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Information on EC 1.17.1.5 - nicotinate dehydrogenase
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1.17.1.5 nicotinate dehydrogenaseIUBMB 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.
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Word Map
- 1.17.1.5
- testosteroni
-
comamonas
- putida
- 6-hydroxynicotinate
- eubacterium
- barkeri
-
multi-subunit
-
t7-like
- pastoris
-
surpass
- molybdenum
-
chassis
- 3-cyanopyridine
-
pichia
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
nicotinate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, nicotinate
-
-
-
-
EC 1.5.1.13
-
-
formerly
-
NA hydroxylase
NAH
-
-
-
-
NahAB1B2
NDH
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
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-
-
NahAB1B2
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
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-
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NDH
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-
-
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nicotinic acid hydroxylase
-
-
-
-
nicotinic acid hydroxylase
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
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-
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three-component NA hydroxylase
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
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-
-
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
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-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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
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
2,3-pyrazinedicarboxylate + H2O + NADP+
?
-
10-20% of the activity with nicotinate
-
-
?
2-hydroxynicotinate + H2O + electron acceptor
?
-
hydroxylation at a low rate
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-
?
3,5-pyridinedicarboxylate + H2O + NADP+
?
-
5-10% of the activity with nicotinate
-
-
?
3-cyanopyridine + H2O + electron acceptor
?
-
hydroxylation at a low rate
-
-
?
6-methylnicotinate + H2O + NADP+
?
-
5-10% of the activity with nicotinate
-
-
?
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+
-
-
-
-
?
trigonelline + H2O + NADP+
?
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5-10% of the activity with nicotinate
-
-
?
2-pyrazinecarboxylate + H2O + NADP+
?
-
30% of the activity with nicotinate
-
-
r
2-pyrazinecarboxylate + H2O + NADP+
?
-
equally as effective as nicotinate
-
-
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
-
-
-
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
-
-
-
?
nicotinate + H2O + 2,6-dichloroindophenol
6-hydroxynicotinate + reduced 2,6-dichloroindophenol
Pusillimonas sp. (ex Stolz et al. 2005)
-
-
-
-
?
nicotinate + H2O + 2,6-dichloroindophenol
6-hydroxynicotinate + reduced 2,6-dichloroindophenol
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
-
-
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
flavin may be the primary electron acceptor, tetrazolium dye as electron acceptor
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
first step of nicotinate catabolism
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
-
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
equilibrium lies far in direction of 6-hydroxynicotinate formation
-
r
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
high substrate specificity, mixture of phenazine ethosulfate and 2,6-dichlorophenolindophenol as electron acceptor
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
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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
-
r
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
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first step of nicotinate catabolism
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
nicotinate degradation
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
high substrate specificity, mixture of phenazine ethosulfate and 2,6-dichlorophenolindophenol as electron acceptor
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
nicotinate degradation
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
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
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
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first step of nicotinate catabolism
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
enzyme is linked to the cytochrome respiratory chain, phenazine methosulfate may accelerate the electron transfer from the electron respiratory chain to oxygen
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
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
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
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first step of nicotinate catabolism
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?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
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enzyme is linked to the cytochrome respiratory chain, phenazine methosulfate may accelerate the electron transfer from the electron respiratory chain to oxygen
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
-
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
-
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
-
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
-
-
?
nicotinate + H2O + NAD+
6-hydroxynicotinate + NADH + H+
Pusillimonas sp. (ex Stolz et al. 2005)
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-
-
-
?
nicotinate + H2O + NAD+
6-hydroxynicotinate + NADH + H+
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
-
-
-
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
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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
-
r
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
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equilibrium lies far in direction of 6-hydroxynicotinate formation
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r
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
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first step in the anaerobic decomposition of nicotinate, NADP+ may be the natural, primary electron acceptor
-
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
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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
-
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
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NADP+ or various dyes as electron acceptors
with NADPH as substrate, enzyme exhibits NADPH oxidase activity in presence of oxygen
r
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
-
-
-
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
-
-
-
?
nicotinate + H2O + phenazine methosulfate
6-hydroxynicotinate + reduced phenazine methosulfate
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-
-
?
nicotinate + H2O + phenazine methosulfate
6-hydroxynicotinate + reduced phenazine methosulfate
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-
-
?
nicotinate + H2O + phenazine methosulfate
6-hydroxynicotinate + reduced phenazine methosulfate
Pusillimonas sp. (ex Stolz et al. 2005)
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-
-
-
?
nicotinate + H2O + phenazine methosulfate
6-hydroxynicotinate + reduced phenazine methosulfate
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
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-
-
-
?
pyridine-3-carboxylate + NADP+ + H2O
6-hydroxy-pyridine-3-carboxylate + NADPH + H+
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-
-
-
?
pyridine-3-carboxylate + NADP+ + H2O
6-hydroxy-pyridine-3-carboxylate + NADPH + H+
-
-
-
-
?
additional information
?
-
-
not as substrates: nicotinamide, isonicotinate, picolinate, nicotinic acid N-oxide, N-methylnicotinamide, trigonelline, hypoxanthine, not as electron acceptor: NAD+
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
Pusillimonas sp. (ex Stolz et al. 2005)
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after addition of an artificial electron acceptor, such as phenazine methosulfate, or 2,6-dichloroindophenol, the nicotinate hydroxylase activity is significantly increased
-
-
?
additional information
?
-
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
after addition of an artificial electron acceptor, such as phenazine methosulfate, or 2,6-dichloroindophenol, the nicotinate hydroxylase activity is significantly increased
-
-
?
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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
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH
-
first step in the anaerobic decomposition of nicotinate, NADP+ may be the natural, primary electron acceptor
-
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
-
-
-
?
3-cyanopyridine + H2O + NADP+
6-hydroxy-3-cyanopyridine + NADPH + H+
-
-
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
first step of nicotinate catabolism
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
first step of nicotinate catabolism
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
nicotinate degradation
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
nicotinate degradation
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
first step of nicotinate catabolism
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
enzyme is linked to the cytochrome respiratory chain, phenazine methosulfate may accelerate the electron transfer from the electron respiratory chain to oxygen
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
first step of nicotinate catabolism
-
?
nicotinate + H2O + electron acceptor
6-hydroxynicotinate + reduced electron acceptor
-
enzyme is linked to the cytochrome respiratory chain, phenazine methosulfate may accelerate the electron transfer from the electron respiratory chain to oxygen
-
?
nicotinate + H2O + NAD+
6-hydroxynicotinate + NADH + H+
Pusillimonas sp. (ex Stolz et al. 2005)
-
-
-
-
?
nicotinate + H2O + NAD+
6-hydroxynicotinate + NADH + H+
Pusillimonas sp. (ex Stolz et al. 2005) T2 / CCTCC M2014272
-
-
-
-
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
-
-
-
?
nicotinate + H2O + NADP+
6-hydroxynicotinate + NADPH + H+
-
-
-
?
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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
Pusillimonas sp. (ex Stolz et al. 2005)
-
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
Pusillimonas sp. (ex Stolz et al. 2005)
-
after addition of an artificial electron acceptor such as 2,6-dichloroindophenol, the nicotinate hydroxylase activity is significantly increased
phenazine methosulfate
Pusillimonas sp. (ex Stolz et al. 2005)
-
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
Pusillimonas sp. (ex Stolz et al. 2005)
-
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
1.18 micromol/min/mg protein (cells free extract)
additional information
1.89 micromol/min/mg dry weight for resting cells
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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
