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Literature summary for 1.2.1.12 extracted from
- New pieces to the carbon metabolism puzzle of Nitrosomonas europaea kinetic characterization of glyceraldehyde-3 phosphate and succinate semialdehyde dehydrogenases (2019), Biochimie, 158, 238-245 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene cbbG, 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 [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | enzyme kinetics, the recombinant enzyme exhibits about 6fold higher Km value toward 1,3-bisPGA compared to Ga3P. kcat in the way of Ga3P oxidation is about 5fold higher than in the opposite direction, thus resulting in a similar catalytic efficiency (kcat/Km) of the enzyme for the forward and the reverse reactions | Nitrosomonas europaea |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 75000 | - |
recombinant enzyme, gel filtration | Nitrosomonas europaea |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Nitrosomonas europaea | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r |  |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Nitrosomonas europaea NBRC 14298 | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Nitrosomonas europaea ATCC 19718 | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Nitrosomonas europaea KCTC 2705 | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Nitrosomonas europaea CIP 103999 | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Nitrosomonas europaea | Q82XE7 | - |
- |
| Nitrosomonas europaea ATCC 19718 | Q82XE7 | - |
- |
| Nitrosomonas europaea CIP 103999 | Q82XE7 | - |
- |
| Nitrosomonas europaea KCTC 2705 | Q82XE7 | - |
- |
| Nitrosomonas europaea NBRC 14298 | Q82XE7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Nitrosomonas europaea |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
purified recombinant CbbG, pH 8.5, 30°C | Nitrosomonas europaea |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Nitrosomonas europaea | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Nitrosomonas europaea NBRC 14298 | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Nitrosomonas europaea ATCC 19718 | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Nitrosomonas europaea KCTC 2705 | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Nitrosomonas europaea CIP 103999 | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
| additional information | enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer | Nitrosomonas europaea | ? | - |
- |
|
| additional information | enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer | Nitrosomonas europaea NBRC 14298 | ? | - |
- |
|
| additional information | enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer | Nitrosomonas europaea ATCC 19718 | ? | - |
- |
|
| additional information | enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer | Nitrosomonas europaea KCTC 2705 | ? | - |
- |
|
| additional information | enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer | Nitrosomonas europaea CIP 103999 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 36200, recombinant enzyme, SDS-PAGE | Nitrosomonas europaea |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CbbG | - |
Nitrosomonas europaea |
| Ga3P dehydrogenase | - |
Nitrosomonas europaea |
| Ga3PDHase | - |
Nitrosomonas europaea |
| glyceraldehyde-3 phosphate dehydrogenase | - |
Nitrosomonas europaea |
| NAD-dependent Ga3PDHase | - |
Nitrosomonas europaea |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Nitrosomonas europaea |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Nitrosomonas europaea |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Nitrosomonas europaea | |
| NADH | - |
Nitrosomonas europaea | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | sequence comparisons | Nitrosomonas europaea |
| physiological function | the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH | Nitrosomonas europaea |
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Release 2023.1 (January 2023)
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