Information on EC 1.1.1.391 - 3beta-hydroxycholanate 3-dehydrogenase (NAD+)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.391
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RECOMMENDED NAME
GeneOntology No.
3beta-hydroxycholanate 3-dehydrogenase (NAD+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
isolithocholate + NAD+ = 3-oxo-5beta-cholan-24-oate + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycocholate metabolism (bacteria)
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iso-bile acids biosynthesis I
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Secondary bile acid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
isolithocholate:NAD+ 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 1.1.1.393, 3beta-hydroxycholanate 3-dehydrogenase (NADP+).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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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-5-beta-cholan-24-oic acid + NADH + H+
3beta,12alpha-hydroxy-5-beta-cholan-24-oic acid + NAD+
show the reaction diagram
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
3beta,12alpha-dihydroxy-5beta-cholan-24-oic acid + NAD+
show the reaction diagram
3,12-dioxo-5-beta-cholan-24-oic acid + NADH + H+
3beta-hydroxy-12-oxo-5beta-cholan-24-oic acid + NAD+
show the reaction diagram
3,12-dioxo-5beta-cholan-24-oic acid + NADH + H+
3beta-hydroxy-12-oxo-5beta-cholan-24-oic acid + NAD+
show the reaction diagram
3,7-dioxo-5beta-cholan-24-oic acid + NADH + H+
3beta-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD+
show the reaction diagram
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?
3beta,7alpha-dihydroxy-5beta-cholan-24-oic acid + NAD+
7alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
show the reaction diagram
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i.e. isochenodeoxycholic acid
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3beta,7beta-dihydroxy-5beta-cholan-24-oic acid + NAD+
7beta-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
show the reaction diagram
3beta-hydroxy-5beta-cholan-24-oic acid + NAD+
3-oxo-5beta-cholan-24-oic acid + NADH + H+
show the reaction diagram
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i.e. isolithocholic acid
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?
3beta12alpha-dihydroxy-5beta-cholan-24-oic acid + NAD+
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
show the reaction diagram
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i.e. isodeoxycholic acid
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?
7alpha,12alpha-dihydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
3beta,7alpha,12alpha-trihydroxy-5beta-cholan-24-oic acid + NAD+
show the reaction diagram
7alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
3beta,7alpha-dihydroxy-5beta-cholan-24-oic acid + NAD+
show the reaction diagram
additional information
?
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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
12alpha-hydroxy-3-oxo-5-beta-cholan-24-oic acid + NADH + H+
3beta,12alpha-hydroxy-5-beta-cholan-24-oic acid + NAD+
show the reaction diagram
3,12-dioxo-5-beta-cholan-24-oic acid + NADH + H+
3beta-hydroxy-12-oxo-5beta-cholan-24-oic acid + NAD+
show the reaction diagram
3beta,7beta-dihydroxy-5beta-cholan-24-oic acid + NAD+
7beta-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
show the reaction diagram
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substrate docking of isoursodeoxycholic acid to the active site of a three-dimensional model of human class I gammagamma alcohol dehydrogenase reveals that the ADH gammagamma isozyme is the iso bile acid 3beta-hydroxysteroid dehydrogenase present in human liver cytosol, with NAD+ as a cofactor, but ethanol is the preferred substrate
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7alpha,12alpha-dihydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
3beta,7alpha,12alpha-trihydroxy-5beta-cholan-24-oic acid + NAD+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no activity with NADP+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-oxo bile acids
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the specific enzyme activity is significantly reduced by growth medium supplementation with 3-oxo bile acids, with trisubstituted acids being more effective than disubstituted ones
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Bile acids
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specific enzymatic activities are significantly reduced when bacteria are grown in the presence of 3-oxo bile acids, while other bile acids are ineffective
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.63 - 2.66
12alpha-hydroxy-3-oxo-5-beta-cholan-24-oic acid
0.0153
3beta,7alpha-dihydroxy-5beta-cholan-24-oic acid
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pH 7.5, 25C, recombinant enzyme
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0.0238
3beta,7beta-dihydroxy-5beta-cholan-24-oic acid
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pH 7.5, 25C, recombinant enzyme
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0.0183 - 0.0283
3beta-hydroxy-5beta-cholan-24-oic acid
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additional information
additional information
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Michaelis-Menten kinetis
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.73 - 29.71
12alpha-hydroxy-3-oxo-5-beta-cholan-24-oic acid
0.022
3beta,7alpha-dihydroxy-5beta-cholan-24-oic acid
Homo sapiens
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pH 7.5, 25C, recombinant enzyme
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0.033
3beta,7beta-dihydroxy-5beta-cholan-24-oic acid
Homo sapiens
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pH 7.5, 25C, recombinant enzyme
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0.015 - 0.047
3beta-hydroxy-5beta-cholan-24-oic acid
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
3beta,7alpha-dihydroxy-5beta-cholan-24-oic acid
Homo sapiens
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pH 7.5, 25C, recombinant enzyme
210510
1.4
3beta,7beta-dihydroxy-5beta-cholan-24-oic acid
Homo sapiens
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pH 7.5, 25C, recombinant enzyme
210511
0.82 - 1.66
3beta-hydroxy-5beta-cholan-24-oic acid
210509
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.35
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pH 9.5, 25C, substrate 3,7-dioxo-5beta-cholan-24-oic acid
0.38
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pH 9.5, 25C, substrate 7alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid
0.59
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pH 9.5, 25C, substrate 3,12-dioxo-5beta-cholan-24-oic acid
1
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pH 9.5, 25C, substrate 7alpha,12alpha-3-oxo-dihydroxy-5beta-cholan-24-oic acid
2.12
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pH 9.5, 25C, substrate 3,7,12-trioxo-5beta-cholan-24-oic acid
2.35
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pH 9.5, 25C, substrate 3,7-dioxo-5beta-cholan-24-oic acid
2.45
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pH 9.5, 25C, substrate 3beta,12alpha-dihydroxy-5beta-cholan-24-oic acid
2.49
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pH 9.5, 25C, substrate 12alpha-hydroxy-3-oxo-5beta-cholate
3.2
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purified enzyme, pH 10.0-10.2, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
assay at; assay at
7.5
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assay at
10 - 10.02
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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crude cell extract, prepared in 0.1 M Tris-HCl, pH 8.5, 1.0 mM EDTA, and 1.0 mM DTT in absence of bile acid substrate, stable for several hours and detectable for at least 36 h
37
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pH 9.5, activity is reduced to about 20% within 1 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT stabilizes, while ETA has no influence on enzyme stability
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EDTA has no effect enzyme thermal stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, crude enzyme extract, pH 8.5, in the presence of dithiothreitol, no loss of activity after 24 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 6.3fold by anion exchange chromatography and gel filtration
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native enzyme by anion exchange chromatography and gel filtration
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recombinant class I ADH g2g2 isozymes from Escherichia coli by anion exchange and 5'-AMP-affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene Elen_0198, DNA and amino acid sequence determination and analysis, recombinant overvexpression in Escherichia coli; gene Elen_1325, DNA and amino acid sequence determination and analysis, recombinant overvexpression in Escherichia coli
recombinant class I ADH g2g2 isozymes cloning and overexpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
effect of bile acids on the production of 3beta-HSDH activity in Clostridium innocuum strain D1144/3