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 |
---|---|---|---|---|---|
0.23 | - |
NADP+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea | |
0.4 | - |
NAD+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea | |
1.9 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant enzyme, with NADP+ | Nitrosomonas europaea | |
2.2 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant enzyme, with NAD+ | Nitrosomonas europaea | |
3 | - |
L-Glyceraldehyde 3-phosphate | about, pH 8.5, 30°C, recombinant enzyme, with NADP+ | Nitrosomonas europaea |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + NAD+ + H2O | Nitrosomonas europaea | - |
3-phospho-D-glycerate + NADH + 2 H+ | - |
ir | |
D-glyceraldehyde 3-phosphate + NADP+ + H2O | Nitrosomonas europaea | - |
3-phospho-D-glycerate + NADPH + 2 H+ | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nitrosomonas europaea | Q82TA7 | cf. EC 1.2.1.16 | - |
Nitrosomonas europaea ATCC 19718 | Q82TA7 | cf. EC 1.2.1.16 | - |
Nitrosomonas europaea CIP 103999 | Q82TA7 | cf. EC 1.2.1.16 | - |
Nitrosomonas europaea KCTC 2705 | Q82TA7 | cf. EC 1.2.1.16 | - |
Nitrosomonas europaea NBRC 14298 | Q82TA7 | cf. EC 1.2.1.16 | - |
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. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + NAD+ + H2O | - |
Nitrosomonas europaea | 3-phospho-D-glycerate + NADH + 2 H+ | - |
ir | |
D-glyceraldehyde 3-phosphate + NADP+ + H2O | - |
Nitrosomonas europaea | 3-phospho-D-glycerate + NADPH + 2 H+ | - |
ir | |
L-glyceraldehyde 3-phosphate + NAD+ + H2O | - |
Nitrosomonas europaea | 3-phospho-L-glycerate + NADH + 2 H+ | - |
ir | |
L-glyceraldehyde 3-phosphate + NADP+ + H2O | - |
Nitrosomonas europaea | 3-phospho-L-glycerate + NADPH + 2 H+ | - |
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 | Nitrosomonas europaea | ? | - |
- |
|
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 | Nitrosomonas europaea NBRC 14298 | ? | - |
- |
|
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 | Nitrosomonas europaea ATCC 19718 | ? | - |
- |
|
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 | Nitrosomonas europaea KCTC 2705 | ? | - |
- |
|
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 | Nitrosomonas europaea CIP 103999 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
More | see also EC 1.2.1.16 | Nitrosomonas europaea |
non-phosphorylating Ga3PDHase | - |
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 |
---|---|---|---|---|---|
0.007 | - |
L-Glyceraldehyde 3-phosphate | about, pH 8.5, 30°C, recombinant enzyme | Nitrosomonas europaea | |
0.0133 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant enzyme, with NADP+ | Nitrosomonas europaea | |
0.0133 | - |
NADP+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea | |
0.0167 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant enzyme, with NAD+ | Nitrosomonas europaea | |
0.0167 | - |
NAD+ | 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 | when D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed | Nitrosomonas europaea | |
NAD+ | - |
Nitrosomonas europaea | |
NADP+ | - |
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. 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, EC 1.2.1.16) | Nitrosomonas europaea |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0023 | - |
L-Glyceraldehyde 3-phosphate | about, pH 8.5, 30°C, recombinant enzyme, with NADP+ | Nitrosomonas europaea | |
0.007 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant enzyme, with NADP+ | Nitrosomonas europaea | |
0.0076 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant enzyme, with NAD+ | Nitrosomonas europaea | |
0.0418 | - |
NAD+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea | |
0.0578 | - |
NADP+ | pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde | Nitrosomonas europaea |