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Information on EC 1.14.13.114 - 6-hydroxynicotinate 3-monooxygenase
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1.14.13.114 6-hydroxynicotinate 3-monooxygenaseIUBMB Comments
A flavoprotein (FAD) . The reaction is involved in the aerobic catabolism of nicotinic acid.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
6-hydroxynicotinate 3-monooxygenase, 6-hydroxynicotinic acid 3-monooxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-hydroxynicotinic acid 3-monooxygenase
BB1770
BbNicC
NicC
6-hydroxynicotinic acid 3-monooxygenase
Bordetella bronchiseptica ATCC BAA-588 / NCTC 13252 / RB50
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
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-
-
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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
-
-
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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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
6-hydroxynicotinate,NADH:oxygen oxidoreductase (3-hydroxylating, decarboxylating)
A flavoprotein (FAD) [1]. The reaction is involved in the aerobic catabolism of nicotinic acid.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-chloro-6-hydroxynicotinate + NADH + H+ + O2
4-chloro-2,5-dihydroxypyridine + NAD+ + H2O + CO2
4-hydroxybenzoate + NADH + H+ + O2
hydroquinone + NAD+ + H2O + CO2
the homocyclic analogue of 6-hydroxynicotinate (6-HNA), 4-hydroxybenzoic acid (4-HBA), is decarboxylated and hydroxylated by NicC with a 420fold lower catalytic efficiency than is 6-HNA
-
-
?
4-hydroxybenzoate + NADH + H+ + O2
hydroquinone + NAD+ + H2O + CO2
the homocyclic analogue of 6-hydroxynicotinate (6-HNA), 4-hydroxybenzoic acid (4-HBA), is decarboxylated and hydroxylated by NicC with a 420fold lower catalytic efficiency than is 6-HNA
-
-
?
4-hydroxybenzoate + NADH + H+ + O2
hydroquinone + NAD+ + H2O + CO2
the homocyclic analogue of 6-hydroxynicotinate (6-HNA), 4-hydroxybenzoic acid (4-HBA), is decarboxylated and hydroxylated by NicC with a 420fold lower catalytic efficiency than is 6-HNA
-
-
?
4-hydroxybenzoate + NADH + H+ + O2
hydroquinone + NAD+ + H2O + CO2
the homocyclic analogue of 6-hydroxynicotinate (6-HNA), 4-hydroxybenzoic acid (4-HBA), is decarboxylated and hydroxylated by NicC with a 420fold lower catalytic efficiency than is 6-HNA
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-
?
4-hydroxybenzoate + NADH + H+ + O2
hydroquinone + NAD+ + H2O + CO2
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6.0% relative activity compared with 6-hydroxynicotinate
-
-
?
4-hydroxybenzoate + NADH + H+ + O2
hydroquinone + NAD+ + H2O + CO2
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6.0% relative activity compared with 6-hydroxynicotinate
-
-
?
5-chloro-6-hydroxynicotinate + NADH + H+ + O2
4-chloro-2,5-dihydroxypyridine + NAD+ + H2O + CO2
substrate analogue 5-chloro-6-HNA is 10fold more catalytically efficient than 6-HNA
-
-
?
5-chloro-6-hydroxynicotinate + NADH + H+ + O2
4-chloro-2,5-dihydroxypyridine + NAD+ + H2O + CO2
substrate analogue 5-chloro-6-HNA is 10fold more catalytically efficient than 6-HNA
-
-
?
5-chloro-6-hydroxynicotinate + NADH + H+ + O2
4-chloro-2,5-dihydroxypyridine + NAD+ + H2O + CO2
substrate analogue 5-chloro-6-HNA is 10fold more catalytically efficient than 6-HNA
-
-
?
5-chloro-6-hydroxynicotinate + NADH + H+ + O2
4-chloro-2,5-dihydroxypyridine + NAD+ + H2O + CO2
substrate analogue 5-chloro-6-HNA is 10fold more catalytically efficient than 6-HNA
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
Bordetella bronchiseptica ATCC BAA-588 / NCTC 13252 / RB50
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-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH
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-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
NADH is 5times more effective than NADPH
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-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
NADH is 5times more effective than NADPH
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-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
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-
-
?
additional information
?
-
-
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
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-
?
additional information
?
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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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
Bordetella bronchiseptica ATCC BAA-588 / NCTC 13252 / RB50
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
riboflavin or FMN do not serve as enzyme cofactors
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FAD
-
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
NADH
-
the enzyme activity is NADH-dependent and FAD-dependent. NADH is 5times more effective than NADPH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-hydroxynicotinaldehyde
competitive inhibition with respect to 6-hydroxynicotinate is weak
additional information
-
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0039
5-chloro-6-hydroxynicotinate
pH 7.5, 25°C, recombinant wild-type enzyme
-
0.6
4-hydroxybenzoate
pH 7.5, 25°C, recombinant wild-type enzyme
0.02
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant H302A
0.051
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant Y225F
0.118
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant wild-type enzyme
0.193
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant H211A
0.2
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant C202A
1.6
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant Y215F
additional information
additional information
kinetic analysis
-
additional information
additional information
Michaelis-Menten kinetics, comparative steady-state kinetic analysis with different substrates, 13C kinetic isotope effects, wild-type enzyme and mutants, overview. Comparison of the initial steady-state rates of product (2,5-DHP and NAD+) formation measured by HPLC and equilibrium dissociation constants for the NicC-FAD-6HNA complex
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.074
4-hydroxybenzoate
pH 7.5, 25°C, recombinant wild-type enzyme
2.18
5-chloro-6-hydroxynicotinate
pH 7.5, 25°C, recombinant wild-type enzyme
-
0.26
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant C202A
0.9
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant H302A
5
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant wild-type enzyme
5.24
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant Y225F
5.9
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant H211A
12
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant Y215F
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.123
4-hydroxybenzoate
pH 7.5, 25°C, recombinant wild-type enzyme
559
5-chloro-6-hydroxynicotinate
pH 7.5, 25°C, recombinant wild-type enzyme
-
1.3
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant C202A
7.5
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant Y215F
30.6
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant H211A
42.4
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant wild-type enzyme
45
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant H302A
102.8
6-Hydroxynicotinate
pH 7.5, 25°C, recombinant mutant Y225F
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.98
6-hydroxynicotinaldehyde
pH 7.5, 25°C, recombinant enzyme
additional information
additional information
inhibition kinetics
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH-dependence of the enzyme fitting to a double-bell curve pH-rate profile, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
6-hydroxynicotinate 3-monooxygenase (NicC) is a group A FAD-dependent monooxygenase
evolution
-
6-hydroxynicotinate 3-monooxygenase (NicC) is a group A FAD-dependent monooxygenase
-
evolution
-
6-hydroxynicotinate 3-monooxygenase (NicC) is a group A FAD-dependent monooxygenase
-
evolution
-
6-hydroxynicotinate 3-monooxygenase (NicC) is a group A FAD-dependent monooxygenase
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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
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
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
metabolism
Bordetella bronchiseptica ATCC BAA-588 / NCTC 13252 / RB50
-
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
-
physiological function
-
6-hydroxynicotinic acid 3-monooxygenase is a decarboxylative hydroxylase involved in aerobic nicotinate degradation
physiological function
6-hydroxynicotinic acid 3-monooxygenase is a decarboxylative hydroxylase involved in aerobic nicotinate degradation
physiological function
6-hydroxynicotinic acid 3-monooxygenase is a decarboxylative hydroxylase involved in aerobic nicotinate degradation
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
physiological function
Bordetella bronchiseptica ATCC BAA-588 / NCTC 13252 / RB50
-
6-hydroxynicotinic acid 3-monooxygenase is a decarboxylative hydroxylase involved in aerobic nicotinate degradation
-
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
-
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
-
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
-
additional information
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
additional information
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
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
Show AA Sequence and Transmembrane Helices (509 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42886
-
1 * 42886, including the starting methionine, calculated from sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
structure of the PpNicC monomer, modeling, overview
monomer
-
1 * 42886, including the starting methionine, calculated from sequence
monomer
-
1 * 42886, including the starting methionine, calculated from sequence
-
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H211A
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
H302A
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
H47A
site-directed mutagenesis, inactive mutant, unable to bind FAD
H47E
site-directed mutagenesis, the mutant can bind FAD, but shows very low activity compared to wild-type. The mutant shows significant consequences in its hydroxylating activity, with NADH oxidization proceeding much more rapidly than 6-HNA is decarboxylated and hydroxylated
H47F
site-directed mutagenesis, inactive mutant, unable to bind FAD
Y215F
site-directed mutagenesis, the mutant shows significant consequences in its hydroxylating activity, with NADH oxidization proceeding much more rapidly than 6-HNA is decarboxylated and hydroxylated
Y225F
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
H211A
-
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
-
H47A
-
site-directed mutagenesis, inactive mutant, unable to bind FAD
-
H47F
-
site-directed mutagenesis, inactive mutant, unable to bind FAD
-
Y215F
-
site-directed mutagenesis, the mutant shows significant consequences in its hydroxylating activity, with NADH oxidization proceeding much more rapidly than 6-HNA is decarboxylated and hydroxylated
-
H211A
-
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
-
H47A
-
site-directed mutagenesis, inactive mutant, unable to bind FAD
-
H47F
-
site-directed mutagenesis, inactive mutant, unable to bind FAD
-
Y215F
-
site-directed mutagenesis, the mutant shows significant consequences in its hydroxylating activity, with NADH oxidization proceeding much more rapidly than 6-HNA is decarboxylated and hydroxylated
-