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

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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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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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redox reaction
-
-
-
-
reduction
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
nicotinate degradation III
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Nicotinate and nicotinamide metabolism
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Microbial metabolism in diverse environments
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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
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-
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Manually annotated by BRENDA team
strain DSMZ 1223
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-
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
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reduced or oxidized, as electron carrier
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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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
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crude enzyme fractions: pyruvate, ferredoxin, CoA and phosphate or arsenate required for maximal activity
phosphate
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crude enzyme fractions: pyruvate, ferredoxin, CoA and phosphate or arsenate required for maximal activity
pyruvate
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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
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-
-
0.3
methyl viologen
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-
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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
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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
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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
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SDS-PAGE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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391150
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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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
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ethylene glycol high concentrations stabilize
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glycerol, concentrations above 30% stabilize
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Na2S * 9 H2O stabilizes, maximal effect at 0.03%
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stable to freezing and thawing
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
air, 5�C, 24 h, 50% loss of activity
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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)