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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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
beta-3-methylaspartyl phosphate + NADPH
beta-3-methylaspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
L-aspartate 4-semialdehyde + arsenate + NADP+
?
-
-
-
-
r
L-aspartate 4-semialdehyde + HasO42- + NADP+
?
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NAD+
L-4-aspartyl phosphate + NADH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + vanadate + NADP+
?
-
-
-
-
r
L-aspartate-4-semialdehyde + cacodylate + NADP+
L-4-aspartyl cacodylate + NADPH
10% of the activity with phosphate
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
additional information
?
-
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
enzyme in pathway from L-aspartic acid to L-lysine, L-methionine, L-threonine and L-isoleucine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of methionine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of methionine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
part of the biosynthetic aspartate pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
reductive dephosphorylation
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
2nd step in the biosynthetic aspartate pathway, also required for biosynthesis of the beta-lactam caphamycin, overview
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
2nd step in the biosynthetic aspartate pathway, also required for biosynthesis of the beta-lactam caphamycin, overview
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
reductive dephosphorylation in the aspartate biosynthetic pathway of plants and microorganisms
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
-
r
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NAD+
L-4-aspartyl phosphate + NADH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NAD+
L-4-aspartyl phosphate + NADH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
ASADH is an important enzyme, occupying the first branch position of the biosynthetic pathway of the aspartate family of amino acids, i.e. lysine, methionine, isoleucine and threonine, L-aspartate-beta-semialdehyde is a key intermediate in the biosynthesis of diaminopimelic acid
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
the enzyme takes part in the lysine/homoserine-biosynthetic pathway
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
active site structure, overview
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
ASADH is an important enzyme, occupying the first branch position of the biosynthetic pathway of the aspartate family of amino acids, i.e. lysine, methionine, isoleucine and threonine, L-aspartate-beta-semialdehyde is a key intermediate in the biosynthesis of diaminopimelic acid
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
active site structure, overview
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
-
the essential ASADH produces the first branch-point metabolite in the biosynthetic pathways that lead to the production of lysine, threonine, methionine and isoleucine as well as the cell-wall precursor diaminopimelate
-
-
?
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
reverse reaction: reductive dephosphorylation
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
?
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
reductive dephosphorylation in the aspartate biosynthetic pathway
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
reductive dephosphorylation in the aspartate biosynthetic pathway, aspartate-beta-semialdehydr is the key intermediate in biosynthesis of diaminopimelic acid
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
formation of an acyl-enzyme intermediate
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
formation of an acyl-enzyme intermediate
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
-
-
r
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
-
reverse reaction: reductive dephosphorylation
-
r
additional information
?
-
-
the putative phosphate side contains arginine and a lysine that can provide electrostratic attraction to bind an oxyanion
-
-
?
additional information
?
-
-
maximum velocity with HAsO42- is 0.4 times that with HPO42-
-
-
?
additional information
?
-
-
the kinetic parameters with arsenate are comparable to those of phosphate, vanadate is an excellent substrate for the enzyme
-
-
?
additional information
?
-
oxyanion binding sites and structures with arsenate and periodate
-
-
?
additional information
?
-
-
when arsenate is substituted for phosphate the rates are about one-half those with corresponding phosphate concentrations
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
enzyme in pathway from L-aspartic acid to L-lysine, L-methionine, L-threonine and L-isoleucine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of threonine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of methionine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
synthesis of methionine
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
part of the biosynthetic aspartate pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
2nd step in the biosynthetic aspartate pathway, also required for biosynthesis of the beta-lactam caphamycin, overview
-
-
?
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
2nd step in the biosynthetic aspartate pathway, also required for biosynthesis of the beta-lactam caphamycin, overview
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L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
reductive dephosphorylation in the aspartate biosynthetic pathway of plants and microorganisms
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L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
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L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
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L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
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L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
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L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
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L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
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L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
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L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
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L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
ASADH is an important enzyme, occupying the first branch position of the biosynthetic pathway of the aspartate family of amino acids, i.e. lysine, methionine, isoleucine and threonine, L-aspartate-beta-semialdehyde is a key intermediate in the biosynthesis of diaminopimelic acid
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
the enzyme takes part in the lysine/homoserine-biosynthetic pathway
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
ASADH is an important enzyme, occupying the first branch position of the biosynthetic pathway of the aspartate family of amino acids, i.e. lysine, methionine, isoleucine and threonine, L-aspartate-beta-semialdehyde is a key intermediate in the biosynthesis of diaminopimelic acid
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
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the essential ASADH produces the first branch-point metabolite in the biosynthetic pathways that lead to the production of lysine, threonine, methionine and isoleucine as well as the cell-wall precursor diaminopimelate
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L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
reductive dephosphorylation in the aspartate biosynthetic pathway
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L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
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reductive dephosphorylation in the aspartate biosynthetic pathway, aspartate-beta-semialdehydr is the key intermediate in biosynthesis of diaminopimelic acid
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(1R)-5-[(2-carboxyphenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
(1R)-5-[(3-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
(1R)-5-[(4-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
(2R,3aR)-5-[(methylsulfonyl)methyl]-2,3,3a,4-tetrahydro-1H-indole-2-carboxylate
(2R,5R)-2,3,4,5-tetrahydropyridine-2,5-dicarboxylate
(2R,5R)-5-nitro-2,3,4,5-tetrahydropyridine-2-carboxylate
(2R,7aR)-2,3,7,7a-tetrahydro-1H-indole-2,6-dicarboxylate
(2R,7aR)-6-hydroxy-2,3,7,7a-tetrahydro-1H-indole-2-carboxylate
(2R,7aR)-6-nitro-2,3,7,7a-tetrahydro-1H-indole-2-carboxylate
(2R,8aR)-2,7-dinitro-1,2,8,8a-tetrahydronaphthalene
(3aR)-2-oxo-2,3,3a,4-tetrahydro-1H-benzimidazole-5-carboxylic acid
(3aR)-5-nitro-1,3,3a,4-tetrahydro-2H-benzimidazol-2-one
(3aR)-5-nitro-3a,4-dihydro-1H-indene-1,3(2H)-dione
(3aR)-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
(3aR)-6-chloro-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
(7aR)-2-oxo-2,3,7,7a-tetrahydro-1H-indole-6-carboxylate
(7aR)-3-(carboxylatomethyl)-6-nitro-7,7a-dihydro-1H-indole-2-carboxylate
(S)-2-amino-5-fluoro-4-oxo-5-phosphono-pentanoic acid
irreversible inhibition
(S)-2-amino-5-phosphono-pent-4-ynoic acid
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1-amino-2-naphthol-4-sulfonic acid
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2,3-dichloro-1,4-naphthoquinone
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2,3-dichloro-5,6-dicyano-1,4-benzoquinone
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2,3-dichloro-5,8-dihydroxy-1,4-naphthoquinone
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2-bromo-1,4-naphthoquinone
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2-Chloro-1,4-naphthoquinone
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2-chloro-3-methoxy-1,4-naphthoquinone
a selective, low to sub-micromolar inhibitors of the fungal ASADHs
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3-Chloroacetylpyridine-adenine dinucleotide phosphate
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NADP+ and NADPH protect
3-hydroxyaspartic acid
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4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
4-benzoquinone
enzyme binding structure analysis, a competitive and rel. weak inhibitor. The carbonyl oxygens of the inhibitor each participate in hydrogen bonds, one with the epsilon-nitrogen of Lys211 and the guanidine nitrogen of Arg114 (substrate binding residues), and the other with the thiol of the Cys154 nucleophile. There are also hydrophobic interactions with Asn153. While the position of these carbonyl groups are fixed, the aromatic ring adopts a somewhat different orientation in each of the subunits of the dimer
4-nitro-N,N-diethylbenzimidazolinone
4-nitro-N,N-dimethylbenzimidazolinone
4-nitro-N-ethylphthalimide
4-nitro-N-methylphthalimide
5-(carboxylatocarbonyl)-1H-pyrrole-2-carboxylate
5-aminoisoquinoline
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5-[[(4-nitrophenyl)amino]carbonyl]-1,3-benzenedimethylcarboxylate
acetylenic and z-olefinic analogues
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competitive inhibition
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adenosine 5'-triphosphate
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causes a time-dependent inactivation at a concentration of 3.5 mM, 0°C, pH 6.5 and 2 mM dithiothreitol, inactivation can be completely reversed by warming the reaction mixture to 25°C, 50% inactivation occurs at a concentration of 2.5 mM, NADH protects
aromatic aldehydes
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e.g.: benzaldehyde, weak
caulerpin
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molecular docking and dynamics simulation of Vibrio anguillarum aspartate semialdehyde dehydrogenase with natural product caulerpin, which binds with high energy. Caulerpin can be used as antibiotic against Vibrio anguillarum in fish aquaculture industry
cis-5-phosphonic acid pipecolic acid
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cysteine
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in the reverse reaction
D-Cystine
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70% inhibition at 0.01 mM, binds via the cysteine moiety covalently to the catalytic Cys135 of the enzyme, pH-dependent proces, optimal at pH 7.0-7.5, inhibition is reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione, no protection by aspartate-beta-semialdehyde, NADP+ or NADPH, inhibition mechanism and kinetics
dimethyl pyridine-2,5-dicarboxylate
DTNB
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reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione
GSSG
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oxidized glutathione
homocysteine
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in the reverse reaction
iodoacetamide
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at 0.1 mM: 45.4% inactivation in the absence of NADP+, 22% inactivation in the presence of 1 mM NADP+
L-2-Amino-4-oxo-5-chloropentanoic acid
L-cystine diethyl ester
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68% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione
L-cystine dimethyl ester
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67% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione
L-cystine hydroxamate
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20% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione
L-leucine
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inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.004 units in specific activity
methyl 5-nitropyridine-2-carboxylate
N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(1-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(2-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(2-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(2-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(3-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(3-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(4-biphenyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(4-bromobenzyl)-N-(2-carboxy)ethyl-3,4-dicarboxybenzylamine
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N-(4-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(4-carboxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(4-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(4-t-butylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-(ethylmorpholino)-N-carboxymethyl-3,4-dicarboxybenzylamine
N-acetal-N-carboxymethyl-3,4-dicarboxybenzylamine
N-acetonitrile, N-carboxymethyl-3,4-dicarboxybenzylamine
N-allyl, N-carboxymethyl-3,4-dicarboxybenzylamine
N-benzyl, N-carboxymethyl-3,4-dicarboxybenzylamine
N-carboxyethyl-3,4-dicarboxybenzylamine
N-carboxymethyl-3,4-dicarboxybenzylamine
N-methyl, N-carboxymethyl-3,4-dicarboxybenzylamine
NADPH-Tris-chloride buffer
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promotes a weak inactivation at 0°C, NADH protects
naphthalene-2,3-dialdehyde
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p-hydroxymercuribenzoate
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perrhenate
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very weak inhibitor
phosphonate
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weak inhibitor
pipecolic acid-5-(R)-phosphate hydrochloric acid
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pipecolic acid-5-(S)-phosphate hydrochloric acid
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potassium phosphate
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at a concentration of 10 mM promotes 60% inactivation at 0°C in the presence of 10 mM ATP, at a concentration of 100 mM promotes 61% inactivation in the presence of 10 mM ATP and 32% inactivation in the absence of ATP, NADH protects
S-methyl cysteine sulfoxide
inhibitor binding structure deduced from crystal structure
S-methyl-L-cysteine sulfoxide
covalently binding inhibitor via Cys134 at the active site, inactivation, inhibition and binding mechanism, reversible by addition of DTT or 2-mercaptoethanol
tetrachloro-1,4-benzoquinone
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thieno[2,3-b]thiophene-2,5-dicarboxylate
trans-5-phosphonic acid pipecolic acid
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(1R)-5-[(2-carboxyphenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
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(1R)-5-[(2-carboxyphenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
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(1R)-5-[(3-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
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(1R)-5-[(3-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
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(1R)-5-[(4-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
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(1R)-5-[(4-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
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(2R,3aR)-5-[(methylsulfonyl)methyl]-2,3,3a,4-tetrahydro-1H-indole-2-carboxylate
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(2R,3aR)-5-[(methylsulfonyl)methyl]-2,3,3a,4-tetrahydro-1H-indole-2-carboxylate
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(2R,5R)-2,3,4,5-tetrahydropyridine-2,5-dicarboxylate
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(2R,5R)-2,3,4,5-tetrahydropyridine-2,5-dicarboxylate
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(2R,5R)-5-nitro-2,3,4,5-tetrahydropyridine-2-carboxylate
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(2R,5R)-5-nitro-2,3,4,5-tetrahydropyridine-2-carboxylate
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(2R,7aR)-2,3,7,7a-tetrahydro-1H-indole-2,6-dicarboxylate
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(2R,7aR)-2,3,7,7a-tetrahydro-1H-indole-2,6-dicarboxylate
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(2R,7aR)-6-hydroxy-2,3,7,7a-tetrahydro-1H-indole-2-carboxylate
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(2R,7aR)-6-hydroxy-2,3,7,7a-tetrahydro-1H-indole-2-carboxylate
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(2R,7aR)-6-nitro-2,3,7,7a-tetrahydro-1H-indole-2-carboxylate
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(2R,7aR)-6-nitro-2,3,7,7a-tetrahydro-1H-indole-2-carboxylate
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(2R,8aR)-2,7-dinitro-1,2,8,8a-tetrahydronaphthalene
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(2R,8aR)-2,7-dinitro-1,2,8,8a-tetrahydronaphthalene
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(3aR)-2-oxo-2,3,3a,4-tetrahydro-1H-benzimidazole-5-carboxylic acid
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(3aR)-2-oxo-2,3,3a,4-tetrahydro-1H-benzimidazole-5-carboxylic acid
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(3aR)-5-nitro-1,3,3a,4-tetrahydro-2H-benzimidazol-2-one
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(3aR)-5-nitro-1,3,3a,4-tetrahydro-2H-benzimidazol-2-one
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(3aR)-5-nitro-3a,4-dihydro-1H-indene-1,3(2H)-dione
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(3aR)-5-nitro-3a,4-dihydro-1H-indene-1,3(2H)-dione
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(3aR)-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
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(3aR)-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
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(3aR)-6-chloro-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
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(3aR)-6-chloro-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
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(7aR)-2-oxo-2,3,7,7a-tetrahydro-1H-indole-6-carboxylate
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(7aR)-2-oxo-2,3,7,7a-tetrahydro-1H-indole-6-carboxylate
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(7aR)-3-(carboxylatomethyl)-6-nitro-7,7a-dihydro-1H-indole-2-carboxylate
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(7aR)-3-(carboxylatomethyl)-6-nitro-7,7a-dihydro-1H-indole-2-carboxylate
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2-Aminoadipate
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4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
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4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
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4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
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4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
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4-nitro-N,N-diethylbenzimidazolinone
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4-nitro-N,N-diethylbenzimidazolinone
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4-nitro-N,N-dimethylbenzimidazolinone
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4-nitro-N,N-dimethylbenzimidazolinone
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4-nitro-N-ethylphthalimide
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4-nitro-N-ethylphthalimide
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4-nitro-N-methylphthalimide
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4-nitro-N-methylphthalimide
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5-(carboxylatocarbonyl)-1H-pyrrole-2-carboxylate
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5-(carboxylatocarbonyl)-1H-pyrrole-2-carboxylate
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5-[[(4-nitrophenyl)amino]carbonyl]-1,3-benzenedimethylcarboxylate
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5-[[(4-nitrophenyl)amino]carbonyl]-1,3-benzenedimethylcarboxylate
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dimethyl pyridine-2,5-dicarboxylate
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dimethyl pyridine-2,5-dicarboxylate
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iodoacetate
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iodoacetate
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inhibition of arsenolysis, inhibition of the reduction of beta-aspartyl phosphate
iodoacetate
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at 1 mM: completely inhibits in the absence or presence of NADP+, at 0.1 mM: 3% inactivation in the absence of NADP+, 50% inactivation in the presence of 1 mM NADP+
L-2-Amino-4-oxo-5-chloropentanoic acid
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L-aspartate 4-semialdehyde protects the enzyme against inactivation, both NADP+ and NADPH decrease the rate of inactivation
L-2-Amino-4-oxo-5-chloropentanoic acid
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substrate analogue, irreversible inactivation, pseudo-first-order kinetics
L-cystine
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complete inhibition at 0.01 mM, binds via the cysteine moiety covalently to the catalytic Cys135 of the enzyme, pH-dependent process, optimal at pH 7.0-7.5, inhibition is reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione, no protection by aspartate-beta-semialdehyde, NADP+ or NADPH, inhibition mechanism and kinetics
L-cystine
inactivation, reversible by addition of DTT or 2-mercaptoethanol
L-isoleucine
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at 1 mM: 18% repression of enzyme synthesis, at 5 mM: 62% repression of enzyme synthesis
L-isoleucine
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inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.003 units in specific activity
L-lysine
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at 1 mM: 22% repression of the enzyme synthesis, at 5 mM: 44% repression of the enzyme synthesis, at 10 mM: 28% inhibition of the enzyme activity assayed in the reverse reaction
L-lysine
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enzyme assayed in the reverse reaction at pH 10
L-lysine
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slightly represses the enzyme
L-methionine
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at 1 mM: 40% repression of the enzyme synthesis, at 5 mM: 62% repression of the enzyme synthesis
L-methionine
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inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.004 units in specific activity
L-threonine
-
at 1 mM: 25% repression of the enzyme synthesis, at 5 mM: 43% repression of the enzyme synthesis, at 10 mM: 37% inhibition of the enzyme activity assayed in the reverse reaction
L-threonine
-
enzyme assayed in the reverse reaction at pH 10
L-threonine
-
represses the enzyme considerably
methyl 5-nitropyridine-2-carboxylate
-
-
methyl 5-nitropyridine-2-carboxylate
-
N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(1-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(1-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(3-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(3-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(3-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(3-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-biphenyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-biphenyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-carboxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-carboxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-t-butylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-t-butylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(ethylmorpholino)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-(ethylmorpholino)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-acetal-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-acetal-N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-acetonitrile, N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-acetonitrile, N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-allyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-allyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-benzyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-benzyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-carboxyethyl-3,4-dicarboxybenzylamine
-
-
N-carboxyethyl-3,4-dicarboxybenzylamine
-
-
N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
only 1 mol per subunit causes complete inactivation, at 0.1 mM: 91% inactivation in the absence of NADP+, 12% inactivation in the presence of 1 mM NADP+
N-methyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
N-methyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
-
petrosamine B
-
50% inhibition at 0.306 mM. Petrosamine B is a pyridoacridine alkaloid isolated from the sponge Oceanapia sp.; isolated from the methanol extract of the saustralian sponge Oceanapia sp.
petrosamine B
-
50% inhibition at 0.306 mM. Petrosamine B is a pyridoacridine alkaloid isolated from the sponge Oceanapia sp.
thieno[2,3-b]thiophene-2,5-dicarboxylate
-
-
thieno[2,3-b]thiophene-2,5-dicarboxylate
-
Tris salts
-
-
Tris salts
-
100 mM promotes 60.5% inactivation in the presence of 10 mM ATP and 17% inactivation in the absence of ATP
additional information
-
cytotoxicity analysis of inhibitors against Candida albicans cells, overview
-
additional information
-
-
-
additional information
-
not: chelating agents
-
additional information
-
no inhibition by N,N'-diacetyl-L-cystine, L-cystine di-beta-naphthylamide, disulfiram, N-acetyl-L-cystine, 2,2-dithiodipyridine, 4,4-dithiodipyridine, L- and D-cysteine, and oxidized and reduced coenzyme A
-
additional information
inhibitor binding structure and mechanism
-
additional information
molecular docking and simulation studies of the priority target, enzyme ASD, reveals the therapeutic potential of the ASD inhibitors based on selected natural products (huperzine A, rosmarinic acid, and curcumin), overview
-
additional information
-
no feed-back inhibition by threonine or methionine
-
additional information
-
-
-
additional information
-
the ASADH enzyme family shares the same substrate binding and active site catalytic groups, but the enzymes from representative bacterial and fungal species show different inhibition patterns when previously screened against low molecular weight inhibitors identified from fragment library screening. ASADH inhibitor development, overview
-
additional information
no inhibition by pathway endproducts amino acids threonine, methionine, lysine, and isoleucine
-
additional information
-
no inhibition by pathway endproducts amino acids threonine, methionine, lysine, and isoleucine
-
additional information
-
the ASADH enzyme family shares the same substrate binding and active site catalytic groups, but the enzymes from representative bacterial and fungal species show different inhibition patterns when previously screened against low molecular weight inhibitors identified from fragment library screening. ASADH inhibitor development, overview. No inhibition by 4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid, N-(4-bromobenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine , and N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
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0.11 - 0.18
(1R)-5-[(4-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
0.69 - 1.2
(2R,5R)-2,3,4,5-tetrahydropyridine-2,5-dicarboxylate
1.2 - 2.1
(2R,5R)-5-nitro-2,3,4,5-tetrahydropyridine-2-carboxylate
0.4 - 1.1
(3aR)-5-nitro-1,3,3a,4-tetrahydro-2H-benzimidazol-2-one
2.6 - 3.3
(3aR)-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
0.15 - 0.18
(3aR)-6-chloro-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
1.2
(S)-2-amino-5-fluoro-4-oxo-5-phosphono-pentanoic acid
0.2 M Tris, 1 mM EDTA, pH 8.6, 15 mM phosphate, 0.15 mM NADP+, 37°C
3.9
(S)-2-amino-5-phosphono-pent-4-ynoic acid
0.2 M Tris, 1 mM EDTA, pH 8.6, 15 mM phosphate, 0.15 mM NADP+, 37°C
0.062
1,4-Naphthoquinone
-
pH and temperature not specified in the publication
0.093
1-amino-2-naphthol-4-sulfonic acid
-
pH and temperature not specified in the publication
-
0.05
2'-phosphoribose AMP
-
-
0.00065
2,3-dichloro-1,4-naphthoquinone
-
pH and temperature not specified in the publication
0.0576
2,3-dichloro-5,6-dicyano-1,4-benzoquinone
-
pH and temperature not specified in the publication
0.0115
2,3-dichloro-5,8-dihydroxy-1,4-naphthoquinone
-
pH and temperature not specified in the publication
-
0.0061
2-bromo-1,4-naphthoquinone
-
pH and temperature not specified in the publication
-
0.0041
2-Chloro-1,4-naphthoquinone
-
pH and temperature not specified in the publication
0.04
3-Chloroacetylpyridine-adenine dinucleotide phosphate
-
competitive inhibitor with respect to NADP+
0.324 - 0.654
4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
0.296 - 0.609
4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
0.126
4-benzoquinone
pH 8.6, 25°C, recombinant enzyme
4
4-nitro-N,N-diethylbenzimidazolinone
0.086
4-nitro-N,N-dimethylbenzimidazolinone
4
4-nitro-N-ethylphthalimide
0.89 - 1.1
4-nitro-N-methylphthalimide
0.084
5-aminoisoquinoline
-
pH and temperature not specified in the publication
-
20
5-[[(4-nitrophenyl)amino]carbonyl]-1,3-benzenedimethylcarboxylate
0.121
catechol
-
pH and temperature not specified in the publication
0.154
cyclohexyl iodide
-
pH and temperature not specified in the publication
-
20
dimethyl pyridine-2,5-dicarboxylate
20
methyl 5-nitropyridine-2-carboxylate
0.476 - 1.1
N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.396 - 0.749
N-(1-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.529 - 0.737
N-(2-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.524 - 0.721
N-(2-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.329 - 0.724
N-(2-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.54 - 0.708
N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.509 - 0.727
N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.442 - 0.665
N-(3-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.43 - 0.69
N-(3-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.427 - 0.684
N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.441 - 0.678
N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.009 - 0.639
N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
0.012 - 0.634
N-(4-biphenyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
3.6
N-(4-bromobenzyl)-N-(2-carboxy)ethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.057 - 0.629
N-(4-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.229 - 0.649
N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.072 - 0.635
N-(4-carboxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.054 - 0.698
N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.063 - 0.608
N-(4-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.016 - 0.648
N-(4-t-butylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.036 - 0.663
N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.024 - 3.8
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.176 - 0.692
N-(ethylmorpholino)-N-carboxymethyl-3,4-dicarboxybenzylamine
0.276 - 0.655
N-acetal-N-carboxymethyl-3,4-dicarboxybenzylamine
0.22 - 0.498
N-acetonitrile, N-carboxymethyl-3,4-dicarboxybenzylamine
0.303 - 0.663
N-allyl, N-carboxymethyl-3,4-dicarboxybenzylamine
0.297 - 0.696
N-benzyl, N-carboxymethyl-3,4-dicarboxybenzylamine
2.4
N-carboxyethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.246 - 0.528
N-carboxymethyl-3,4-dicarboxybenzylamine
0.296 - 0.675
N-methyl, N-carboxymethyl-3,4-dicarboxybenzylamine
0.045
naphthalene-2,3-dialdehyde
-
pH and temperature not specified in the publication
-
0.073
p-benzoquinone
-
pH and temperature not specified in the publication
0.065
p-hydroquinone
-
pH and temperature not specified in the publication
0.063
phthalaldehyde
-
pH and temperature not specified in the publication
0.066
tetrachloro-1,4-benzoquinone
-
pH and temperature not specified in the publication
additional information
additional information
-
inhibition kinetics at 21°C and pH 7.5
-
0.11
(1R)-5-[(4-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.18
(1R)-5-[(4-nitrophenyl)carbamoyl]cyclohexa-3,5-diene-1,3-dicarboxylate
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.69
(2R,5R)-2,3,4,5-tetrahydropyridine-2,5-dicarboxylate
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
1.2
(2R,5R)-2,3,4,5-tetrahydropyridine-2,5-dicarboxylate
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
1.2
(2R,5R)-5-nitro-2,3,4,5-tetrahydropyridine-2-carboxylate
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
2.1
(2R,5R)-5-nitro-2,3,4,5-tetrahydropyridine-2-carboxylate
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.4
(3aR)-5-nitro-1,3,3a,4-tetrahydro-2H-benzimidazol-2-one
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
1.1
(3aR)-5-nitro-1,3,3a,4-tetrahydro-2H-benzimidazol-2-one
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
2.6
(3aR)-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
3.3
(3aR)-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.15
(3aR)-6-chloro-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.18
(3aR)-6-chloro-5-nitro-3a,4-dihydro-1H-isoindole-1,3(2H)-dione
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.324
4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
pH 8.6, 22°C
0.654
4-([[(1S)-1-carboxy-2-hydroxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
pH 8.6, 22°C
0.296
4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
pH 8.6, 22°C
0.609
4-([[(1S)-1-carboxyethyl]amino]methyl)benzene-1,2-dicarboxylic acid
-
pH 8.6, 22°C
4
4-nitro-N,N-diethylbenzimidazolinone
-
Ki above 4 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
4
4-nitro-N,N-diethylbenzimidazolinone
Ki above 4 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.086
4-nitro-N,N-dimethylbenzimidazolinone
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.086
4-nitro-N,N-dimethylbenzimidazolinone
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
4
4-nitro-N-ethylphthalimide
-
Ki above 4 mM in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
4
4-nitro-N-ethylphthalimide
Ki above 4 mM in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.89
4-nitro-N-methylphthalimide
-
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
1.1
4-nitro-N-methylphthalimide
in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
5-[[(4-nitrophenyl)amino]carbonyl]-1,3-benzenedimethylcarboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
5-[[(4-nitrophenyl)amino]carbonyl]-1,3-benzenedimethylcarboxylate
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
dimethyl pyridine-2,5-dicarboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
dimethyl pyridine-2,5-dicarboxylate
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
methyl 5-nitropyridine-2-carboxylate
-
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
20
methyl 5-nitropyridine-2-carboxylate
Ki above 20 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C
0.476
N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
1.1
N-((4-(2-benzyl)vinyl)benzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.396
N-(1-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.749
N-(1-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.529
N-(2-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.737
N-(2-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.524
N-(2-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.721
N-(2-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.329
N-(2-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.724
N-(2-naphthyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.54
N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.708
N-(2-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.509
N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.727
N-(2-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.442
N-(3-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.665
N-(3-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.43
N-(3-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.69
N-(3-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.427
N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.684
N-(3-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.441
N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.678
N-(3-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.009
N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.639
N-(4-(2-perfluoropropyl))-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.012
N-(4-biphenyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.634
N-(4-biphenyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.057
N-(4-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.629
N-(4-bromobenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.229
N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.649
N-(4-carboxamidebenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.072
N-(4-carboxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.635
N-(4-carboxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.054
N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.698
N-(4-difluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.063
N-(4-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.608
N-(4-methylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.016
N-(4-t-butylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.648
N-(4-t-butylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.036
N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.663
N-(4-trifluoromethoxybenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.024
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.628
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
3.8
N-(4-trifluoromethylbenzyl)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.176
N-(ethylmorpholino)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.692
N-(ethylmorpholino)-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.276
N-acetal-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.655
N-acetal-N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.22
N-acetonitrile, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.498
N-acetonitrile, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.303
N-allyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.663
N-allyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.297
N-benzyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.696
N-benzyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.246
N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.528
N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.296
N-methyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
0.675
N-methyl, N-carboxymethyl-3,4-dicarboxybenzylamine
-
pH 8.6, 22°C
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evolution
-
the ASADH enzyme family shares the same substrate binding and active site catalytic groups, but the enzymes from representative bacterial and fungal species show different inhibition patterns when previously screened against low molecular weight inhibitors identified from fragment library screening
evolution
-
the ASADH enzyme family shares the same substrate binding and active site catalytic groups, but the enzymes from representative bacterial and fungal species show different inhibition patterns when previously screened against low molecular weight inhibitors identified from fragment library screening
malfunction
deletion of the asdA gene precluded the growth of Edwardsiella ictaluri in absence of diaminopimelic acid
malfunction
-
enzyme deficiency or inhibition of enzyme activity leads to 80% reduced cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview
malfunction
-
the aspartate semialdehyde dehydrogenase (asd)-inactivated mutant exhibits significantly reduced growth in calf serum compared with the wild-type. The mutant also exhibits significantly reduced growth in medium, mimicking the concentrations of amino acids and glucose in calf serum, but can be recovered by addition of lysine and threonine
malfunction
-
enzyme deficiency or inhibition of enzyme activity leads to 80% reduced cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview
-
malfunction
-
the aspartate semialdehyde dehydrogenase (asd)-inactivated mutant exhibits significantly reduced growth in calf serum compared with the wild-type. The mutant also exhibits significantly reduced growth in medium, mimicking the concentrations of amino acids and glucose in calf serum, but can be recovered by addition of lysine and threonine
-
malfunction
-
deletion of the asdA gene precluded the growth of Edwardsiella ictaluri in absence of diaminopimelic acid
-
metabolism
-
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
-
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
-
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
-
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
the enzyme lies at the first branch point in the biosynthetic pathway of important amino acids including lysine and methionine and the cell-wall component diaminopimelate
metabolism
-
Asd is an essential enzyme for the biosynthesis of lysine, methionine, and threonine from aspartate
metabolism
-
aspartate-beta-semialdehyde dehydrogenase lies at the first branch point in the aspartate metabolic pathway which leads to the biosynthesis of several essential amino acids and some important metabolites. This pathway is crucial for many metabolic processes in plants and microbes like bacteria and fungi, but is absent in mammals
metabolism
-
aspartate-beta-semialdehyde dehydrogenase lies at the first branch point in the aspartate metabolic pathway which leads to the biosynthesis of several essential amino acids and some important metabolites. This pathway is crucial for many metabolic processes in plants and microbes like bacteria and fungi, but is absent in mammals
metabolism
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
metabolism
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
metabolism
the enzyme has a rate-limiting key function in the biosynthesis of amino acids L-threonine, L-lysine, and L-isoleucine from L-aspartate via L-homoserine
metabolism
mathematical modeling of the lysine metabolism in Mycobacterium tuberculosis strain H37Rv involving the enzyme, overview
metabolism
-
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
-
metabolism
-
the enzyme lies at the first branch point in the biosynthetic pathway of important amino acids including lysine and methionine and the cell-wall component diaminopimelate
-
metabolism
-
mathematical modeling of the lysine metabolism in Mycobacterium tuberculosis strain H37Rv involving the enzyme, overview
-
metabolism
-
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
-
metabolism
-
mathematical modeling of the lysine metabolism in Mycobacterium tuberculosis strain H37Rv involving the enzyme, overview
-
metabolism
-
Asd is an essential enzyme for the biosynthesis of lysine, methionine, and threonine from aspartate
-
physiological function
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
physiological function
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
physiological function
aspartate beta-semialdehyde dehydrogenase (ASADH) catalyzes the conversion of phosphoaspartate to aspartate beta-semialdehyde (L-ASA) via reductive dephosphorylation using NADPH as a cofactor
physiological function
-
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
-
physiological function
-
aspartate beta-semialdehyde dehydrogenase (ASADH) catalyzes the conversion of phosphoaspartate to aspartate beta-semialdehyde (L-ASA) via reductive dephosphorylation using NADPH as a cofactor
-
physiological function
-
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
-
additional information
active site structure analysis and comparison, detailed overview
additional information
-
active site structure analysis and comparison, detailed overview
additional information
The structure of CnASADH belongs to the Rossmann-fold superfamily of pyridine-linked dehydrogenases and shares the same overall monomeric structural features as the other ASADHs for which structures are determined
additional information
active site of FtASADH and NADP+ binding, structure analysis, overview
additional information
the nicotinamide moiety near the active site cysteine also places it in an optimal position for hydride transfer from NADPH to the enzyme-bound intermediate during the catalytic cycle
additional information
-
the nicotinamide moiety near the active site cysteine also places it in an optimal position for hydride transfer from NADPH to the enzyme-bound intermediate during the catalytic cycle
additional information
-
The structure of CnASADH belongs to the Rossmann-fold superfamily of pyridine-linked dehydrogenases and shares the same overall monomeric structural features as the other ASADHs for which structures are determined
-
additional information
-
active site of FtASADH and NADP+ binding, structure analysis, overview
-
additional information
-
active site structure analysis and comparison, detailed overview
-
additional information
-
the nicotinamide moiety near the active site cysteine also places it in an optimal position for hydride transfer from NADPH to the enzyme-bound intermediate during the catalytic cycle
-
additional information
-
the nicotinamide moiety near the active site cysteine also places it in an optimal position for hydride transfer from NADPH to the enzyme-bound intermediate during the catalytic cycle
-
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purified recombinant C-terminally His-tagged enzyme, hanging drop vapour diffusion method, crystallization screening, mixing of 0.001 ml protein solution plus 0.001 ml reservoir solution containing 1.9 M ammonium sulfate, 100 mM Bis-Tris, pH 6.5, at 20°C, crystals are either soaked or cocrystallized with 5 mM NADP+ and with several moderate inhibitors that are identified from fragment library screening, crystal cryoprotection with reservoir solution containing 20% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.8-3.2 A resolution, modeling by molecular replacement using CaASADH, PDB ID 3hsk, as the search model
purified recombinant His6-tagged enzyme free or in complex with NADP+ and inhibitor 4-benzoquinone, hanging drop vapor diffusion, mixing of 12 mg/ml protein solution with reservoir solution containing 0.2 M ammonium citrate, pH 7.0, and 18% PEG 3350, for inhibitor complexed crystals soaking in reservoir solution with added 15% v/v ethylene glycol and 5 mM NADP+, X-ray diffraction structure determination and analysis at 2.4-2.6 A resolution, molecular replacement using the structure of Candida albicans ASADH (PDB ID 3hsk) as the search model
hanging drop vapor diffusion method, using 20% (w/v) PEG 400, 0.1 M HEPES pH 6.5, 0.1 M MgCl2, at 20°C
purified recombinant C-terminally His-tagged enzyme, hanging drop vapour diffusion method, crystallization screening, mixing of 9 mg/ml protein solution with reservoir solution containing 10% PEG 8000, 6% ethylene glycol, 0.1 M HEPES pH 7.5, in a 2:1 ration, at 20°C, crystals are cocrystallized with 4 mM NADP+, X-ray diffraction structure determination and analysis at 2.6 A resolution, modeling by molecular replacement
enzyme in open and closed form, 30 mg/ml purified recombinant enzyme in 10 mM Tris, pH 7.4, 40 mM KCl, with equal volume of reservoir solution, 0.006 ml sitting drops by vapour diffusion utilizing micro-bridges, 20% v/v ethylene glycol, 4°C, X-ray diffraction structure determination and analysis at 1.95 A and 1.6 A resolution, respectively, modeling
using the hanging drop method
purified enzyme, X-ray diffractions structure determination and analysis at 2.45 A resolution
10 mg/ml purified recombinant wild-type and mutant enzymes free or in complex with the substrates, protein in 10 mM HEPES, pH 7.0, 1 mM EDTA, 1 mM DTT, by hanging drop vapour diffusion, 20°C, mixed with equal volume of precipitant solution containing 22-24% PEG 3350, and 0.2 M ammonium acetate, crystals are soaked for 1 h in a solution containing 2 mM aspartate-beta-semialdehyde or 100 mM phosphate, 26% PEG 3350, 0.2 M ammonium acetate, 0.1 M Tris-HCl, pH 8.5, and 20% glycerol, X-ray diffraction structure determination and analysis at about 2.0 A resolution
-
15 mg/ml purified recombinant enzyme, in 10 mM HEPES, pH 7.0, 1 mM EDTA, 1 mM DTT, crystallized as apoenzyme, as hemithioacetal, or as hemithioacetal structure with bound phosphate, hanging drop vapour diffusion method, 20°C, 1:1 mixture of protein solution and precipitant solution, the latter containing 24-28% PEG 3350, 0.2 M ammonium acetate, 0.1 M Tris, pH 8.5, overnight, substrate complexing by soaking of crystals in mother liquor with 50 mM potassium phosphate, crystals are frozen in precipitant solution with 20% glycerol added, X-ray diffraction structure determination and analysis at 2.0-2.15 A resolution, modeling
15 mg/ml purified recombinant wild-type enzyme in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, enzyme is free or complexed with substrates phosphate and/or asparate-beta-semialdehyde, hanging drop vapour diffusion method, 20°C, against an equal volume of precipitant solution containing 24-28% PEG 3350, 0.2 M ammonium acetate, and 0.1 M Tris-HCl, pH 8.5, soaking of crystals before harvest in 100 mM phosphate and 2 mM aspartate-beta-semialdehyde, crystallization of mutant H277N in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, by addition of precipitant solution containing 5 mM NADP+ and 5 mM inhibitor S-methyl-L-cysteine sulfoxide, 22% PEG 3350, 0.2 M ammonium acetate and 0.1 M sodium cacodylate, pH 6.5, X-ray diffraction structure determination and analysis at about 2.0 A resolution
about 10 mg/ml pure recombinant wild-type enzyme in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, complexed with oxyanions arsenate or periodate, hanging drop vapour diffusion method, 20°C, against an equal volume of precipitant solution containing 22-24% PEG 4000, 0.2 M ammonium acetate, and Tris-HCl, pH 8.5, soaking of crystals before harvest in a solution containing 26% PEG3350, 0.2 M ammonium acetate, 100 mM periodate or arsenate,0.1 M Tris-HCl, pH 8.5, and 20% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution
the structure of aspartate-beta-semialdehyde dehydrogenase has been determined to 2.3 A resolution using multiwavelength anomalous diffraction phasing of a seleno-methionine-substituted derivative
-
by using the hanging-drop vapour-diffusion method, crystallization in 2 different crystal forms, diffraction data analysis suggests the presence of up to four monomers in the asymmetric unit of the orthorhombic crystal form and of one or 2 monomers in the cubic crystal form
in complex with S-methyl-l-cysteine sulfoxide and sulfate, sitting drop vapor diffusion method, using 1.6 M ammonium sulfate and 100 mM citric acid pH 5.0
purified recombinant His-tagged enzyme, 9 mg/ml protein in 10 mM potassium phosphate buffer, pH 8.0, and 10 mM DTT, sitting drop vapour diffusion method, mixing of 500 nl of protein and of reservoir solution, the latter containing 1.6 M ammonium sulfate and 100 mM citric acid, pH 5.0, 2 days at 18°C, two different crystal forms, X-ray diffraction structure determination and analysis at 2.18-2.75 A resolution
crystallization of the apo-enzyme, in complex with NADP+, in complex with L-aspartate-beta-semialdehyde, in complex with NADP+ and L-aspartate-beta-semialdehyde
-
12 mg/ml purified recombinant enzyme free or in ternary complex with NADP+ and covalently bound inhibitor S-methyl-L-cysteine sulfoxide, protein in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, hanging drop vapour diffusion method, 20°C, with or without 5 mM NADP+ and 5 mM inhibitor, against an equal volume of precipitant solution: containing 18% PEG 3350, 0.2 M sodium acetate, and 0.1 M Tris, pH 8.5 for the free enzyme, or containing 22% PEG 3350, 0.2 M sodium acetate, and 0.1 M sodium citrate, pH 5.6 for the ternary complex, addition of 20% glycerol for crystal freezing, X-ray diffraction structure determination and analysis at 2.8 A and 1.84 A resolution, respectively
apoenzyme and enzyme in complex with substrate L-aspartate semialdehyde, method optimization, purified protein in 50 mM sodium citrate, pH 5.6, with 0.2 M ammonium acetate and 2 mM DTT via dialysis overnight, hanging drop vapour diffusion method, 4°C, diluted back into 100 mM Tris, pH 8.5, with 200 mM ammonium acetate and 5 mM DTT with 12 mg/ml protein, 0.001 ml protein solution is mixed with 0.001 ml of precipitant containing 0.1 M sodium citrate, pH 5.5-6.5, 5 mM DTT, 0.1-0.4 M ammonium acetate, and 24-27% PEG 8000, method optimization, overview, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution, molecular replacement method
-
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Shames, S.L.; Ash, D.E.; Wedler, F.C.; Villafranca, J.J.
Interaction of aspartate and aspartate-derived antimetabolites with the enzymes of the threonine biosynthetic pathway of Escherichia coli
J. Biol. Chem.
259
15331-15339
1984
Escherichia coli
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Aspartic semialdehyde dehydrogenase (Escherichia coli K12)
Methods Enzymol.
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708-713
1970
Escherichia coli
-
brenda
Cohen, G.N.
Aspartate-semialdehyde dehydrogenase from Escherichia coli
Methods Enzymol.
113
600-602
1985
Escherichia coli
brenda
Holland, M.J.; Westhead, E.W.
Purification and characterization of aspartic -semialdehyde dehydrogenase from yeast and purification of an isozyme of glyceraldehyde-3-phosphate dehydrogenase
Biochemistry
12
2264-2270
1973
Saccharomyces cerevisiae
brenda
Biellmann, J.F.; Eid, P.; Hirth, C.; Jrnvall, H.
Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Purification and general properties
Eur. J. Biochem.
104
53-58
1980
Escherichia coli
brenda
Bielmann, J.F.; Eid, P.; Hirth, C.
Affinity labeling of the Escherichia coli aspartate-beta-semialdehyde dehydrogenase with an alkylating coenzyme analogue. Half-site reactivity and competition with the substrate alkylating analogue
Eur. J. Biochem.
104
65-69
1980
Escherichia coli
brenda
Biellmann, J.F.; Eid, P.; Hirth, C.; Jrnvall, H.
Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Affinity labeling with the substrate analogue L-2-amino-4-oxo-5-chloropentanoic acid: an example of half-site reactivity
Eur. J. Biochem.
104
59-64
1980
Escherichia coli
brenda
Jenkins, M.B.; Garner, H.R.
Studies of a homoserineless bradytroph of Neurospora crassa: demonstration of an altered aspartate beta-semialdehyde dehydrogenase
Biochim. Biophys. Acta
141
287-295
1967
Neurospora crassa
brenda
Surdin, Y.
Semi-aldehyde aspartic dehydrogenase of Saccharomyces cerevisiae: properties and regulation
Eur. J. Biochem.
2
341-348
1967
Saccharomyces cerevisiae
brenda
Black, S.; Wright, N.G.
Aspartic beta-semialdehyde dehydrogenase and aspartic beta-semialdehyde
J. Biol. Chem.
213
39-50
1955
Saccharomyces cerevisiae
brenda
Thomas, D.; Surdin-Kerjan, Y.
Structure of the HOM2 gene of Saccharomyces cerevisiae and regulation of its expression
Mol. Gen. Genet.
217
149-154
1989
Saccharomyces cerevisiae
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Jagusztyn, E.K.; Malaszewska-Keough, A.; Kauc, B.
Cloning and expression of Thiobacillus versutus aspartate-semialdehyde gene in Escherichia coli
FEMS Microbiol. Lett.
59
21-26
1989
Paracoccus versutus
-
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Preiss, J.; Mazelis, M.; Greenberg, E.
Cloning of the aspartate-beta-semialdehyde dehydrogenase structural gene from Escherichia coli K12
Curr. Microbiol.
7
263-268
1982
Escherichia coli
-
brenda
Jagusztyn-Krynicka, E.K.; Smorawinska, M.; Curtiss III, R.
Expression of Streptococcus mutans aspartate-semialdehyde dehydrogenase gene cloned into plasmid pBR322
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128
1135-1145
1982
Streptococcus mutans
brenda
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Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum
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1988
Corynebacterium glutamicum
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Regulation of the enzymes of lysine biosynthesis in Bacillus sphaericus NCTC 9602 during vegetative growth
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132
3169-3177
1986
Lysinibacillus sphaericus
-
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Chatterjee, M.; Chatterjee, S.P.; White, P.J.
The mechanism of threonine inhibition of growth and lysine production of Micrococcus luteus 236b
FEMS Microbiol. Lett.
12
163-166
1981
Micrococcus luteus
-
brenda
Holland, M.J.; Westhead, E.W.
Chemical reactivity at the catalytic sites of aspartic -semialdehyde dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase
Biochemistry
12
2276-2281
1973
Saccharomyces cerevisiae
brenda
Holland, M.J.; Westhead, E.W.
Adenosine 5-triphosphate induced cold inactivation of yeast aspartic -semialdehyde dehydrogenase
Biochemistry
12
2270-2275
1973
Saccharomyces cerevisiae
brenda
Hadfield, A.; Kryger, G.; Ouyang, J.; Petsko, G.A.; Ringe, D.; Viola, R.
Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis
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289
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1999
Escherichia coli (P0A9Q9), Escherichia coli
brenda
Kish, M.M.; Viola, R.E.
Oxyanion specificity of L-Aspartate-beta-semialdehyde dehydrogenase
Inorg. Chem.
38
818-820
1999
Escherichia coli
brenda
Zhang, W.W.; Jiang, W.H.; Zhao, G.P.; Yang, Y.L.; Chiao, J.S.
Expression in Escherichia coli, purification and kinetic analysis of the aspartokinase and aspartate semialdehyde dehydrogenase from the rifamycin SV-producing Amycolatopsis mediterranei U32
Appl. Microbiol. Biotechnol.
54
52-58
2000
Amycolatopsis mediterranei U32
brenda
Moore, R.A.; Bocik, W.E.; Viola, R.E.
Expression and purification of aspartate beta-semialdehyde dehydrogenase from infectious microorganisms
Protein Expr. Purif.
25
189-194
2002
Haemophilus influenzae, Helicobacter pylori (O25801), Helicobacter pylori, Vibrio cholerae (P23247), Vibrio cholerae, Pseudomonas aeruginosa (Q51344), Pseudomonas aeruginosa
brenda
Paris, S.; Wessel, P.M.; Dumas, R.
Overproduction, purification, and characterization of recombinant aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
Protein Expr. Purif.
24
99-104
2002
Arabidopsis thaliana (Q9FVC4), Arabidopsis thaliana
brenda
Blanco, J.; Moore, R.A.; Faehnle, C.R.; Coe, D.M.; Viola, R.E.
The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase
Acta Crystallogr. Sect. D
60
1388-1395
2004
Haemophilus influenzae
brenda
Blanco, J.; Moore, R.A.; Faehnle, C.R.; Viola, R.E.
Critical catalytic functional groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase
Acta Crystallogr. Sect. D
60
1808-1815
2004
Haemophilus influenzae (P44801), Haemophilus influenzae
brenda
Faehnle, C.R.; Blanco, J.; Viola, R.E.
Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-beta-semialdehyde dehydrogenase
Acta Crystallogr. Sect. D
60
2320-2324
2004
Haemophilus influenzae (P44801)
brenda
Alvarez, E.; Ramon, F.; Magan, C.; Diez, E.
L-cystine inhibits aspartate-beta-semialdehyde dehydrogenase by covalently binding to the essential 135Cys of the enzyme
Biochim. Biophys. Acta
1696
23-29
2004
Escherichia coli
brenda
Shafiani, S.; Sharma, P.; Vohra, R.M.; Tewari, R.
Cloning and characterization of aspartate-beta-semialdehyde dehydrogenase from Mycobacterium tuberculosis H37 Rv
J. Appl. Microbiol.
98
832-838
2005
Mycobacterium tuberculosis (P9WNX5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNX5), Mycobacterium tuberculosis H37Rv
brenda
Nichols, C.E.; Dhaliwal, B.; Lockyer, M.; Hawkins, A.R.; Stammers, D.K.
High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase
J. Mol. Biol.
341
797-806
2004
Escherichia coli (P0A9Q9), Escherichia coli
brenda
Blanco, J.; Moore, R.A.; Viola, R.E.
Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase
Proc. Natl. Acad. Sci. USA
100
12613-12617
2003
no activity in Homo sapiens, Haemophilus influenzae (P44801), Haemophilus influenzae
brenda
Blanco, J.; Moore, R.A.; Kabaleeswaran, V.; Viola, R.E.
A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae
Protein Sci.
12
27-33
2003
Vibrio cholerae (Q9KQG2), Vibrio cholerae
brenda
Tunca, S.; Yilmaz, E.I.; Piret, J.; Liras, P.; Ozcengiz, G.
Cloning, characterization and heterologous expression of the aspartokinase and aspartate semialdehyde dehydrogenase genes of cephamycin C-producer Streptomyces clavuligerus
Res. Microbiol.
155
525-534
2004
Streptomyces clavuligerus (Q8KQ27), Streptomyces clavuligerus, Streptomyces clavuligerus NRRL 3585 (Q8KQ27)
brenda
Cahyanto, M.N.; Kawasaki, H.; Nagashio, M.; Fujiyama, K.; Seki, T.
Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarum
Microbiology
152
105-112
2006
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum NCIMB 8826
brenda
Cox, R.J.; Gibson, J.S.; Hadfield, A.T.
Design, synthesis and analysis of inhibitors of bacterial aspartate semialdehyde dehydrogenase
ChemBiochem
6
2255-2260
2005
Bacteria, Escherichia coli (P0A9Q9)
brenda
Faehnle, C.R.; Le Coq, J.; Liu, X.; Viola, R.E.
Examination of key intermediates in the catalytic cycle of aspartate-beta-semialdehyde dehydrogenase from a gram-positive infectious bacteria
J. Biol. Chem.
281
31031-31040
2006
Streptococcus pneumoniae
brenda
Faehnle, C.R.; Ohren, J.F.; Viola, R.E.
A new branch in the family: structure of aspartate-beta-semialdehyde dehydrogenase from Methanococcus jannaschii
J. Mol. Biol.
353
1055-1068
2005
Methanocaldococcus jannaschii
brenda
Carroll, A.R.; Ngo, A.; Quinn, R.J.; Redburn, J.; Hooper, J.N.
Petrosamine B, an inhibitor of the Helicobacter pylori enzyme aspartyl semialdehyde dehydrogenase from the Australian sponge Oceanapia sp
J. Nat. Prod.
68
804-806
2005
Helicobacter pylori
brenda
Viola, R.E.; Liu, X.; Ohren, J.F.; Faehnle, C.R.
The structure of a redundant enzyme: a second isoform of aspartate beta-semialdehyde dehydrogenase in Vibrio cholerae
Acta Crystallogr. Sect. D
D64
321-330
2008
Vibrio cholerae serotype O1
brenda
Vyas, R.; Kumar, V.; Panjikar, S.; Karthikeyan, S.; Kishan, K.V.; Tewari, R.; Weiss, M.S.
Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
64
167-170
2008
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WNX5), Mycobacterium tuberculosis H37Rv (P9WNX5)
brenda
Cahyanto, M.N.; Kawasaki, H.; Nagashio, M.; Fujiyama, K.; Seki, T.
Construction of Lactobacillus plantarum strain with enhanced L-lysine yield
J. Appl. Microbiol.
102
674-679
2007
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum IAM 12477
brenda
Singh, A.; Kushwaha, H.R.; Sharma, P.
Molecular modelling and comparative structural account of aspartyl beta-semialdehyde dehydrogenase of Mycobacterium tuberculosis (H37Rv)
J. Mol. Model.
14
249-263
2008
Mycobacterium tuberculosis (P9WNX5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNX5)
brenda
Arachea, B.T.; Liu, X.; Pavlovsky, A.G.; Viola, R.E.
Expansion of the aspartate beta-semialdehyde dehydrogenase family: the first structure of a fungal ortholog
Acta Crystallogr. Sect. D
66
205-212
2010
Candida albicans (Q5ALM0)
brenda
Vyas, R.; Tewari, R.; Weiss, M.S.; Karthikeyan, S.
Structures of ternary complexes of aspartate-semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. D
68
671-679
2012
Mycobacterium tuberculosis (P9WNX5), Mycobacterium tuberculosis H37Rv (P9WNX5), Mycobacterium tuberculosis H37Rv
brenda
Luniwal, A.; Wang, L.; Pavlovsky, A.; Erhardt, P.W.; Viola, R.E.
Molecular docking and enzymatic evaluation to identify selective inhibitors of aspartate semialdehyde dehydrogenase
Bioorg. Med. Chem.
20
2950-2956
2012
Streptococcus pneumoniae, Vibrio cholerae (Q9KQG2), Vibrio cholerae
brenda
Viola, R.E.; Faehnle, C.R.; Blanco, J.; Moore, R.A.; Liu, X.; Arachea, B.T.; Pavlovsky, A.G.
The catalytic machinery of a key enzyme in amino acid biosynthesis
J. Amino Acids
2011
352538
2011
Candida albicans, Streptococcus pneumoniae, Escherichia coli, Methanocaldococcus jannaschii, Haemophilus influenzae (P44801), Vibrio cholerae (Q9KQG2)
brenda
Evitt, A.S.; Cox, R.J.
Synthesis and evaluation of conformationally restricted inhibitors of aspartate semialdehyde dehydrogenase
Mol. Biosyst.
7
1564-1575
2011
Salmonella enterica
brenda
Santander, J.; Xin, W.; Yang, Z.; Curtiss, R.
The aspartate-semialdehyde dehydrogenase of Edwardsiella ictaluri and its use as balanced-lethal system in fish vaccinology
PLoS ONE
5
e15944
2010
Edwardsiella ictaluri (C5BB06), Edwardsiella ictaluri, Edwardsiella ictaluri 93-146 (C5BB06)
brenda
Dahal, G.; Viola, R.E.
Structure of a fungal form of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans
Acta Crystallogr. Sect. F
71
1365-1371
2015
Cryptococcus neoformans var. neoformans (Q5KPK7), Cryptococcus neoformans var. neoformans ATCC MYA-565 (Q5KPK7)
brenda
Dahal, G.P.; Viola, R.E.
Structure of a fungal form of aspartate-semialdehyde dehydrogenase from Aspergillus fumigatus
Acta Crystallogr. Sect. F
73
36-44
2017
Aspergillus fumigatus (Q4WWR8), Aspergillus fumigatus, Aspergillus fumigatus ATCC MYA-4609 (Q4WWR8), no activity in Homo sapiens
brenda
Oogai, Y.; Yamaguchi, M.; Kawada-Matsuo, M.; Sumitomo, T.; Kawabata, S.; Komatsuzawa, H.
Lysine and threonine biosynthesis from aspartate contributes to Staphylococcus aureus growth in calf serum
Appl. Environ. Microbiol.
82
6150-6157
2016
Staphylococcus aureus, Staphylococcus aureus MW2
brenda
Thangavelu, B.; Bhansali, P.; Viola, R.E.
Elaboration of a fragment library hit produces potent and selective aspartate semialdehyde dehydrogenase inhibitors
Bioorg. Med. Chem.
23
6622-6631
2015
Streptococcus pneumoniae, Vibrio cholerae serotype O1
brenda
Xu, X.; Chen, J.; Wang, Q.; Duan, C.; Li, Y.; Wang, R.; Yang, S.
Mutagenesis of key residues in the binding center of L-aspartate-beta-semialdehyde dehydrogenase from Escherichia coli enhances utilization of the cofactor NAD(H)
ChemBioChem
17
56-64
2016
Escherichia coli (P0A9Q9), Escherichia coli
brenda
Meng, J.; Yang, Y.; Xiao, C.; Guan, Y.; Hao, X.; Deng, Q.; Lu, Z.
Identification and validation of aspartic acid semialdehyde dehydrogenase as a new anti-Mycobacterium tuberculosis target
Int. J. Mol. Sci.
16
23572-23586
2015
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Subramani, P.; Mahendran, R.; Michael, R.
Molecular docking and dynamics simulation of Vibrio anguillarum aspartate semialdehyde dehydrogenase with natural product caulerpin
Lett. Drug Design Disc.
13
255-261
2016
Vibrio anguillarum
-
brenda
Mank, N.; Pote, S.; Majorek, K.; Arnette, A.; Klapper, V.; Hurlburt, B.; Chruszcz, M.
Structure of aspartate beta-semialdehyde dehydrogenase from Francisella tularensis
Acta Crystallogr. Sect. F
74
14-22
2018
Francisella tularensis subsp. tularensis (Q5NHM4), Francisella tularensis subsp. tularensis Schu 4 (Q5NHM4)
brenda
Dahal, G.P.; Viola, R.E.
Structural insights into inhibitor binding to a fungal ortholog of aspartate semialdehyde dehydrogenase
Biochem. Biophys. Res. Commun.
503
2848-2854
2018
Blastomyces dermatitidis (C5GC63), Blastomyces dermatitidis, Blastomyces dermatitidis ER-3 (C5GC63), Blastomyces dermatitidis ATCC MYA-2586 (C5GC63)
brenda
Dahal, G.P.; Launder, D.; McKeone, K.M.M.; Hunter, J.P.; Conti, H.R.; Viola, R.E.
Aspartate semialdehyde dehydrogenase inhibition suppresses the growth of the pathogenic fungus Candida albicans
Drug Dev. Res.
81
736-744
2020
Candida albicans, Candida albicans CAF2-1
brenda
Khan, S.; Somvanshi, P.; Bhardwaj, T.; Mandal, R.K.; Dar, S.A.; Wahid, M.; Jawed, A.; Lohani, M.; Khan, M.; Areeshi, M.Y.; Haque, S.
Aspartate-beta-semialdeyhyde dehydrogenase as a potential therapeutic target of Mycobacterium tuberculosis H37Rv Evidence from in silico elementary mode analysis of biological network model
J. Cell. Biochem.
119
2832-2842
2018
Mycobacterium tuberculosis (P9WNX5), Mycobacterium tuberculosis H37Rv (P9WNX5), Mycobacterium tuberculosis ATCC 25618 (P9WNX5)
brenda