Crystallization (Comment) | Organism |
---|---|
the crystal structure of the NAD+-enzyme complex is determined by molecular replacement and refined to an R-value of 17.9% at 2.0 A | Pseudomonas sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas sp. | P47227 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ = biphenyl-2,3-diol + NADH + H+ | a two-step reaction mechanism is proposed | Pseudomonas sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ | modeling studies indicate that the substrate is bound in a deep hydrophobic cleft close to the nicotinamide moiety of the NAD+ cofactor. These studies further suggest that Asn143 is a key determinant of substrate specificity | Pseudomonas sp. | biphenyl-2,3-diol + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
BephB | - |
Pseudomonas sp. |
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase | - |
Pseudomonas sp. |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is involved in the aerobic biodegradation of polychlorinated biphenyls | Pseudomonas sp. |