EC Number | Cloned (Comment) | Organism |
---|---|---|
6.3.5.1 | expressed in Escherichia coli as a His-tagged fusion protein | Acinetobacter baumannii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.5.1 | 0.017 | - |
deamido-NAD+ | pH 7.5, 30°C | Acinetobacter baumannii | |
6.3.5.1 | 4.3 | - |
deamido-NMN | pH 7.5, 30°C | Acinetobacter baumannii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.5.1 | Acinetobacter baumannii | - |
- |
- |
6.3.5.1 | Acinetobacter baumannii | B0V8W9 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.3.5.1 | using Ni-NTA chromatography | Acinetobacter baumannii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.5.1 | ATP + deamido-NAD+ + L-Gln | - |
Acinetobacter baumannii | AMP + diphosphate + NAD+ + L-Glu | - |
? | |
6.3.5.1 | ATP + deamido-NAD+ + NH3 + H2O | - |
Acinetobacter baumannii | AMP + diphosphate + NAD+ | - |
? | |
6.3.5.1 | ATP + deamido-NMN + L-Gln | poor substrate | Acinetobacter baumannii | AMP + diphosphate + NMN + L-Glu | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.3.5.1 | abNadE | enzyme possesses an additional glutamine transferase domain | Acinetobacter baumannii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.3.5.1 | 30 | - |
assay at | Acinetobacter baumannii |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.5.1 | 0.0032 | - |
deamido-NMN | pH 7.5, 30°C | Acinetobacter baumannii | |
6.3.5.1 | 0.57 | - |
deamido-NAD+ | pH 7.5, 30°C | Acinetobacter baumannii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.3.5.1 | 7.5 | - |
assay at | Acinetobacter baumannii |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.3.5.1 | malfunction | nadE is dispensable when the nondeamidating salvage pathway functions as the only route of NAD biogenesis | Acinetobacter baumannii |
6.3.5.1 | metabolism | due to the presence of an additional glutamine transferase domain, abNadE can efficiently utilize l-glutamine (as well as ammonia) for the amidation of NAD precursor | Acinetobacter baumannii |
6.3.5.1 | physiological function | nadE, encoding glutamine-dependent NAD synthetase, is dispensable when the nondeamidating salvage pathway of nicotinamide salvage/recycling functions as the only route of NAD biogenesis | Acinetobacter baumannii |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.5.1 | 0.00074 | - |
deamido-NMN | pH 7.5, 30°C | Acinetobacter baumannii | |
6.3.5.1 | 34 | - |
deamido-NAD+ | pH 7.5, 30°C | Acinetobacter baumannii |