EC Number   |
Substrates |
Organism |
Products |
Reversibility  |
|---|
   1.2.1.90 | more |
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 |
Nitrosomonas europaea |
? |
- |
- |
| 1.2.1.90 | more |
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 |
Nitrosomonas europaea NBRC 14298 |
? |
- |
- |
| 1.2.1.90 | more |
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 |
Nitrosomonas europaea ATCC 19718 |
? |
- |
- |
| 1.2.1.90 | more |
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 |
Nitrosomonas europaea KCTC 2705 |
? |
- |
- |
| 1.2.1.90 | more |
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 |
Nitrosomonas europaea CIP 103999 |
? |
- |
- |
| 1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O |
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 |
Thermoproteus tenax |
3-phospho-D-glycerate + NAD(P)H + 2 H+ |
- |
ir |
| 1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
- |
Thermoproteus tenax |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
| 1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
- |
Nitrosomonas europaea |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
| 1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
part of the modified Emden-Meyerhof-Parnas pathway in Thermoproteus tenax |
Thermoproteus tenax |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
| 1.2.1.90 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
the enzyme is part of the modified EmbdenÂMeyerhofÂParnas pathway, the main route for carbohydrate metabolism in Thermoproteus tenax |
Thermoproteus tenax |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
