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
Synonyms
GAPN, More, NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD+-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, non-phosphorylating Ga3PDHase, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, nonphosphorylating NAD+-dependent GAPN
ECTree
1.2.1.90 glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]Advanced search results
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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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O
3-phospho-D-glycerate + NAD(P)H + 2 H+
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical EmbdenÂMeyerhofÂParnas 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 EmbdenÂMeyerhofÂParnas 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 EmbdenÂMeyerhofÂParnas 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
L-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-L-glycerate + NADH + 2 H+
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ir
L-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-L-glycerate + NADPH + 2 H+
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-
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ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
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-
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ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
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-
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ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
part of the modified Emden-Meyerhof-Parnas pathway in Thermoproteus tenax
-
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ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
the enzyme is part of the modified EmbdenÂMeyerhofÂParnas pathway, the main route for carbohydrate metabolism in Thermoproteus tenax
-
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ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
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
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
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ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
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
additional information
?
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
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additional information
?
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-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
-
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-
additional information
?
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
-
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-
additional information
?
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
-
-
-
additional information
?
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
-
-
-
additional information
?
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
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