1.2.1.90: glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]

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

Reaction

D-glyceraldehyde 3-phosphate
+
NAD(P)+
+
H2O
=
3-phospho-D-glycerate
+
NAD(P)H
+ 2 H+

Synonyms

GAPN, NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD+-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, nonphosphorylating NAD+-dependent GAPN

ECTree

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

Substrates Products

Substrates Products on EC 1.2.1.90 - glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]

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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O
3-phospho-D-glycerate + NAD(P)H + 2 H+
show the reaction diagram
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical Embden–Meyerhof–Parnas glycolysis, as found in Eucarya and Bacteria, the oxidation of D-glyceraldehyde 3-phosphate is coupled to phosphorylation to yield 1,3-diphosphoglycerate, which in turn is utilized by phosphoglycerate kinase giving 3-phosphoglycerate and ATP. These steps are reversible and non-regulated in the common Embden–Meyerhof–Parnas pathway. In contrast, the direct and irreversible oxidation of D-glyceraldehyde 3-phosphate to 3-phospho-D-glycerate without production of ATP is catalysed either by non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase or by glyceraldehyde-3-phosphate ferredoxin oxidoreductase (EC 1.2.7.6). The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase/glyceraldehyde-3-phosphate ferredoxin oxidoreductase substitution in the catabolic Embden–Meyerhof–Parnas pathway avoids the production of the highly thermolabile compound 1,3-diphosphoglycerate and could minimize the pools of the thermolabile intermediates D-glyceraldehyde 3-phosphate and dihydroxyacetonphosphate by driving the carbon flow down the pathway and thus reducing the velocity of their heat destruction
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-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
show the reaction diagram
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
show the reaction diagram
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3
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ir