Information on EC 1.14.14.57 - taurochenodeoxycholate 6alpha-hydroxylase

for references in articles please use BRENDA:EC1.14.14.57
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.14.14.57
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RECOMMENDED NAME
GeneOntology No.
taurochenodeoxycholate 6alpha-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
lithocholate + [reduced NADPH-hemoprotein reductase] + O2 = hyodeoxycholate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(2)
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-
-
taurochenodeoxycholate + [reduced NADPH-hemoprotein reductase] + O2 = taurohyocholate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(1)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
taurochenodeoxycholate,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (6alpha-hydroxylating)
A heme-thiolate protein (P-450). Requires cytochrome b5 for maximal activity. Acts on taurochenodeoxycholate, taurodeoxycholate and less readily on lithocholate and chenodeoxycholate. In adult pig (Sus scrofa), hyocholic acid replaces cholic acid as a primary bile acid [5].
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CAS REGISTRY NUMBER
COMMENTARY hide
105669-85-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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
lithocholate + [reduced NADPH-hemoprotein reductase] + O2
hyocholate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
activity is low compared to activity with taurochenodeoxycholate
-
-
?
taurochenodeoxycholate + [reduced NADPH-hemoprotein reductase] + O2
taurohyocholate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0629
taurochenodeoxycholate
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-
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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x * 53000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 53000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6alpha-hydroxylase (CYP4A21) gene: evolution by gene duplication and gene conversion
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transfection into COS cells
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.14.57)
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)