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1.2.1.59: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

This is an abbreviated version!
For detailed information about glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating), go to the full flat file.

Word Map on EC 1.2.1.59

Reaction

D-glyceraldehyde 3-phosphate
+
phosphate
+
NAD(P)+
=
3-phospho-D-glyceroyl phosphate
+
NAD(P)H
+
H+

Synonyms

cgap, chloroplast glyceraldehyde-3-phosphate dehydrogenase, CjGAPDH, Dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide (phosphate)), GAP, GapA, GapB, GAPC, GAPDH, GAPDH2, GBS GAPDH, glyceraldehyde 3-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)), NAD(NADP)-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD(P)-dependent G3P dehydrogenase, NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase, NADP-dependent glyceraldehyde 3-phosphate dehydrogenase, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase, NADP-dependent glyceraldehydephosphate dehydrogenase, pcal_0632, phosphorylating glyceraldehyde-3-phosphate dehydrogenase, STK_13560, Triosephosphate dehydrogenase (NAD(P)), Tsac_2486

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.59 glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

Engineering

Engineering on EC 1.2.1.59 - glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C150S
D35G
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is 3fold lower than with NAD+
D35G/L36R/P192S
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency
D35G/L36T/T37K
site-directed mutagenesis, introducing a third mutation T37K into the mutant D35G/L36T completely reverses the coenzyme specificity of the enzyme
D35G/L36T/T37K/P192S
site-directed mutagenesis, the mutant shows high catalytic efficiency with NADP+ while the catalytic efficiency with NAD+ also increases. The replacement of Pro192 to Ser benefits the binding affinity of both NAD+ and NADP+
L36T
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is lower than with NAD+
D35G
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is 3fold lower than with NAD+
-
D35G/L36R/P192S
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency
-
D35G/L36T/T37K
-
site-directed mutagenesis, introducing a third mutation T37K into the mutant D35G/L36T completely reverses the coenzyme specificity of the enzyme
-
L36T
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is lower than with NAD+
-
D35G
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is 3fold lower than with NAD+
-
D35G/L36R/P192S
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency
-
D35G/L36T/T37K
-
site-directed mutagenesis, introducing a third mutation T37K into the mutant D35G/L36T completely reverses the coenzyme specificity of the enzyme
-
L36T
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is lower than with NAD+
-
additional information