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Information on EC 1.17.1.5 - nicotinate dehydrogenase
for references in articles please use BRENDA:EC1.17.1.5
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EC Tree 1 Oxidoreductases
1.17 Acting on CH or CH2 groups
1.17.1 With NAD+ or NADP+ as acceptor
1.17.1.5 nicotinate dehydrogenase
IUBMB Comments
A flavoprotein containing non-heme iron. The enzyme is capable of acting on a variety of nicotinate analogues to varying degrees, including pyrazine-2-carboxylate, pyrazine 2,3-dicarboxylate, trigonelline and 6-methylnicotinate. The enzyme from Clostridium barkeri also possesses a catalytically essential, labile selenium that can be removed by reaction with cyanide.
The enzyme appears in viruses and cellular organisms
- 1.17.1.5
- testosteroni
-
comamonas
- putida
- 6-hydroxynicotinate
- eubacterium
- barkeri
-
multi-subunit
-
t7-like
- pastoris
-
surpass
- molybdenum
-
chassis
- 3-cyanopyridine
-
pichia
showSynonyms
nicotinate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, nicotinate
-
-
-
-
EC 1.5.1.13
-
-
formerly
-
NA hydroxylase
NAH
-
-
-
-
NahAB1B2
NDH
NDHase
NdhL
NdhM
NdhS
nicotinate dehydrogenase
nicotinic acid hydroxylase
three-component NA hydroxylase
three-component nicotinic acid hydroxylase
NA hydroxylase
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
-
-
NahAB1B2
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
-
-
NDH
-
-
-
-
nicotinic acid hydroxylase
-
-
-
-
nicotinic acid hydroxylase
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
-
-
three-component NA hydroxylase
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
-
-
three-component nicotinic acid hydroxylase
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nicotinate + H2O + NADP+ = 6-hydroxynicotinate + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroxylation
-
-
-
-
oxidation
redox reaction
reduction
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
nicotinate degradation III
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SYSTEMATIC NAME
IUBMB Comments
nicotinate:NADP+ 6-oxidoreductase (hydroxylating)
A flavoprotein containing non-heme iron. The enzyme is capable of acting on a variety of nicotinate analogues to varying degrees, including pyrazine-2-carboxylate, pyrazine 2,3-dicarboxylate, trigonelline and 6-methylnicotinate. The enzyme from Clostridium barkeri also possesses a catalytically essential, labile selenium that can be removed by reaction with cyanide.
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CAS REGISTRY NUMBER
COMMENTARY
9059-03-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-pyrazinedicarboxylate + H2O + NADP+
?
-
Substrates: 10-20% of the activity with nicotinate
Products: -
Products: -
?
2-hydroxynicotinate + H2O + electron acceptor
?
-
Substrates: hydroxylation at a low rate
Products: -
Products: -
?
3,5-pyridinedicarboxylate + H2O + NADP+
?
-
Substrates: 5-10% of the activity with nicotinate
Products: -
Products: -
?
3-succinoyl-pyridine + H2O + NADP+
6-hydroxy-3-succinoyl-pyridine + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
6-methylnicotinate + H2O + NADP+
?
-
Substrates: 5-10% of the activity with nicotinate
Products: -
Products: -
?
nicotinate + H2O + 2,6-dichloroindophenol
6-hydroxynicotinate + reduced 2,6-dichloroindophenol
nicotinate + H2O + phenazine methosulfate
6-hydroxynicotinate + reduced phenazine methosulfate
picolinic acid + NADP+ + H2O
6-hydroxypicolinic acid + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
trigonelline + H2O + NADP+
?
-
Substrates: 5-10% of the activity with nicotinate
Products: -
Products: -
?
2-pyrazinecarboxylate + H2O + electron acceptor
?
-
Substrates: -
Products: -
Products: -
?
2-pyrazinecarboxylate + H2O + electron acceptor
?
-
Substrates: -
Products: -
Products: -
?
2-pyrazinecarboxylate + H2O + NADP+
?
-
Substrates: 30% of the activity with nicotinate
Products: -
Products: -
r
2-pyrazinecarboxylate + H2O + NADP+
?
-
Substrates: equally as effective as nicotinate
Products: -
Products: -
?
3-cyanopyridine + H2O + electron acceptor
?
-
Substrates: hydroxylation at a low rate
Products: -
Products: -
?
3-cyanopyridine + H2O + electron acceptor
?
-
Substrates: hydroxylation at a low rate
Products: -
Products: -
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
3-pyridinesulfonate + H2O + electron acceptor
?
-
Substrates: -
Products: -
Products: -
?
3-pyridinesulfonate + H2O + electron acceptor
?
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + 2,6-dichloroindophenol
6-hydroxynicotinate + reduced 2,6-dichloroindophenol
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + 2,6-dichloroindophenol
6-hydroxynicotinate + reduced 2,6-dichloroindophenol
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: flavin may be the primary electron acceptor, tetrazolium dye as electron acceptor
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: first step of nicotinate catabolism
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: equilibrium lies far in direction of 6-hydroxynicotinate formation
Products: -
Products: -
r
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: high substrate specificity, mixture of phenazine ethosulfate and 2,6-dichlorophenolindophenol as electron acceptor
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: high substrate specificity, transfers electrons only to artificial electron acceptors of high redox potential, i.e. thiazolyl blue, nitroblue tetrazolium chloride, mixture of phenazine ethosulfate and 2,6-dichlorophenolindophenol, methylene blue with 40% of the activity with phenazine ethosulfate and 2,6-dichlorophenolindophenol
Products: -
Products: -
r
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: first step of nicotinate catabolism
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: nicotinate degradation
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: high substrate specificity, mixture of phenazine ethosulfate and 2,6-dichlorophenolindophenol as electron acceptor
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: nicotinate degradation
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
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Substrates: purified enzyme probably loses its own native electron acceptor during the course of solubilization and purification, electron acceptors: phenazine methosulfate, potassium ferricyanide and with lower activity nitro blue tetrazolium, negative polarity at the 3-position on the pyridine ring of the substrate is important for reaction
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: first step of nicotinate catabolism
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: enzyme is linked to the cytochrome respiratory chain, phenazine methosulfate may accelerate the electron transfer from the electron respiratory chain to oxygen
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: purified enzyme probably loses its own native electron acceptor during the course of solubilization and purification, electron acceptors: phenazine methosulfate, potassium ferricyanide and with lower activity nitro blue tetrazolium, negative polarity at the 3-position on the pyridine ring of the substrate is important for reaction
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NAD+
6-hydroxynicotinate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NAD+
6-hydroxynicotinate + NADH + H+
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
-
Substrates: specific for NADP+, but artificial electron acceptors, i.e. benzyl viologen and 2,3,5-triphenyltetrazolium dyes, can replace NADP+, high substrate specificity with respect to nicotinate, requiring an unsubstituted pyridine or pyrazine ring nitrogen and a carboxyl group meta to the nitrogen
Products: -
Products: -
r
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
-
Substrates: equilibrium lies far in direction of 6-hydroxynicotinate formation
Products: -
Products: -
r
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
-
Substrates: first step in the anaerobic decomposition of nicotinate, NADP+ may be the natural, primary electron acceptor
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
-
Substrates: high substrate specificity toward electron donor substrates, unsubstituted nitrogen and a carboxyl group at position 3 are absolutely required for substrate hydroxylation and unsubstituted carbon-5 is important for oxidation at carbon-6 of substrate
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
-
Substrates: NADP+ or various dyes as electron acceptors
Products: with NADPH as substrate, enzyme exhibits NADPH oxidase activity in presence of oxygen
Products: with NADPH as substrate, enzyme exhibits NADPH oxidase activity in presence of oxygen
r
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + phenazine methosulfate
6-hydroxynicotinate + reduced phenazine methosulfate
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + phenazine methosulfate
6-hydroxynicotinate + reduced phenazine methosulfate
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + phenazine methosulfate
6-hydroxynicotinate + reduced phenazine methosulfate
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + phenazine methosulfate
6-hydroxynicotinate + reduced phenazine methosulfate
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
Substrates: -
Products: -
Products: -
?
pyridine-3-carboxylate + NADP+ + H2O
6-hydroxy-pyridine-3-carboxylate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
pyridine-3-carboxylate + NADP+ + H2O
6-hydroxy-pyridine-3-carboxylate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: not as substrates: nicotinamide, isonicotinate, picolinate, nicotinic acid N-oxide, N-methylnicotinamide, trigonelline, hypoxanthine, not as electron acceptor: NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with Brilliant cresyl blue, cytochrome c, FAD, ferricyanide, FMN, menadione, NAD(P)+, and both viologens as electron acceptors, not as substrates: 2- or 6-aminonicotinamide, 2-aminonicotinic acid, chelidamic acid, cinchomeronic acid, citrazinic acid, dinicotinic acid, dipicolinic acid, 3-hydroxypicolinic acid, hypoxanthine, isocinchomeronic acid, isonicotinic acid, lutidinic acid, nicotinamide, xanthine
Products: -
Products: -
?
additional information
?
-
-
Substrates: not as substrates: nicotinamide, methyl nicotinate, beta-picoline, 3-pyridylcarbinol, quinolinic acid, 3-pyridylacetic acid, 3-hydroxypyridine, 3-chloropyridine, not as electron acceptors: methylene blue, FAD, FMN, NAD+, NADP+, horse heart cytochrome c, 2,3,5-triphenyl-2H-tetrazolium, neutral red, safranin O, menadione
Products: -
Products: -
?
additional information
?
-
-
Substrates: not as substrates: nicotinamide, methyl nicotinate, beta-picoline, 3-pyridylcarbinol, quinolinic acid, 3-pyridylacetic acid, 3-hydroxypyridine, 3-chloropyridine, not as electron acceptors: methylene blue, FAD, FMN, NAD+, NADP+, horse heart cytochrome c, 2,3,5-triphenyl-2H-tetrazolium, neutral red, safranin O, menadione
Products: -
Products: -
?
additional information
?
-
-
Substrates: after addition of an artificial electron acceptor, such as phenazine methosulfate, or 2,6-dichloroindophenol, the nicotinate hydroxylase activity is significantly increased
Products: -
Products: -
?
additional information
?
-
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
Substrates: after addition of an artificial electron acceptor, such as phenazine methosulfate, or 2,6-dichloroindophenol, the nicotinate hydroxylase activity is significantly increased
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-succinoyl-pyridine + H2O + NADP+
6-hydroxy-3-succinoyl-pyridine + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
-
Substrates: first step in the anaerobic decomposition of nicotinate, NADP+ may be the natural, primary electron acceptor
Products: -
Products: -
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: first step of nicotinate catabolism
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: first step of nicotinate catabolism
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: nicotinate degradation
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: nicotinate degradation
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: first step of nicotinate catabolism
Products: -
Products: -
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
Substrates: enzyme is linked to the cytochrome respiratory chain, phenazine methosulfate may accelerate the electron transfer from the electron respiratory chain to oxygen
Products: -
Products: -
?
nicotinate + H2O + NAD+
6-hydroxynicotinate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NAD+
6-hydroxynicotinate + NADH + H+
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
-
primary electron acceptor, 1.5-2 mol tightly bound flavin per mol of enzyme
4Fe-4S-center
-
enzyme contains Fe/S centers, 8.3 mol iron per mol of enzyme, 1.5 mol acid-labile sulfur per mol of enzyme
4Fe-4S-center
-
two [2Fe-2S] clusters, 5-7 atoms Fe per 160 kDa enzyme molecule
Bactopterin
-
enzyme contains bactopterin, an eubacterial modification of molybdopterin, the organic moiety of the molybdenum cofactor
Bactopterin
-
molybdoenzyme with bactopterin, which differs from molybdopterin in MW, phosphate content and structure
molybdenum cofactor
-
molybdoenzyme with eubacterial molybdenum cofactor contains bactopterin
molybdenum cofactor
-
enzyme contains 1.5 mol molybdenum per mol of enzyme and bactopterin
molybdopterin
-
Mo is bound to a dinucleotide form of molybdopterin and is coordinated with selenium, 1 mol Mo per 160 kDa enzyme molecule, molybdenum is directly coordinated to selenium, Se-Mo center is required for enzymic oxidation of nicotinate
molybdopterin
-
molybdenum in the molybdopterin cofactor is coordinated directly with a dissociable selenium moiety, molybdenum center plays a role in the reaction step involving hydroxylation of the heterocyclic ring with oxygen derived from water
NADP+
-
specific for NADP+, artificial electron acceptors, i.e. benzyl viologen and 2,3,5-triphenyltetrazolium dyes, can replace NADP+
NADP+
-
NADP+ as ultimate electron acceptor, can be replaced by various dyes
additional information
-
NAD+ can not replace NADP+, but NADH can replace NADPH
-
additional information
-
enzyme contains a dissociable selenium moiety, which is coordinated directly with molybdenum in the molybdopterin cofactor, selenium is essential for enzyme activity, molar ratio of selenium to enzyme is 0.4-0.8, enzyme contains 1 g selenium per mol of native active enzyme, selenium is completely dissociated from protein in the SDS-gel
-
additional information
-
enzyme contains labile selenium cofactor which is essential for hydroxylase activity of enzyme, Se is directly coordinated to Mo, up to 1 Se atom per enzyme molecule
-
additional information
-
approximately 8 molecules tightly bound iron per enzyme molecule
-
additional information
-
enzyme contains 11 mol non-heme iron and 6 mol acid-labile sulfide per mole of enzyme
-
additional information
-
no activity with FMN and NADP+
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
the enzyme contains a [2Fe2S] domain, a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, overview
additional information
-
enzyme activity increases with increasing concentrations of molybdate in growth medium
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
1 mM, 10 min at 35°C, complete loss of activity
Selenophosphate
-
7 mM, 30 min, anaerobic conditions, reversible complete inactivation, time-dependent
sodium selenide
-
7 mM, 10 min, anaerobic conditions, reversible complete inactivation, time-dependent
additional information
-
not inhibited by incubation for 1 h at room temperature with 100 mM KCN
-
KCN
-
2 mM, complete loss of enzyme activity in anaerobically incubated crude extract
KCN
-
after removal of cyanide under anaerobic conditions, enzyme activity can be reconstituted by anaerobic incubation with Na2S
KCN
-
strong inhibition, partially restored by addition of phenazine methosulfate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-dichloroindophenol
-
after addition of an artificial electron acceptor such as 2,6-dichloroindophenol, the nicotinate hydroxylase activity is significantly increased
phenazine methosulfate
-
after addition of an artificial electron acceptor such as phenazine methosulfate, PMS, the nicotinate hydroxylase activity is significantly increased
additional information
-
not activated by high concentrations of citrate, sulfate, or diphosphate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0659
nicotinate
-
recombinant enzyme, with phenazine methosulfate, pH 7.0, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.2
-
crude extract, high activity achieved if nicotinate is the only substrate
20
-
purified enzyme, average value, Difco yeast extract with selenium as growth medium
4.4
-
purified enzyme, Difco yeast extract without selenium as growth medium
additional information
additional information
-
more values for specific activities in crude extract
additional information
1.89 micromol/min/mg dry weight for resting cells
additional information
1.18 micromol/min/mg protein (cells free extract)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bacillus sp. DSM 2923 is characterized as a new species Bacillus niacini
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
strain T2 is capable of utilizing nicotinic acid as sole carbon and nitrogen source
brenda
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
strain T2 is capable of utilizing nicotinic acid as sole carbon and nitrogen source
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
an enzyme-knockout mutant does not grow on basic salt medium supplemented with nicotine as the sole carbon and nitrogen source but can grow well on basic salt medium supplemented with glucose or glycerol plus (NH4)2SO4
physiological function
additional information
physiological function
-
the enzyme is involved in the degradation of nicotinic acid
physiological function
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
the enzyme is involved in the degradation of nicotinic acid
-
additional information
when the small unit of NaDHJA1 is replaced by the small subunit from NaDHKT2440 of Pseudomonas putida KT2440, the hybrid protein is able to catalyze the hydroxylation of nicotinate, but loses the ability to catalyze hydroxylation of 3-cyanopyridine
additional information
when the small unit of NaDHJA1 is replaced by the small subunit from NaDHKT2440 of Pseudomonas putida KT2440, the hybrid protein is able to catalyze the hydroxylation of nicotinate, but loses the ability to catalyze hydroxylation of 3-cyanopyridine
additional information
when the small unit of NaDHJA1 is replaced by the small subunit from NaDHKT2440 of Pseudomonas putida KT2440, the hybrid protein is able to catalyze the hydroxylation of nicotinate, but loses the ability to catalyze hydroxylation of 3-cyanopyridine
additional information
-
when the small unit of NaDHJA1 is replaced by the small subunit from NaDHKT2440 of Pseudomonas putida KT2440, the hybrid protein is able to catalyze the hydroxylation of nicotinate, but loses the ability to catalyze hydroxylation of 3-cyanopyridine
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NICB_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
1187
0
127875
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
20000
-
x * 85000 + x * 34000 + x * 20000, additional bands with increasing period of storage, subunits are loosely linked by electrostatic interactions, SDS-PAGE
23000
34000
-
x * 85000 + x * 34000 + x * 20000, additional bands with increasing period of storage, subunits are loosely linked by electrostatic interactions, SDS-PAGE
37000
50000
85000
-
x * 85000 + x * 34000 + x * 20000, additional bands with increasing period of storage, subunits are loosely linked by electrostatic interactions, SDS-PAGE
160000
-
major form, occurence of additional enzyme forms of 400 kDa and 120 kDa with same subunit composition, gel filtration and native PAGE
23000
dimer of heterotetramers, subunits of the heterotetramer: 1 * 50000 + 1 * 37000 + 1* 33000 + 1 * 23000, X-ray diffraction
37000
dimer of heterotetramers, subunits of the heterotetramer: 1 * 50000 + 1 * 37000 + 1* 33000 + 1 * 23000, X-ray diffraction
50000
dimer of heterotetramers, subunits of the heterotetramer: 1 * 50000 + 1 * 37000 + 1* 33000 + 1 * 23000, X-ray diffraction
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
monomer
octamer
dimer of heterotetramers, subunits of the heterotetramer: 1 * 50000 + 1 * 37000 + 1* 33000 + 1 * 23000, X-ray diffraction
oligomer
-
x * 85000 + x * 34000 + x * 20000, additional bands with increasing period of storage, subunits are loosely linked by electrostatic interactions, SDS-PAGE
heterotetramer
-
1 * 50000 + 1 * 37000 + 1 * 33000 + 1 * 23000, SDS-PAGE
heterotetramer
-
23 kDa protein is less stained and may be a degradation product
monomer
-
1 * 80000, SDS-PAGE, in presence of 50 mM 2-mercaptoethanol
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
when the small unit of NaDHJA1 is replaced by the small subunit from NaDHKT2440 of Pseudomonas putida KT2440, the hybrid protein is able to catalyze the hydroxylation of nicotinate, but loses the ability to catalyze hydroxylation of 3-cyanopyridine
additional information
when the small unit of NaDHJA1 is replaced by the small subunit from NaDHKT2440 of Pseudomonas putida KT2440, the hybrid protein is able to catalyze the hydroxylation of nicotinate, but loses the ability to catalyze hydroxylation of 3-cyanopyridine
additional information
when the small unit of NaDHJA1 is replaced by the small subunit from NaDHKT2440 of Pseudomonas putida KT2440, the hybrid protein is able to catalyze the hydroxylation of nicotinate, but loses the ability to catalyze hydroxylation of 3-cyanopyridine
additional information
-
when the small unit of NaDHJA1 is replaced by the small subunit from NaDHKT2440 of Pseudomonas putida KT2440, the hybrid protein is able to catalyze the hydroxylation of nicotinate, but loses the ability to catalyze hydroxylation of 3-cyanopyridine
-
additional information
-
4 chlorate-resistant mutants are no longer able to degrade nicotinate
additional information
-
4 chlorate-resistant mutants are no longer able to degrade nicotinate
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
the enzyme retains about 40% activity after 10 h at pH 7.0. The enzyme retains about 40% activity after 8 h at pH 8.0 and 9.0. The enzyme retains about 40% activity after 4 h at pH 10.0
additional information
-
maximal stability during incubation for 14 h at room temperature, after 9 days storage at pH 8, 25% of the initial activity retained
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
the enzyme retains more than 85% activity after 10 h at 30°C. At 40°C, the enzyme retains more than 70% and 42% activity after 4 h and 6 h, respectively. The enzyme retains more than 50% activity after 2 h at 50°C. The enzyme is inactive after 2 h at 60°C. The half-life of the enzyme at 30, 40, 50°C is 32, 5.6 and 2 h, respectively
additional information
-
hydroxylase activity is more sensitive to heat inactivation than are diaphorase and NADPH-oxidase activities
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is most stable at alkaline pH in the presence of glycerol, 20% glycerol and 400 mM KCl stabilize
-
lyophilization completely inactivates, high protein concentration may have a stabilizing effect on enzyme activity, sugar protects enzyme from dissociation
-
membrane-bound enzyme is stable, but solubilized enzyme is very labile, 20 mM nicotinate stabilizes
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
exposure of substrate-reduced enzyme to air results in a complete loss of activity, enzyme before reduction is much less sensitive to oxygen inactivation
-
644535
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
room temperature, 50 mM Tris-HCl buffer, pH 8.2, after 1 day 40% loss of hydroxylase activity, after 7 days 62% loss of hydroxylase activity, NADPH oxidase and diaphorase activity of enzyme are more stable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells and Comamonas testosteroni strain CNB-2
expressed in Pseudomonas entomophila, subcloning of mutants in Escherichia coli failed
gene ndhL, belongs to the ndh cluster with genes ndhS and ndhM, DNA and amino acid sequence determination, sequence comparison, recombinant expression of the nicotinate dehydrogenase gene cluster as His-tagged proteins in Pseudomonas entomophila strain L48, subcloning in Escherichia coli strain DH10B
gene ndhM, belongs to the ndh cluster with genes ndhL and ndhS, DNA and amino acid sequence determination, sequence comparison, recombinant expression of the nicotinate dehydrogenase gene cluster as His-tagged proteins in Pseudomonas entomophila strain L48, subcloning in Escherichia coli strain DH10B
gene ndhS, belongs to the ndh cluster with genes ndhL and ndhM, DNA and amino acid sequence determination, sequence comparison, recombinant expression of the nicotinate dehydrogenase gene cluster as His-tagged proteins in Pseudomonas entomophila strain L48, subcloning in Escherichia coli strain DH10B
genes nahAB1B2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant enzyme expression in the non-nicotinic acid-degrading Shinella sp. strain HZN7. The recombinant HZN7-pBBR-nahAB1B2 converts nicotinic acid into equimolar 6-hydroxynicotinic acid, while the recombinants HZN7-pBBR-nahAB1 (lacking component B2) and HZN7-pBBRnahAB2 (lacking component B1) cannot convert nicotinic acid. Cell-free extracts of HZN7-pBBR-nahAB1B2 exhibit nicotinic acid hydroxylase activity
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
after denaturation by acid precipitation at pH 4.5 with HCl, recombining and neutralizing of precipitated protein and yellow supernatant results in a reconstitution of over 90% of the original activity
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kruger, B.; Meyer, O.; Nagel, M.; Andreesen, J.R.; Meincke, M.; Bock, E.; Blumle, S.; Zumft, W.G.
Evidence for the presence of bactopterin in the eubacterial molybdoenzymes nicotinic acid dehydrogenase, nitrite oxidoreductase, and respiratory nitrate reductase
FEMS Microbiol. Lett.
48
225-227
1987
Neobacillus niacini
-
brenda
Gladyshev, V.N.; Khangulov, S.V.; Stadtman, T.C.
Nicotinic acid hydroxylase from Clostridium barkeri: Electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme
Proc. Natl. Acad. Sci. USA
91
232-236
1994
Eubacterium barkeri
brenda
Hurh, B.; Yamane, T.; Nagasawa, T.
Purification and characterization of nicotinic acid dehydrogenase from Pseudomonas fluorescens TN5
J. Ferment. Bioeng.
78
19-26
1994
Delftia acidovorans, Pseudomonas fluorescens, Pseudomonas fluorescens TN5, Serratia marcescens, Serratia marcescens IFO 12648
-
brenda
Hirschberg, R.; Ensign, J.C.
Oxidation of nicotinic acid by a Bacillus species: purification and properties of nicotinic acid and 6-hydroxynicotinic acid hydroxylases
J. Bacteriol.
108
751-756
1971
Bacillus sp. (in: firmicutes)
brenda
Nagel, M.; Andreesen, J.R.
Molybdenum-dependent degradation of nicotinic acid by Bacillus sp. DSM 2923
FEMS Microbiol. Lett.
59
147-152
1989
Neobacillus niacini, Neobacillus niacini DSM 2923
-
brenda
Nagel, M.; Andreesen, J.R.
Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini
Arch. Microbiol.
154
605-613
1990
Neobacillus niacini
-
brenda
Holcenberg, J.S.; Stadtman, E.R.
Nicotinic acid metabolism. III. Purification and properties of a nicotinic acid hydroxylase
J. Biol. Chem.
244
1194-1203
1969
Clostridium sp.
brenda
Gladyshev, V.N.; Khangulov, S.V.; Stadtman, T.C.
Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri
Biochemistry
35
212-223
1996
Eubacterium barkeri
brenda
Wieser, M.; Heinzmann, K.; Kiener, A.
Bioconversion of 2-cyanopyrazine to 5-hydroxypyrazine-2-carboxylic acid with Agrobacterium sp. DSM 6336
Appl. Microbiol. Biotechnol.
48
174-180
1997
Agrobacterium sp.
-
brenda
Petersen, M.; Kiener, A.
Biocatalysis - preparation and functionalization of N-heterocycles
Green Chem.
2
99-106
1999
Achromobacter xylosoxidans, Alcaligenes faecalis
-
brenda
Yang, Y.; Yuan, S.; Chen, T.; Ma, P.; Shang, G.; Dai, Y.
Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from Pseudomonas putida KT2440
Biodegradation
20
541-549
2009
Pseudomonas putida (Q88FX8), Pseudomonas putida KT 2240 (Q88FX8)
brenda
Wagener, N.; Pierik, A.J.; Ibdah, A.; Hille, R.; Dobbek, H.
The Mo-Se active site of nicotinate dehydrogenase
Proc. Natl. Acad. Sci. USA
106
11055-11060
2009
Eubacterium barkeri (Q0QLF2), Eubacterium barkeri
brenda
Yang, Y.; Chen, T.; Ma, P.; Shang, G.; Dai, Y.; Yuan, S.
Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine
Biodegradation
21
593-602
2010
Comamonas testosteroni (B1PHD1), Comamonas testosteroni (B1PHD2), Comamonas testosteroni (B1PHD3), Comamonas testosteroni JA1 (B1PHD1), Comamonas testosteroni JA1 (B1PHD2), Comamonas testosteroni JA1 (B1PHD3), Comamonas testosteroni JA1
brenda
Yuan, M.; Zhang, Y.; Zhao, L.; Ma, Y.; He, Q.; He, J.; Qiu, J.
Identification and characterization of a new three-component nicotinic acid hydroxylase NahAB1 B2 from Pusillimonas sp. strain T2
Lett. Appl. Microbiol.
66
321-328
2018
Pusillimonas sp. (ex Stolz et al. 2005), Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
brenda
Lu, Z.H.; Yang, L.R.; Wu, J.P.
Construction of an efficient nicotinate dehydrogenase expression system in Comamonas testosteroni CNB-2 with multi-level N-terminal engineering
Appl. Biochem. Biotechnol.
192
923-934
2020
Comamonas testosteroni (B1PHD1), Comamonas testosteroni (B1PHD2), Comamonas testosteroni (B1PHD3)
brenda
Li, J.; Li, S.; Xie, L.; Chen, G.; Shen, M.; Pan, F.; Shu, M.; Yang, Y.; Jiao, Y.; Zhang, F.; Linhardt, R.J.; Zhong, W.
Additional role of nicotinic acid hydroxylase for the transformation of 3-succinoyl-pyridine by Pseudomonas sp. strain JY-Q
Appl. Environ. Microbiol.
87
e02740-20
2021
Pseudomonas sp. JY-Q
brenda
Lu, Z.H.; Yang, L.R.; Wu, J.P.
Efficient heterologous expression of nicotinate dehydrogenase in Comamonas testosteroni CNB-2 with transcriptional, folding enhancement strategy
Enzyme Microb. Technol.
134
109478
2020
Comamonas testosteroni (B1PHD3), Comamonas testosteroni JA-1 (B1PHD3)
brenda
Shang, Y.; Qin, J.; Gong, J.; Wang, Z.; Li, H.; Li, H.; Shi, J.; Xu, Z.
High-throughput screening of a nicotinate dehydrogenase producing Pseudomonas putida mutant for efficient biosynthesis of 6-hydroxynicotinic acid
Mol. Catal.
509
111600
2021
Pseudomonas putida
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.17.1.5)
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