1.14.13.114: 6-hydroxynicotinate 3-monooxygenase
This is an abbreviated version!
For detailed information about 6-hydroxynicotinate 3-monooxygenase, go to the full flat file.
Reaction
Synonyms
6-hydroxynicotinic acid 3-monooxygenase, 6HNA monooxygenase, BB1770, BbNicC, NicC, PpNicC
ECTree
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Reaction
Reaction on EC 1.14.13.114 - 6-hydroxynicotinate 3-monooxygenase
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6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
proposal of two catalytic mechanisms, overview
6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
proposal of two catalytic mechanisms, overview
6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
reaction mechanism, overview. 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
6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
proposal of two catalytic mechanisms, overview
Bordetella bronchiseptica ATCC BAA-588 / NCTC 13252 / RB50
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6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
reaction mechanism, overview. 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
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6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
reaction mechanism, overview. 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
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6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
reaction mechanism, overview. 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
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