6 * 48000, SDS-PAGE
hexamer
-
6 * 46000, SDS-PAGE
hexamer
-
6 * 45000, SDS-PAGE
hexamer
-
6 * 44000, SDS-PAGE
hexamer
-
6 * 50000, membrane-bound liver enzyme, SDS-PAGE
hexamer
-
6 * 57000, SDS-PAGE
hexamer
6 * 47040, calculated from sequence, the natural enzyme was purified only as a hexameric form, whereas the recombinant enzyme was purified as both monomeric and hexameric forms. Only the enzyme in a hexameric form is active. Upon heat treatment (70°C for 15 min), the inactive monomeric form of the recombinant enzyme is at least partially associated with the hexameric form
hexamer
6 * 47300, SDS-PAGE, the natural enzyme was purified only as a hexameric form, whereas the recombinant enzyme was purified as both monomeric and hexameric forms. Only the enzyme in a hexameric form is active. Upon heat treatment (70°C for 15 min), the inactive monomeric form of the recombinant enzyme is at least partially associated with the hexameric form
hexamer
-
the GdhB-Glu complex is a hexamer that binds 12 glutamate molecules: six molecules are bound at the substrate-binding sites, and the remaining six are bound at subunit interfaces, each composed of three subunits
hexamer
-
6 * 53900, sedimentation equilibrium of enzyme treated with 6 M guanidinium and 0.5% 2-mercaptoethanol
hexamer
-
6 * 40500, SDS-PAGE
hexamer
-
6 * 59500, enzyme from both euthermic and hibernating animals
homohexamer
-
homohexamer
-
6 * 56000, SDS-PAGE
homohexamer
6 * 56000, about, dimer of trimers
homohexamer
dimer of trimers, the enzyme adopts a novel semi-closed conformation, which is an intermediate between known open and closed GDH1 conformations, differing from both. Structure-function analysis, overview. Each monomer consists of the glutamate-binding domain (residues 1-210), the NAD+-binding domain (residues 211-399), the antenna (residues 400-448), the pivot helix (residues 449-478) and the C-terminal alpha-helix (residues 479-501), which are very similar to the structural features of hGDH1. The antenna region is formed by the ascending and descending helix
homohexamer
method of determination not further specified
trimer
-
6 * 56000, mutant enzyme H454Y
trimer
-
analytical ultracentrifugation
trimer
-
analytical ultracentrifugation
-
additional information
gene products genes Gdh1, Gdh2 and Gdh3 are three different Gdh subunits that randomly associate to form a complex array of homo- and hetero-hexamers
additional information
gene products genes Gdh1, Gdh2 and Gdh3 are three different Gdh subunits that randomly associate to form a complex array of homo- and hetero-hexamers
additional information
gene products genes Gdh1, Gdh2 and Gdh3 are three different Gdh subunits that randomly associate to form a complex array of homo- and hetero-hexamers
additional information
structure overview
additional information
structure overview
additional information
-
structure overview
additional information
-
Thermus thermophilus, possesses GDH with a unique subunit configuration composed of two different subunits, GdhA, the regulatory subunit, and GdhB, the catalytic subunit, structure of the GdhA-GdhB-Leu complex, overview
additional information
sequence comparisons and GDH structure homology modeling studies, overview
additional information
-
Thermus thermophilus, possesses GDH with a unique subunit configuration composed of two different subunits, GdhA, the regulatory subunit, and GdhB, the catalytic subunit, structure of the GdhA-GdhB-Leu complex, overview
additional information
GDH is composed of two heterologous subunits, GdhA and GdhB. GdhA and GdhB form a heterohexamer, in which GdhB acts as the catalytic subunit and GdhA acts as the regulatory subunit to sense leucine. In the heterocomplex, GdhB acts as the catalytic subunit, whereas GdhA lacks enzymatic activity and acts as the regulatory subunit for activation by leucine. TTC1249 (APRTh), which is annotated as adenine phosphoribosyltransferase but lacks the enzymatic activity, forms a ternary complex with the enzyme heterodimer. The ternary complex exhibits GDH activity that is activated by leucine, as observed for the GdhA-GdhB binary complex
additional information
-
GDH is composed of two heterologous subunits, GdhA and GdhB. GdhA and GdhB form a heterohexamer, in which GdhB acts as the catalytic subunit and GdhA acts as the regulatory subunit to sense leucine. In the heterocomplex, GdhB acts as the catalytic subunit, whereas GdhA lacks enzymatic activity and acts as the regulatory subunit for activation by leucine. TTC1249 (APRTh), which is annotated as adenine phosphoribosyltransferase but lacks the enzymatic activity, forms a ternary complex with the enzyme heterodimer. The ternary complex exhibits GDH activity that is activated by leucine, as observed for the GdhA-GdhB binary complex
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I397V/I406L/S411A
mutation to residues found in isoforms Gdh1 and Gdh2, increase in thermal stability
I406L/S411A
mutation to residues found in isoforms Gdh1 and Gdh2, increase in thermal stability
S411A
mutation to residue found in isoforms Gdh1 and Gdh2, increase in thermal stability
HH454Y
mutation causes the hyperinsulinism/hyperammonemia syndrome (HHS) where insulin is hypersecreted upon consumption of protein due to loss of GLZD1 function. Mutation lies in the GTP binding pocket
A456G
-
mutant of isoenzyme hGDH2 shows no change in heat inactivation process compared to wild-type enzyme
C119A
-
reduction in the ADP-ribosylation
C119G
-
reduction in the ADP-ribosylation
C119Y
-
reduction in the ADP-ribosylation
C274A
-
reduction in the ADP-ribosylation
C274G
-
reduction in the ADP-ribosylation
C274Y
-
reduction in the ADP-ribosylation
C323G
-
decreased turnover rate of both isoenzymes as compared to wild-type
C323L
-
decreased turnover rate of both isoenzymes as compared to wild-type
C323M
-
decreased turnover rate of both isoenzymes as compared to wild-type
C323R
-
decreased turnover rate of both isoenzymes as compared to wild-type
C323Y
-
decreased turnover rate of both isoenzymes as compared to wild-type
C59A
-
reduction in the ADP-ribosylation
C59G
-
reduction in the ADP-ribosylation
D185A
-
site-directed mutagenesis, the mutant shows no activation by leucine in contrast to the wild-type enzyme
E279L
-
14.1fold increase in Km-value for NAD+
E279M
-
14.1fold increase in Km-value for NAD+
E279R
-
10.7fold increase in Km-value for NAD+
E279Y
-
11.8fold increase in Km-value for NAD+
G446C
-
a one-month-old boy with a rare form of congenital hyperinsulinism characterised by hypoglycaemia and hyperammonaemia is described. The patient is heterozygous for a novel de novo mutation in the GLUD1 gene in exon 11 of chromosome 10, which encodes glutamate dehydrogenase (GDH). This point mutation alters the corresponding guanine-guanine-thymine (GGT) codon to thymine-guaninethymine (TGT), changing the glycine at position 446 to cysteine (Gly446Cys), which is located on the allosteric domain of the enzyme. The result confirmed the diagnosis of hyperinsulinism and hyperammonaemia syndrome. The patient is treated with diazoxide (12 mg/kg/day) and the glucose infusion is gradually decreased over four days. Blood glucose is maintained around 4 mmol/l. However, the infants ammonia level remain above 120 mmol/l
G446D
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
H470R
-
mutant of isoenzyme hGDH2 shows no change in heat inactivation process compared to wild-type enzyme
K333L
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
K337L
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
K344L
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
K346L
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
K450E
-
mutation in the pivot helix, mutant shows diminished basal activity and a strongly decreased maximal activity, no activation by L-leucine, ADP restores the decreased activity of K450E but this occurs at substantially higher concentrations compared to wild-type, mutant shows an increased resistance to GTP inhibition, mutation makes the enzyme extremely heat-labile compared to wild-type. IC50 (GTP): 180
K450G
-
mutant enzyme is unable to bind GTP, no difference in sensitivity to aluminum binding between wild-type and mutant enzyme
L415M
-
mutant of isoenzyme hGDH2 shows no change in heat inactivation process compared to wild-type enzyme
L415M/S443R/A456G
-
triple mutant hGDH2(hGDH1390-465)hGDH2 (amino acid segment 390-465 of hGDH2 replaced by the corresponding hGDH1 segment)
M370L
-
mutation does not abolish basal activity and does not abrogate the activation of the enzyme by L-Leu
M415L
-
mutation does not abolish basal activity and does not abrogate the activation of the enzyme by L-Leu
M415L/R443S/G456A
-
triple mutant hGDH1(hGDH2390-465)hGDH1 (amino acid segment 390-465 of hGDH1 replaced by the corresponding hGDH2 segment)
M415L/R443S/G456A/R470H
site-directed mutagenesis
N498S
mutation does not render the enzyme resistant to GTP inhibition
R151M
-
site-directed mutagenesis, the mutant shows reduced activation by leucine compared to the wild-type enzyme
R443S/G456A
-
resistant to GTP inhibition
R463A
-
stimulatory effect of ADP is eliminated
S331T
-
mutation does not abolish basal activity and does not abrogate the activation of the enzyme by L-Leu
S443R
-
mutant of isoenzyme hGDH2 shows a dramatic increase in thermal stability from 45 min at 45°C for the wild-type enzyme to 300 min for the mutant enzyme. KM-values and turnover-numbers are nearly identical to wild-type enzyme
S445A
site-directed mutagenesis, the specific antibody, generated from 12-amino acid hGDH2-specific peptide PTAEFQDSISGA, corresponding to residues 436-447 of the mature human protein, shows reduced reactivity with the enzyme mutant
Y187E
-
KM-values for NADH and 2-oxoglutareta are similar to wild-type values, about 4fold decrease of Vmax
Y187M
-
KM-values for NADH and 2-oxoglutareta are similar to wild-type values, about 4fold decrease of Vmax, no significant actication by ADP
Y187S
-
KM-values for NADH and 2-oxoglutareta are similar to wild-type values, about 4fold decrease of Vmax, no significant actication by ADP
Y197R
-
KM-values for NADH and 2-oxoglutareta are similar to wild-type values, about 4fold decrease of Vmax, no significant actication by ADP
up
show higher activities in cells grown on the peptides-plus-S(0) medium than in cells using maltose as the sole carbon source
A72D
-
site-directed mutagenesis, the mutant shows no activation by leucine in contrast to the wild-type enzyme
D166A
-
site-directed mutagenesis, the mutant shows reduced activation by leucine compared to the wild-type enzyme
I71T
-
site-directed mutagenesis, the mutant shows reduced activation by leucine compared to the wild-type enzyme
R134A
-
site-directed mutagenesis, the mutant shows no activation by leucine in contrast to the wild-type enzyme
Y38S
-
site-directed mutagenesis, the mutant shows reduced activation by leucine compared to the wild-type enzyme
D172Y
-
ratio of turnover number to Km-value for NAD+ is 1.22fold lower than the wild-type value. Ratio of turnover number to Km-value for glutamate is 1.2fold lower than the wild-type value, isoenzyme hGDH1
D172Y
-
ratio of turnover number to Km-value for NAD+ is 1.2fold lower than the wild-type value. Ratio of turnover number to Km-value for glutamate is 1.1fold lower than the wild-type value, reduced sensitivity to ADP activation, isoenzyme hGDH2
E279G
-
9.8fold increase in Km-value for NAD+
E279G
-
mutant enzyme is unable to bind NAD+, no difference in sensitivity to aluminum binding between wild-type and mutant enzyme
G456A
mutant enzyme is resistant to GTP
G456A
mutation renders the enzyme markedly resistant to GTP inhibition, mutation abolishes the cooperative behavior of the enzyme
G456A
naturally occuring mutation, an evolutionary amino acid substitution compared to hGDH1 which confers GTP resistance, residue 456 from the pivot helix has a key role in the transition between closed and open conformations, a process which includes movements of the pivot helix and the NAD+-binding domain, leading to the opening of the active site cleft. Local flexibility is affected by an intersubunit hydrophobic interaction at the base of the antenna between residues Phe387 and Leu401. In GDH1, flexibility is also affected by the presence of the small and flexible Gly456 residue which packs against the Phe and Leu. Replacement of Gly by the bulkier and less flexible Ala456 in hGDH2 is expected to reduce local flexibility, and thus to affect the opening and closing of the active site cleft
G456A
site-directed mutagenesis, residue 456 from the pivot helix has a key role in the transition between closed and open conformations, a process which includes movements of the pivot helix and the NAD+-binding domain, leading to the opening of the active site cleft. Local flexibility is affected by an intersubunit hydrophobic interaction at the base of the antenna between residues Phe387 and Leu401. In GDH1, flexibility is also affected by the presence of the small and flexible Gly456 residue which packs against the Phe and Leu. Replacement of Gly by the bulkier and less flexible Ala456 as in hGDH2 is expected to reduce local flexibility, and thus to affect the opening and closing of the active site cleft
G96Y
-
ratio of turnover number to Km-value for NAD+ is 1.4fold lower than the wild-type value. Ratio of turnover number to Km-value for glutamate is 13.5fold lower than the wild-type value, isoenzyme hGDH1
G96Y
-
ratio of turnover number to Km-value for NAD+ is 1.4fold lower than the wild-type value. Ratio of turnover number to Km-value for glutamate is 14.3fold lower than the wild-type value, isoenzyme hGDH2
H454Y
-
lower basal activity but comparable maximal activity as wild-type
H454Y
-
mutation results in depolymerization of hexameric enzyme into active trimers. Mutation has no effect on expression or stability of the protein. The Km-value for NADH is 1.5fold greater than the wild-type value and the KM-value for 2-oxoglutarate is 2.5fold greater than the wild-type value. Vmax values are similar for wild-type and mutant enzyme
H454Y
-
mutation in the pivot helix, mutant shows diminished basal activity and a strongly decreased maximal activity, almost no activation by L-leucine, mutant H454Y requires higher concentrations of ADP for its activation than the wild-type, mutant shows an increased resistance to GTP inhibition, mutation makes the enzyme extremely heat-labile compared to wild-type. IC50 (GTP): 2.92
K118Y
-
ratio of turnover number to Km-value for NAD+ is 1.8fold lower than the wild-type value. Ratio of turnover number to Km-value for glutamate is 9.9fold lower than the wild-type value, isoenzyme hGDH1
K118Y
-
ratio of turnover number to Km-value for NAD+ is 2fold lower than the wild-type value. Ratio of turnover number to Km-value for glutamate is 8.1fold lower than the wild-type value, isoenzyme hGDH2
K130Y
-
ratio of turnover number to Km-value for NAD+ is 26.5fold lower than the wild-type value. Ratio of turnover number to Km-value for glutamate is 35fold lower than the wild-type value, isoenzyme hGDH2
K130Y
-
ratio of turnover number to Km-value for NAD+ is 41.6fold lower than the wild-type value. Ratio of turnover number to Km-value for glutamate is 47.3fold lower than the wild-type value, isoenzyme hGDH1
K94Y
-
ratio of turnover number to Km-value for NAD+ is 5.6fold lower than the wild-type value. Ratio of turnover number to Km-value for glutamate is 25.5fold lower than the wild-type value, isoenzyme hGDH2
K94Y
-
ratio of turnover number to Km-value for NAD+ is 6.6fold lower than the wild-type value. Ratio of turnover number to Km-value for glutamate is 37.8fold lower than the wild-type value, isoenzyme hGDH1
Q441R
-
mutation in the small helix of the antenna, basal activity increased by 2fold compared to wild-type, potentiated activation by L-leucine, Q411R substitution has little effect on the allosteric regulation of the mutant by ADP and GTP compared to wild-type, mutation makes the enzyme more resistant to thermal inactivation compared to wild-type. IC50 (GTP): 0.227
Q441R
site-directed mutagenesis, the specific antibody, generated from 12-amino acid hGDH2-specific peptide PTAEFQDSISGA, corresponding to residues 436-447 of the mature human protein, shows reduced reactivity with the enzyme mutant
R443S
mutation abolishes basal activity and renders the enzyme dependent on ADP for function
R443S
-
mutation abolishes basal activity and totally abrogates the activation of the enzyme by L-Leu, 1-10 mM, in absence of other effectors. When ADP, 0.025-0.1 mM, is present, L-Leu (0.3-6.0 mM) activates the mutant enzyme up to 2000%. The mutant enzyme is much less sensitive to ADP than the wild-type enzyme, however at 1 mM ADP the Vmax is comparable with that of wild-type enzyme GLUD1 GDH. KM-value for 2-oxoglutarate is similar to wild-type value
R443S
naturally occuring mutation, an evolutionary amino acid substitution which is associated with lower basal activity, though still permitting activation by ADP. Replacement of the GDH1 residue Arg443 by Ser in GDH2 was a key event early in the evolution of the GLUD2 gene in humans and great apes, which has been related with a lower basal activity and heat sensitivity. Arg443 is involved in the stabilization of open and closed conformations of GDH1. GDH1 structures reveal that the transition from open to closed conformations is associated with partial unfolding of the C-terminus of the descending helix, immediately after residue Arg443, thereby reducing the length of the helix by almost a half turn. Arg443 forms conserved intersubunit hydrogen bonds with backbone and/or side chains of Asp408 and Ser409 residues from the ascending helix of a neighbouring chain and a conserved stacking interaction with Tyr405. Through these interactions, Arg443 establishes crucial intersubunit connections that mutually stabilize the ascending and descending helices. In contrast, substitution of Arg443 by Ser in hGDH2 leads to a loss of the above interactions, and a loose packing in the antenna region. This results in a higher flexibility in the area and in a lower stability of the enzyme, which subsequently may contribute to a lower enzymatic basal activity and an increased heat sensitivity
R443S
site-directed mutagenesis, replacement of the GDH1 residue Arg443 by Ser in GDH2 was a key event early in the evolution of the GLUD2 gene in humans and great apes, which has been related with a lower basal activity and heat sensitivity. Arg443 is involved in the stabilization of open and closed conformations of GDH1. GDH1 structures reveal that the transition from open to closed conformations is associated with partial unfolding of the C-terminus of the descending helix, immediately after residue Arg443, thereby reducing the length of the helix by almost a half turn. Arg443 forms conserved intersubunit hydrogen bonds with backbone and/or side chains of Asp408 and Ser409 residues from the ascending helix of a neighbouring chain and a conserved stacking interaction with Tyr405. Through these interactions, Arg443 establishes crucial intersubunit connections that mutually stabilize the ascending and descending helices. In contrast, substitution of Arg443 by Ser in hGDH2 leads to a loss of the above interactions, and a loose packing in the antenna region. This results in a higher flexibility in the area and in a lower stability of the enzyme, as we observed in earlier studies, which subsequently may contribute to a lower enzymatic basal activity and an increased heat sensitivity
R470H
mutation does not render the enzyme resistant to GTP inhibition
R470H
naturally occuring mutation, an evolutionary amino acid substitution
S445L
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
S445L
-
mutation in the small helix of the antenna, basal activity increased by 2fold compared to wild-type, potentiated activation by L-leucine, S445L mutant retains the regulatory properties of the wild-type concerning its activation by ADP and inhibition by GTP, mutation makes the enzyme more resistant to thermal inactivation compared to wild-type. IC50 (GTP): 0.317
S448P
-
unstable in Tris-buffer especially in the absence of allosteric activators, basal and maximal specific activity is lower than that from wild-type
S448P
-
mutation located in the junction of the antenna with the pivot helix, mutant shows reduced basal activity without significantly altering the allosteric regulation by GTP or ADP, mutant is slightly induced by L-leucine. IC50 (GTP): 0.186
Y187G
-
KM-values for NADH and 2-oxoglutareta are similar to wild-type values, about 4fold decrease of Vmax, no significant actication by ADP
Y187G
-
mutant enzyme is unable to bind ADP, no difference in sensitivity to aluminum binding between wild-type and mutant enzyme
additional information
-
the catalytic properties of the chimeric enzymes GDH1(GDH2390-448)GDH1 and GDH2(GDH1390-448)GDH2 are not altered compared to the wild type enzyme and show almost identical sensitivity to palmitoyl-CoA inhibitory aspects of the original wild type isozymes
additional information
neither FLAG nor (His)6 tags disturb the mitochondrial localization of GDH. The addition of the small tags to the N-terminus of the mature mitochondrial enzyme does not change the ADP activation or GTP inhibition pattern of the proteins
additional information
neither FLAG nor (His)6 tags disturb the mitochondrial localization of GDH. The addition of the small tags to the N-terminus of the mature mitochondrial enzyme does not change the ADP activation or GTP inhibition pattern of the proteins
additional information
-
neither FLAG nor (His)6 tags disturb the mitochondrial localization of GDH. The addition of the small tags to the N-terminus of the mature mitochondrial enzyme does not change the ADP activation or GTP inhibition pattern of the proteins
additional information
neither FLAG nor (His)6 tags disturb the mitochondrial localization of GDH. The addition of the small tags to the N-terminus of the mature mitochondrial enzyme does not change the ADP activation or GTP inhibition pattern of the proteins. The addition of FLAG tag to the C-terminus of the mouse GDH left the recombinant protein fivefold less sensitive to ADP activation
additional information
-
neither FLAG nor (His)6 tags disturb the mitochondrial localization of GDH. The addition of the small tags to the N-terminus of the mature mitochondrial enzyme does not change the ADP activation or GTP inhibition pattern of the proteins. The addition of FLAG tag to the C-terminus of the mouse GDH left the recombinant protein fivefold less sensitive to ADP activation
additional information
growth analysis of the aprth knockout strain (Tt27DELTAAPRTh) and aprth-overexpressing strain (Tt27NStHisAPRTh) of Thermus thermophilus in minimal medium. The Tt27DELTAAPRTh strain exhibits delayed growth and requires approximately 36 h to reach the early stationary phase, whereas the wild-type strain reaches this phase after 21 h of cultivation. The overexpressing Tt27NStHisAPRTh strain exhibits better growth than even the wild-type strain
additional information
-
growth analysis of the aprth knockout strain (Tt27DELTAAPRTh) and aprth-overexpressing strain (Tt27NStHisAPRTh) of Thermus thermophilus in minimal medium. The Tt27DELTAAPRTh strain exhibits delayed growth and requires approximately 36 h to reach the early stationary phase, whereas the wild-type strain reaches this phase after 21 h of cultivation. The overexpressing Tt27NStHisAPRTh strain exhibits better growth than even the wild-type strain
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