EC Number   |
General Information |
Reference |
|---|
  1.14.13.114 | evolution |
6-hydroxynicotinate 3-monooxygenase (NicC) is a group A FAD-dependent monooxygenase |
-, 764159 |
| 1.14.13.114 | metabolism |
the enzyme is involved in the nicotinate degradation pathway catalyzing the the second of three oxidations of nicotinate that activate the pyridine toward ring cleavage by aerobic bacteria, overview |
-, 744353 |
| 1.14.13.114 | more |
modeling of substrate 6-hydroxynicotinate into the active site, substrate binding site structure, overview. The nicC gene in Pseudomonas putida strain KT2440 has been misidentified as salicylate hydroxylase, nahG |
744353 |
| 1.14.13.114 | more |
residues Tyr215 and His47 are both critical determinants of 6-hydroxynicotinate (6-HNA) binding and in coupling rates of 2,5-dihydroxypyridine (2,5-DHP) and NAD+ product formation. Two mechanistic proposals for the substrate hydroxylation and decarboxylation reaction catalyzed by NicC using the C(4a)-hydroperoxyflavin intermediate (FADHOOH), and determination of an electrophilic aromatic substitution reaction mechanism in which His47-Tyr215 may serve as the general base to catalyze substrate hydroxylation and refine the structural model for substrate binding by NicC. Residues H302, Y215, and H47 are critical determinants of the hydroxylation steps in catalysis |
-, 764159 |
| 1.14.13.114 | physiological function |
6-hydroxynicotinate 3-monooxygenase (NicC) is a group A FAD-dependent monooxygenase that catalyzes the decarboxylative hydroxylation of 6-hydroxynicotinic acid (6-HNA) to 2,5-dihydroxypyridine (2,5-DHP) with concomitant oxidation of NADH in nicotinic acid degradation by aerobic bacteria |
-, 764159 |
| 1.14.13.114 | physiological function |
6-hydroxynicotinic acid 3-monooxygenase is a decarboxylative hydroxylase involved in aerobic nicotinate degradation |
-, 744353 |
