3-hydroxybenzoate (0.49% relative activity compared with 6-hydroxynicotinate), 2-hydroxybenzoate (0.18% compared with 6-hydroxynicotinate), 2-hydroxynicotinate (0.31% relative activity compared with 6-hydroxynicotinate) and 6-hydroxypyrazine carboxylate (0.19% relative activity compared with 6-hydroxynicotinate) are less effecive substrates or, in the case of nicotinate, 6-methylnicotinate and benzoate, not substrates at all
3-hydroxybenzoate (0.49% relative activity compared with 6-hydroxynicotinate), 2-hydroxybenzoate (0.18% compared with 6-hydroxynicotinate), 2-hydroxynicotinate (0.31% relative activity compared with 6-hydroxynicotinate) and 6-hydroxypyrazine carboxylate (0.19% relative activity compared with 6-hydroxynicotinate) are less effecive substrates or, in the case of nicotinate, 6-methylnicotinate and benzoate, not substrates at all
the enzyme activity is NADH-dependent and FAD-dependent. The holoenzyme contains 1 M of FAD per 1 M of enzyme. FAD gradually dissociates from the enzyme during purification. Without FAD, no pure enzyme activity is observed, but after the addition of FAD, the apoenzyme is activated immediately
no significant effect on enzyme activity is found with metal-chelating agents such o-phenanthroline, 8-hydroxyquinoline, EDTA, disodium 4,5-dihydroxy-m-benzenedisulfonate, fluoride and azide, and other compounds such as KCl, LiCl, NaCl, BaCl2, CaCl2, MnCl2, MgCl2, PbCl2, ZnCl2, CoCl2, SnCl2, FeSO4, FeCl3, NiCl2, CdCl2, AlCl3, iodoacetic acid, hydroxylamine, phenylhydrazine, semicarbazide, cysteamine, alpha,alpha'-dipyridyl and urea
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
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
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
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
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged selenomethionine-labeled enzyme, hanging drop vapor diffusion method, mixing of 0.0015 ml of protein solution with 0.0015 ml of reservoir solution containing 0.1 M Tris-HCl, pH 7.7-8.3, 27-30% PEG 4000, and 0.2 M magnesium chloride hexahydrate, 18°C, 2-3 days, method optimization, X-ray diffraction structure determination and analysis using SAD phasing at 2.1 A resolution
gene Bb1770, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strains MachI and BL21(DE3)
gene nicC, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strains MachI and BL21(DE3)
the isolated enzyme is used for the synthesis of 2,5-dihydroxypyridine, a precursor for the chemical synthesis of 5-aminolevulinic acid, which is applied as a plant growth hormone, a herbicide and in cancer therapy
the isolated enzyme is used for the synthesis of 2,5-dihydroxypyridine, a precursor for the chemical synthesis of 5-aminolevulinic acid, which is applied as a plant growth hormone, a herbicide and in cancer therapy
Hicks, K.; Yuen, M.; Zhen, W.; Gerwig, T.; Story, R.; Kopp, M.; Snider, M.
Structural and biochemical characterization of 6-hydroxynicotinic acid 3-monooxygenase, a novel decarboxylative hydroxylase involved in aerobic nicotinate degradation
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1.14.13.114 6-hydroxynicotinate 3-monooxygenase
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