Information on EC 1.3.7.1 - 6-hydroxynicotinate reductase

for references in articles please use BRENDA:EC1.3.7.1
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The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
1.3.7.1
-
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RECOMMENDED NAME
GeneOntology No.
6-hydroxynicotinate reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6-oxo-1,4,5,6-tetrahydronicotinate + oxidized ferredoxin = 6-hydroxynicotinate + reduced ferredoxin
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
nicotinate degradation III
-
-
Nicotinate and nicotinamide metabolism
-
-
Microbial metabolism in diverse environments
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-
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SYSTEMATIC NAME
IUBMB Comments
6-oxo-1,4,5,6-tetrahydronicotinate:ferredoxin oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-84-6
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain DSMZ 1223
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4,5,6-tetrahydro-6-oxonicotinate + oxidized ferredoxin
6-hydroxynicotinate + reduced ferredoxin
show the reaction diagram
6-hydroxynicotinate + reduced ferredoxin
1,4,5,6-tetrahydro-6-oxonicotinate + oxidized ferredoxin
show the reaction diagram
-
-
-
-
r
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,4,5,6-tetrahydro-6-oxonicotinate + oxidized ferredoxin
6-hydroxynicotinate + reduced ferredoxin
show the reaction diagram
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
-
crude enzyme fractions: pyruvate, ferredoxin, CoA and phosphate or arsenate required for maximal activity
Ferredoxin
-
reduced or oxidized, as electron carrier
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
one (2Fe-2S)2+/1+ and two (4Fe-4S)2+/1+ clusters
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenate
-
crude enzyme fractions: pyruvate, ferredoxin, CoA and phosphate or arsenate required for maximal activity
phosphate
-
crude enzyme fractions: pyruvate, ferredoxin, CoA and phosphate or arsenate required for maximal activity
pyruvate
-
crude enzyme fractions: pyruvate, ferredoxin, CoA and phosphate or arsenate required for maximal activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
Ferredoxin
-
-
-
0.3
methyl viologen
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
350
-
purified enzyme under strictly anaerobic conditions
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.2
-
pH 5.5: about 60% of activity maximum, pH 8.2: about 20% of activity maximum, rapid decline in activity below pH 5.6 may be partly due to destruction of ferredoxin in acid
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
-
SDS-PAGE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
391150
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
stable in liquid nitrogen, unstable in air
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cobinamide cyanide, 0.01 mM, accelerates loss of activity in air
-
ethylene glycol high concentrations stabilize
-
glycerol, concentrations above 30% stabilize
-
Na2S * 9 H2O stabilizes, maximal effect at 0.03%
-
stable to freezing and thawing
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
air, 5°C, 24 h, 50% loss of activity
-
391150
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
several months in liquid nitrogen and up to 50 h with argon
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
under strictly anaerobic conditions
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.7.1)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)