Cloned (Comment) | Organism |
---|---|
gene gapD, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) | Nitrosomonas europaea |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.003 | - |
succinate semialdehyde | pH 8.5, 30°C, recombinant enzyme, with NADP+ | Nitrosomonas europaea | |
0.004 | - |
NADP+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea | |
0.007 | - |
succinate semialdehyde | pH 8.5, 30°C, recombinant enzyme, with NAD+ | Nitrosomonas europaea | |
1.12 | - |
NAD+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
succinate semialdehyde + NAD+ + H2O | Nitrosomonas europaea | - |
succinate + NADH + 2 H+ | - |
? | |
succinate semialdehyde + NAD+ + H2O | Nitrosomonas europaea NBRC 14298 | - |
succinate + NADH + 2 H+ | - |
? | |
succinate semialdehyde + NAD+ + H2O | Nitrosomonas europaea ATCC 19718 | - |
succinate + NADH + 2 H+ | - |
? | |
succinate semialdehyde + NAD+ + H2O | Nitrosomonas europaea KCTC 2705 | - |
succinate + NADH + 2 H+ | - |
? | |
succinate semialdehyde + NAD+ + H2O | Nitrosomonas europaea CIP 103999 | - |
succinate + NADH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | Nitrosomonas europaea | - |
succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | Nitrosomonas europaea NBRC 14298 | - |
succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | Nitrosomonas europaea ATCC 19718 | - |
succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | Nitrosomonas europaea KCTC 2705 | - |
succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | Nitrosomonas europaea CIP 103999 | - |
succinate + NADPH + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nitrosomonas europaea | Q82TA7 | - |
- |
Nitrosomonas europaea ATCC 19718 | Q82TA7 | - |
- |
Nitrosomonas europaea CIP 103999 | Q82TA7 | - |
- |
Nitrosomonas europaea KCTC 2705 | Q82TA7 | - |
- |
Nitrosomonas europaea NBRC 14298 | Q82TA7 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Nitrosomonas europaea |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. 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+. Preference for NADP+ when SSA is the substrate | Nitrosomonas europaea | ? | - |
- |
|
additional information | the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. 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+. Preference for NADP+ when SSA is the substrate | Nitrosomonas europaea NBRC 14298 | ? | - |
- |
|
additional information | the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. 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+. Preference for NADP+ when SSA is the substrate | Nitrosomonas europaea ATCC 19718 | ? | - |
- |
|
additional information | the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. 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+. Preference for NADP+ when SSA is the substrate | Nitrosomonas europaea KCTC 2705 | ? | - |
- |
|
additional information | the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. 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+. Preference for NADP+ when SSA is the substrate | Nitrosomonas europaea CIP 103999 | ? | - |
- |
|
succinate semialdehyde + NAD+ + H2O | - |
Nitrosomonas europaea | succinate + NADH + 2 H+ | - |
? | |
succinate semialdehyde + NAD+ + H2O | - |
Nitrosomonas europaea NBRC 14298 | succinate + NADH + 2 H+ | - |
? | |
succinate semialdehyde + NAD+ + H2O | - |
Nitrosomonas europaea ATCC 19718 | succinate + NADH + 2 H+ | - |
? | |
succinate semialdehyde + NAD+ + H2O | - |
Nitrosomonas europaea KCTC 2705 | succinate + NADH + 2 H+ | - |
? | |
succinate semialdehyde + NAD+ + H2O | - |
Nitrosomonas europaea CIP 103999 | succinate + NADH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | - |
Nitrosomonas europaea | succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | NADP+ is the preferred cofactor | Nitrosomonas europaea | succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | - |
Nitrosomonas europaea NBRC 14298 | succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | NADP+ is the preferred cofactor | Nitrosomonas europaea NBRC 14298 | succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | - |
Nitrosomonas europaea ATCC 19718 | succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | NADP+ is the preferred cofactor | Nitrosomonas europaea ATCC 19718 | succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | - |
Nitrosomonas europaea KCTC 2705 | succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | NADP+ is the preferred cofactor | Nitrosomonas europaea KCTC 2705 | succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | - |
Nitrosomonas europaea CIP 103999 | succinate + NADPH + 2 H+ | - |
? | |
succinate semialdehyde + NADP+ + H2O | NADP+ is the preferred cofactor | Nitrosomonas europaea CIP 103999 | succinate + NADPH + 2 H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | see also EC 1.2.1.90 | Nitrosomonas europaea |
SSA dehydrogenase | - |
Nitrosomonas europaea |
SSADHase | - |
Nitrosomonas europaea |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Nitrosomonas europaea |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.45 | - |
NAD+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea | |
0.483 | - |
succinate semialdehyde | pH 8.5, 30°C, recombinant enzyme, with NAD+ | Nitrosomonas europaea | |
0.583 | - |
succinate semialdehyde | pH 8.5, 30°C, recombinant enzyme, with NADP+ | Nitrosomonas europaea | |
0.617 | - |
NADP+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
assay at | Nitrosomonas europaea |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the Km value for NADP+ is 26fold higher than that for NAD+. The Km value for SSA increases 3fold with NADP+ in comparison with NAD+ | Nitrosomonas europaea | |
NAD+ | - |
Nitrosomonas europaea | |
NADP+ | preferred cofactor | Nitrosomonas europaea |
General Information | Comment | Organism |
---|---|---|
physiological function | enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase (EC 1.2.1.90). But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase). As an SSADHase, GabD physiologically acts producing succinate and preferentially NADPH over NADH, thus being part of an alternative pathway of the tricarboxylic acid cycle converting alpha-ketoglutarate to succinate | Nitrosomonas europaea |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.4 | - |
NAD+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea | |
70.4 | - |
succinate semialdehyde | pH 8.5, 30°C, recombinant enzyme, with NAD+ | Nitrosomonas europaea | |
154.3 | - |
NADP+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea | |
194.3 | - |
succinate semialdehyde | pH 8.5, 30°C, recombinant enzyme, with NADP+ | Nitrosomonas europaea |