Information on EC 1.1.1.393 - 3beta-hydroxycholanate 3-dehydrogenase (NADP+)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.393
-
RECOMMENDED NAME
GeneOntology No.
3beta-hydroxycholanate 3-dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
isolithocholate + NADP+ = 3-oxo-5beta-cholan-24-oate + NADPH + H+
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
iso-bile acids biosynthesis II
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Secondary bile acid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
isolithocholate:NADP+ 3-oxidoreductase
This bacterial enzyme is involved, along with EC 1.1.1.52, 3alpha-hydroxycholanate dehydrogenase (NAD+), or EC 1.1.1.392, 3alpha-hydroxycholanate dehydrogenase (NADP+), in the modification of secondary bile acids to form 3beta-bile acids (also known as iso-bile acids). The enzyme catalyses the reaction in the reduction direction in vivo. Also acts on related 3-oxo bile acids. cf. EC 1.1.1.391, 3beta-hydroxycholanate 3-dehydrogenase (NAD+).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene RUMGNA_00694
UniProt
Manually annotated by BRENDA team
gene RUMGNA_00694
UniProt
Manually annotated by BRENDA team
isolated from human intestine
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Manually annotated by BRENDA team
isolated from human intestine
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADPH + H+
3beta,12alpha-dihydroxy-5beta-cholan-24-oic acid + NADP+
show the reaction diagram
3,7,12-trioxo-5beta-cholan-24-oic acid + NADPH + H+
3beta-hydroxy-7,12-dioxo-5beta-cholan-24-oic acid + NADP+
show the reaction diagram
3beta,12alpha-dihydroxy-5beta-cholan-24-oic acid + NADP+
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADPH + H+
show the reaction diagram
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
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADPH + H+
3beta,12alpha-dihydroxy-5beta-cholan-24-oic acid + NADP+
show the reaction diagram
3,7,12-trioxo-5beta-cholan-24-oic acid + NADPH + H+
3beta-hydroxy-7,12-dioxo-5beta-cholan-24-oic acid + NADP+
show the reaction diagram
3beta,12alpha-dihydroxy-5beta-cholan-24-oic acid + NADP+
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.056
12alpha-Hydroxy-3-oxo-5beta-cholan-24-oic acid
pH 7.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
157.2
12alpha-Hydroxy-3-oxo-5beta-cholan-24-oic acid
Ruminococcus gnavus
A7AZH2
pH 7.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially, separation from 7beta-hydroxysteroid dehydrogenase, EC 1.1.1.201, by hydrophobic interaction chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene Rumgna_00694, DNA and amino acid sequence determination and analysis, encoded in a three-gene cluster that does not include any additional putative bile acid-metabolic genes, recombinant overvexpression in Escherichia coli