Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NaCl | reaction rate and dissociation at pH 9 are reduced by increasing the NaCl concentration (0-500 mM) | Priestia megaterium |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Priestia megaterium | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-D-glucose + NAD+ | - |
Priestia megaterium | D-glucono-1,5-lactone + NADH + H+ | - |
? | |
D-glucose + NAD+ | - |
Priestia megaterium | D-glucono-1,5-lactone + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9, the enzyme is completely and reversibly dissociated into four inactive protomers | Priestia megaterium |
More | monomers, dimers and tetramers participate in aggregation equilibria which are dependent on enzyme and NaCl concentration and on the pH value | Priestia megaterium |
tetramer | x-ray crystallography | Priestia megaterium |
Synonyms | Comment | Organism |
---|---|---|
beta-D-glucose:NAD(P)+ 1-oxido-reductase | - |
Priestia megaterium |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
6.5 | 9 | the enzyme is stable and active at pH 6.5, by shifting the pH to 9.0 the enzyme is completely and irreversibly dissociated into four inactive protomers | Priestia megaterium |
9 | - |
the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9 the enzyme is completely and reversibly dissociated into four inactive protomers | Priestia megaterium |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Priestia megaterium | |
NADP+ | - |
Priestia megaterium |