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Information on EC 1.1.1.201 - 7beta-hydroxysteroid dehydrogenase (NADP+)
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EC Tree
1.1.1.201 7beta-hydroxysteroid dehydrogenase (NADP+)IUBMB Comments
Catalyses the oxidation of the 7beta-hydroxy group of bile acids such as ursodeoxycholate.
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Word Map
- 1.1.1.201
- synthesis
-
ursodeoxycholic
-
taurinates
- dehydrogenases
-
nadph-dependent
- aerofaciens
- bile
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
7beta-hsdh, 7beta-hsd, 7beta-hydroxysteroid dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
7beta-HSDH
7beta-hydroxysteroid dehydrogenase
NADP-dependent 7beta-hydroxysteroid dehydrogenase
-
-
-
-
RUMGNA_02585
additional information
-
enzyme might belong to the rabbit type I 11beta-HSD enzyme family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 7beta-hydroxysteroid + NADP+ = a 7-oxosteroid + NADPH + H+
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-
-
-
a 7beta-hydroxysteroid + NADP+ = a 7-oxosteroid + NADPH + H+
Catalyses the oxidation of the 7beta-hydroxyl group of bile salts such as ursodeoxycholate
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
7beta-hydroxysteroid:NADP+ 7-oxidoreductase
Catalyses the oxidation of the 7beta-hydroxy group of bile acids such as ursodeoxycholate.
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CAS REGISTRY NUMBER
COMMENTARY
79393-83-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,7,12-triketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-3,12-diketo-5beta-cholanoic acid + NADP+
-
-
-
?
3,7,12-triketo-5beta-cholanoyl taurine + NADPH
7beta-hydroxy-3,12-diketo-5beta-cholanoyl taurine + NADP+
-
-
-
?
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
3alpha,7beta-dihydroxy-5beta-cholanoyl glycine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl glycine + NADPH
3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH
3alpha-hydroxy-7,12-diketo-5beta-cholanoic acid + NADPH
3alpha,7beta-dihydroxy-12-keto-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADPH + H+
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
5-cholesten-3beta,7beta-diol + NADP+
5-cholesten-3beta-ol-7-one + NADPH
-
i.e. 7beta-hydroxycholesterol
-
-
?
7,12-diketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-12-keto-5beta-cholanoic acid + NADP+
corticosterone + NADP+
21-hydroxy-pregn-4-ene-3,11,20-trione + NADPH
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oxidation at C-11
-
-
?
3,7-diketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-3-keto-5beta-cholanoic acid + NADP+
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-
-
?
3,7-diketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-3-keto-5beta-cholanoic acid + NADP+
-
-
-
?
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
-
-
-
?
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
-
-
-
?
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
-
partially reversible, poor substrate
-
r
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
-
ursocholic acid
-
r
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
-
ursocholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
i.e. ursodeoxycholic acid, exclusive specificity for the hydroxyl group in beta configuration at the C-7 position
-
-
r
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
i.e. ursodeoxycholic acid, exclusive specificity for the hydroxyl group in beta configuration at the C-7 position
-
-
r
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
only active on free and conjugated bile salts
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?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
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?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
activity only in the reductive reaction
-
-
ir
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
activity only in the reductive reaction
-
-
ir
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
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ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
r
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
partially reversible
-
r
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
only active on free and conjugated bile salts
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
active on both free and conjugated bile salts
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyl glycine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl glycine + NADPH
-
-
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyl glycine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl glycine + NADPH
-
-
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH
-
-
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH
-
-
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH
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partially reversible, poore substrate
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r
3alpha-hydroxy-7,12-diketo-5beta-cholanoic acid + NADPH
3alpha,7beta-dihydroxy-12-keto-5beta-cholanoic acid + NADP+
-
-
-
?
3alpha-hydroxy-7,12-diketo-5beta-cholanoic acid + NADPH
3alpha,7beta-dihydroxy-12-keto-5beta-cholanoic acid + NADP+
-
-
-
?
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADPH + H+
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
i.e. 7-oxo-lithocholic acid
i.e. ursodeoxycholic acid
-
r
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADPH + H+
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
i.e 7-oxo-lithocholic acid, the forward reaction is preferred, formation of ursodeoxycholic acid
i.e. ursodeoxycholic acid
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r
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADPH + H+
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
i.e. 7-oxo-lithocholic acid
i.e. ursodeoxycholic acid
-
r
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADPH + H+
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
i.e 7-oxo-lithocholic acid, the forward reaction is preferred, formation of ursodeoxycholic acid
i.e. ursodeoxycholic acid
-
r
7,12-diketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-12-keto-5beta-cholanoic acid + NADP+
-
-
-
?
7,12-diketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-12-keto-5beta-cholanoic acid + NADP+
-
-
-
?
7,12-dioxo-ursodeoxycholic acid + NADPH + H+
12-oxo-ursodeoxycholic acid + NADP+
-
-
-
-
?
7,12-dioxo-ursodeoxycholic acid + NADPH + H+
12-oxo-ursodeoxycholic acid + NADP+
-
-
-
-
?
7,12-dioxo-ursodeoxycholic acid + NADPH + H+
12-oxo-ursodeoxycholic acid + NADP+
-
-
-
-
?
7,12-dioxo-ursodeoxycholic acid + NADPH + H+
12-oxo-ursodeoxycholic acid + NADP+
-
-
-
-
?
7,12-dioxo-ursodeoxycholic acid + NADPH + H+
12-oxo-ursodeoxycholic acid + NADP+
-
-
-
-
?
7-ketolithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
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-
only product, 90% conversion, 71% yield
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r
7-ketolithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
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-
only product, 90% conversion, 71% yield
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r
7-oxo-lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
7-oxo-lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
after a first reaction step with EC 1.1.1.159, 7alpha-hydroxysteroid dehydrogenase, from chenodeoxycholic acid
-
-
?
7-oxo-lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
[Ruminococcus] torques ATCC 35915
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after a first reaction step with EC 1.1.1.159, 7alpha-hydroxysteroid dehydrogenase, from chenodeoxycholic acid
-
-
?
7-oxo-lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
[Ruminococcus] torques ATCC 35915
-
-
-
-
?
7beta-hydroxysteroid + NADP+
7-oxosteroid + NADPH + H+
-
-
-
r
7beta-hydroxysteroid + NADP+
7-oxosteroid + NADPH + H+
stereoselective with 7-beta-hydroxysteroids
-
-
r
7beta-hydroxysteroid + NADP+
7-oxosteroid + NADPH + H+
-
-
-
r
7beta-hydroxysteroid + NADP+
7-oxosteroid + NADPH + H+
stereoselective with 7-beta-hydroxysteroids
-
-
r
chenodeoxycholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
chenodeoxycholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
chenodeoxycholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
chenodeoxycholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
dehydrocholic acid + NADPH + H+
12-oxo-ursodeoxycholic acid + NADP+
-
-
-
-
?
dehydrocholic acid + NADPH + H+
12-oxo-ursodeoxycholic acid + NADP+
-
-
-
-
?
dehydrocholic acid + NADPH + H+
12-oxo-ursodeoxycholic acid + NADP+
-
-
-
-
?
dehydrocholic acid + NADPH + H+
12-oxo-ursodeoxycholic acid + NADP+
-
-
-
-
?
dehydrocholic acid + NADPH + H+
12-oxo-ursodeoxycholic acid + NADP+
-
-
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
presence of both 7alpha-HSDH (EC 1.1.1.159) and 7beta-HSDH in one organism allows epimerization by a single bacterium
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
presence of both 7alpha-HSDH (EC 1.1.1.159) and 7beta-HSDH in one organism allows epimerization by a single bacterium
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
presence of both 7alpha-HSDH (EC 1.1.1.159) and 7beta-HSDH in one organism allows epimerization by a single bacterium
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
presence of both 7alpha-HSDH (EC 1.1.1.159) and 7beta-HSDH in one organism allows epimerization by a single bacterium
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
presence of both 7alpha-HSDH (EC 1.1.1.159) and 7beta-HSDH in one organism allows epimerization by a single bacterium
-
-
?
ursodeoxycholic acid + NADP+
7-ketolithocholic acid + NADPH + H+
-
-
-
-
r
ursodeoxycholic acid + NADP+
7-ketolithocholic acid + NADPH + H+
-
-
-
-
r
ursodeoxycholic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
-
-
-
r
ursodeoxycholic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
-
-
-
r
additional information
?
-
no activity with chenodeoxycholic acid, i.e. 3alpha,7alpha-dihydroxy-5beta-cholan-24-oic acid
-
-
?
additional information
?
-
no activity with chenodeoxycholic acid, i.e. 3alpha,7alpha-dihydroxy-5beta-cholan-24-oic acid
-
-
?
additional information
?
-
-
enzyme might also show 11beta-hydroxysteroid dehydrogenase activity, no activity with cholesterol, 7alpha-hydroxycholesterol, 25-hydroxycholesterol, pregnenolone, dehydroepiandrosterone, chenodoxycolic acid, and ursodeoxycholic acid
-
-
?
additional information
?
-
in vivo, the forward reaction that produces ursodeoxycholic acid from 7-oxo-lithocholic acid is observed to have a growth-dependent conversion rate of 90-100% after culture in anaerobic medium broth containing 1 mM 7-oxo-lithocholic acid, while the reverse reaction is undetectable. The purified 7beta-HSDH shows a kcat/Km value that is about 55fold higher for the forward reaction than for the reverse reaction, indicating that the enzyme favors the UDCA producing reaction
-
-
?
additional information
?
-
in vivo, the forward reaction that produces ursodeoxycholic acid from 7-oxo-lithocholic acid is observed to have a growth-dependent conversion rate of 90-100% after culture in anaerobic medium broth containing 1 mM 7-oxo-lithocholic acid, while the reverse reaction is undetectable. The purified 7beta-HSDH shows a kcat/Km value that is about 55fold higher for the forward reaction than for the reverse reaction, indicating that the enzyme favors the UDCA producing reaction
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,7,12-triketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-3,12-diketo-5beta-cholanoic acid + NADP+
-
-
-
?
3,7,12-triketo-5beta-cholanoyl taurine + NADPH
7beta-hydroxy-3,12-diketo-5beta-cholanoyl taurine + NADP+
-
-
-
?
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
3alpha,7beta-dihydroxy-5beta-cholanoyl glycine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl glycine + NADPH
3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH
3alpha-hydroxy-7,12-diketo-5beta-cholanoic acid + NADPH
3alpha,7beta-dihydroxy-12-keto-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADPH + H+
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
7,12-diketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-12-keto-5beta-cholanoic acid + NADP+
3,7-diketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-3-keto-5beta-cholanoic acid + NADP+
-
-
-
?
3,7-diketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-3-keto-5beta-cholanoic acid + NADP+
-
-
-
?
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
-
-
-
?
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
-
-
-
?
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
-
partially reversible, poor substrate
-
r
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
-
ursocholic acid
-
r
3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+
3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH
-
ursocholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
only active on free and conjugated bile salts
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
activity only in the reductive reaction
-
-
ir
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
activity only in the reductive reaction
-
-
ir
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
r
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
partially reversible
-
r
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
only active on free and conjugated bile salts
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
ursodeoxycholic acid
-
?
3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH
-
active on both free and conjugated bile salts
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyl glycine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl glycine + NADPH
-
-
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyl glycine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl glycine + NADPH
-
-
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH
-
-
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH
-
-
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+
3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH
-
partially reversible, poore substrate
-
r
3alpha-hydroxy-7,12-diketo-5beta-cholanoic acid + NADPH
3alpha,7beta-dihydroxy-12-keto-5beta-cholanoic acid + NADP+
-
-
-
?
3alpha-hydroxy-7,12-diketo-5beta-cholanoic acid + NADPH
3alpha,7beta-dihydroxy-12-keto-5beta-cholanoic acid + NADP+
-
-
-
?
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADPH + H+
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
i.e. 7-oxo-lithocholic acid
i.e. ursodeoxycholic acid
-
r
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADPH + H+
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+
i.e. 7-oxo-lithocholic acid
i.e. ursodeoxycholic acid
-
r
7,12-diketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-12-keto-5beta-cholanoic acid + NADP+
-
-
-
?
7,12-diketo-5beta-cholanoic acid + NADPH
7beta-hydroxy-12-keto-5beta-cholanoic acid + NADP+
-
-
-
?
7beta-hydroxysteroid + NADP+
7-oxosteroid + NADPH + H+
-
-
-
r
7beta-hydroxysteroid + NADP+
7-oxosteroid + NADPH + H+
-
-
-
r
chenodeoxycholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
chenodeoxycholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
chenodeoxycholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
chenodeoxycholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
presence of both 7alpha-HSDH (EC 1.1.1.159) and 7beta-HSDH in one organism allows epimerization by a single bacterium
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
-
-
-
?
ursodeoxycholic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
-
-
-
r
ursodeoxycholic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
-
-
-
r
additional information
?
-
in vivo, the forward reaction that produces ursodeoxycholic acid from 7-oxo-lithocholic acid is observed to have a growth-dependent conversion rate of 90-100% after culture in anaerobic medium broth containing 1 mM 7-oxo-lithocholic acid, while the reverse reaction is undetectable. The purified 7beta-HSDH shows a kcat/Km value that is about 55fold higher for the forward reaction than for the reverse reaction, indicating that the enzyme favors the UDCA producing reaction
-
-
?
additional information
?
-
in vivo, the forward reaction that produces ursodeoxycholic acid from 7-oxo-lithocholic acid is observed to have a growth-dependent conversion rate of 90-100% after culture in anaerobic medium broth containing 1 mM 7-oxo-lithocholic acid, while the reverse reaction is undetectable. The purified 7beta-HSDH shows a kcat/Km value that is about 55fold higher for the forward reaction than for the reverse reaction, indicating that the enzyme favors the UDCA producing reaction
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme shows specificity toward NADPH/NADP+ against NADH/NAD+
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.974
3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid
pH 10.0, 37°C, recombinant enzyme
0.0388
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid
pH 6.0, 37°C, recombinant enzyme
0.021
7-oxo-lithocholic acid
-
mutant enzyme I28V/V38A/I76V/V207M, at pH 8.0 and 30°C
0.023
7-oxo-lithocholic acid
-
mutant enzyme N240I, at pH 8.0 and 30°C
0.028
7-oxo-lithocholic acid
-
mutant enzyme I112V/N240D, at pH 8.0 and 30°C
0.031
7-oxo-lithocholic acid
-
mutant enzyme T189V, at pH 8.0 and 30°C
0.034
7-oxo-lithocholic acid
-
mutant enzyme G57S/I163V/V207M, at pH 8.0 and 30°C
0.035
7-oxo-lithocholic acid
-
mutant enzyme V207M, at pH 8.0 and 30°C
0.04
7-oxo-lithocholic acid
-
mutant enzyme T189V/V207M, at pH 8.0 and 30°C
0.057
7-oxo-lithocholic acid
-
mutant enzyme K44E/T189I, at pH 8.0 and 30°C
0.19
7-oxo-lithocholic acid
-
mutant enzyme I112V/T189I/N240D, at pH 8.0 and 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.3
7-oxo-lithocholic acid
-
mutant enzyme I112V/T189I/N240D, at pH 8.0 and 30°C
7.8
7-oxo-lithocholic acid
-
mutant enzyme K44E/T189I, at pH 8.0 and 30°C
17.5
7-oxo-lithocholic acid
-
mutant enzyme I28V/V38A/I76V/V207M, at pH 8.0 and 30°C
21.4
7-oxo-lithocholic acid
-
mutant enzyme I112V/N240D, at pH 8.0 and 30°C
23
7-oxo-lithocholic acid
-
mutant enzyme T189V/V207M, at pH 8.0 and 30°C
31
7-oxo-lithocholic acid
-
mutant enzyme G57S/I163V/V207M, at pH 8.0 and 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17
7-oxo-lithocholic acid
-
mutant enzyme I112V/T189I/N240D, at pH 8.0 and 30°C
140
7-oxo-lithocholic acid
-
mutant enzyme K44E/T189I, at pH 8.0 and 30°C
580
7-oxo-lithocholic acid
-
mutant enzyme T189V/V207M, at pH 8.0 and 30°C
760
7-oxo-lithocholic acid
-
mutant enzyme I112V/N240D, at pH 8.0 and 30°C
830
7-oxo-lithocholic acid
-
mutant enzyme I28V/V38A/I76V/V207M, at pH 8.0 and 30°C
910
7-oxo-lithocholic acid
-
mutant enzyme G57S/I163V/V207M, at pH 8.0 and 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
350
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
strain N53 converts 7-oxo-lithocholic acid to ursodeoxycholic acid, and the conversion rates peaks during stationary phase, suggesting that the reductive conversion reaction is growth-dependent. In contrast, when strain N53 is cultured in the presence of ursodeoxycholic acid, 7-oxo-lithocholic acid is not detected
brenda
additional information
-
strain N53 converts 7-oxo-lithocholic acid to ursodeoxycholic acid, and the conversion rates peaks during stationary phase, suggesting that the reductive conversion reaction is growth-dependent. In contrast, when strain N53 is cultured in the presence of ursodeoxycholic acid, 7-oxo-lithocholic acid is not detected
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
the 7beta-hydroxysteroid dehydrogenase from Ruminococcus gnavus strain N53 (ATCC 29149) contributes to ursodeoxycholic acid formation in the human colon
physiological function
-
the 7beta-hydroxysteroid dehydrogenase from Ruminococcus gnavus strain N53 (ATCC 29149) contributes to ursodeoxycholic acid formation in the human colon
-
additional information
crystal structure analysis reveals a loop gating active site accessibility, the bases of the specificity for NADP+, and the general architecture of the steroid binding site. Conserved residues Ser143 and Tyr156 of 7beta-HSDH are homologous with and structurally superimpose to Ser146 and Tyr159 of 7alpha-HSDH
additional information
-
crystal structure analysis reveals a loop gating active site accessibility, the bases of the specificity for NADP+, and the general architecture of the steroid binding site. Conserved residues Ser143 and Tyr156 of 7beta-HSDH are homologous with and structurally superimpose to Ser146 and Tyr159 of 7alpha-HSDH
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HSDHB_COLAA
Collinsella aerofaciens (strain ATCC 25986 / DSM 3979 / JCM 10188 / KCTC 3647 / NCTC 11838 / VPI 1003)
263
0
28753
Swiss-Prot
-
HSDHB_RUMGV
Ruminococcus gnavus (strain ATCC 29149 / VPI C7-9)
263
0
29289
Swiss-Prot
-
DHI1_BOVIN
292
1
32309
Swiss-Prot
Secretory Pathway (Reliability: 2)
DHI1_CAVPO
300
1
33226
Swiss-Prot
Secretory Pathway (Reliability: 1)
DHI1_HUMAN
292
1
32401
Swiss-Prot
Secretory Pathway (Reliability: 2)
DHI1_MESAU
292
1
32305
Swiss-Prot
Secretory Pathway (Reliability: 1)
DHI1_MOUSE
292
1
32364
Swiss-Prot
Secretory Pathway (Reliability: 1)
DHI1_RABIT
292
1
32125
Swiss-Prot
Secretory Pathway (Reliability: 1)
DHI1_RAT
288
0
31883
Swiss-Prot
Secretory Pathway (Reliability: 2)
DHI1_SAISC
291
1
32364
Swiss-Prot
Secretory Pathway (Reliability: 2)
DHI1_SHEEP
292
1
32154
Swiss-Prot
Secretory Pathway (Reliability: 2)
D5A7S2_DROME
126
0
13392
TrEMBL
other Location (Reliability: 2)
E3TDR7_ICTPU
260
0
27009
TrEMBL
Mitochondrion (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
homodimer
a dimer of identical subunits arranged with C2 symmetry
homodimer
-
a dimer of identical subunits arranged with C2 symmetry
-
additional information
crystal structure analysis reveals a loop gating active site accessibility, the bases of the specificity for NADP+, and the general architecture of the steroid binding site
additional information
-
crystal structure analysis reveals a loop gating active site accessibility, the bases of the specificity for NADP+, and the general architecture of the steroid binding site
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme bound to NADP+, sitting drop vapor diffusion method, using 0.1 M sodium malonate pH 7.0, 12% (w/v) polyethylene glycol 3350
-
purified His-tagged enzyme complexed with NADP+, mixing of 10-15 mg/ml protein in 20% v/v glycerol, 20 mM potassium phosphate, pH 7.0, and 5 mM NADP+, with1 M sodium formate, 100 mM sodium acetate, pH 4.6, at room temperature, 3-4days, X-ray diffraction structure determination and analysis at 1.6 A resolution, modelling, molecular replacement using the the apoform structure of 7alpha-HSDH from Escherichia coli as search model, PDB ID 1AHH
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G57S/I163V/V207M
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
I112V/N240D
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
I112V/T189I/N240D
-
the mutant shows strongly decreased catalytic efficiency compared to the wild type enzyme
I28V/V38A/I76V/V207M
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
K44E/T189I
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
N240I
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
T189V
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
T189V/V207M
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
V207M
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
G57S/I163V/V207M
[Ruminococcus] torques ATCC 35915
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
I112V/N240D
[Ruminococcus] torques ATCC 35915
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
I28V/V38A/I76V/V207M
[Ruminococcus] torques ATCC 35915
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
K44E/T189I
[Ruminococcus] torques ATCC 35915
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
-
N240I
[Ruminococcus] torques ATCC 35915
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
additional information
additional information
-
development and evaluation of a selected multi-step reaction system for the synthesis of ursodeoxycholic acid, separation of each step by isolation of the intermediates using ultrafiltration membranes, overview
additional information
-
development and evaluation of a selected multi-step reaction system for the synthesis of ursodeoxycholic acid, separation of each step by isolation of the intermediates using ultrafiltration membranes, overview
additional information
-
development and evaluation of a selected multi-step reaction system for the synthesis of ursodeoxycholic acid, separation of each step by isolation of the intermediates using ultrafiltration membranes, overview
additional information
-
development and evaluation of a selected multi-step reaction system for the synthesis of ursodeoxycholic acid, separation of each step by isolation of the intermediates using ultrafiltration membranes, overview
additional information
-
development and evaluation of a selected multi-step reaction system for the synthesis of ursodeoxycholic acid, separation of each step by isolation of the intermediates using ultrafiltration membranes, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
purified recombinant His-tagged enzyme, in 100 mM MES, pH 6.0, 30 min, reductive reaction, loss of 50% activity at 50°C, and inactivation at 60°C
40
50
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM potassium phosphate, pH 8.0, stable for at least 3 months with several times of freezing and thawing
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography, Mono Q column chromatography, Mono S column chromatography and Superdex 75 gel filtration
-
native enzyme from liver microsomes 300fold by ion exchange, hydroxylapatite, 2',5'-ADP affinity
-
recombinant His6-tagged enzyme from Escherichia coli strain JM109 by nickel affinity chromatography, dialysis, and ultrafiltration
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
to homogeneity, chromatography techniques
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene RUMGNA_02585, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain JM109
recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
the enzyme is useful in production of ursodeoxycholic acid, a secondary bile acid, which is used as a drug for the treatment of various liver diseases
synthesis
-
the enzyme is useful in production of ursodeoxycholic acid, a secondary bile acid, which is used as a drug for the treatment of various liver diseases
synthesis
-
the enzyme is useful in production of ursodeoxycholic acid, a secondary bile acid, which is used as a drug for the treatment of various liver diseases
synthesis
-
the enzyme is useful in production of ursodeoxycholic acid, a secondary bile acid, which is used as a drug for the treatment of various liver diseases
synthesis
-
the enzyme is useful in production of ursodeoxycholic acid, a secondary bile acid, which is used as a drug for the treatment of various liver diseases
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
MacDonald, I.A.; Roach, P.D.
Bile induction of 7alpha- and 7beta-hydroxysteroid dehydrogenases in Clostridium absonum
Biochim. Biophys. Acta
665
262-269
1981
Clostridium sardiniense
brenda
Macdonald, I.A.; Rochon, Y.P.; Hutchinson, D.M.; Holdeman, L.V.
Formation of ursodeoxycholic acid from chenodeoxycholic acid by a 7beta-hydroxysteroid dehydrogenase-elaborating Eubacterium aerofaciens strain cocultured with 7alpha-hydroxysteroid dehydrogenase-elaborating organisms
Appl. Environ. Microbiol.
44
1187-1195
1982
Collinsella aerofaciens
brenda
Hirano, S.; Masuda, N.
Characterization of NADP-dependent 7beta-hydroxysteroid dehydrogenases from Peptostreptococcus productus and Eubacterium aerofaciens
Appl. Environ. Microbiol.
43
1057-1063
1982
Collinsella aerofaciens, Blautia producta
brenda
Sutherland, J.D.; Williams, C.N.
Bile acid induction of 7alpha- and 7beta-hydroxysteroid dehydrogenases in Clostridium limosum
J. Lipid Res.
26
344-350
1985
Hathewaya limosa
brenda
Edenharder, R.; Pfutzner, A.; Hammann, R.
Characterization of NAD-dependent 3alpha- and 3beta-hydroxysteroid dehydrogenase and of NADP-dependent 7beta-hydroxysteroid dehydrogenase from Peptostreptococcus productus
Biochim. Biophys. Acta
1004
230-238
1989
Blautia producta
brenda
Edenharder, R.; Pfutzner, A.; Hammann, R.
NADP-dependent 3beta-, 7alpha- and 7beta-hydroxysteroid dehydrogenase activities from a lecithinase-lipase-negative Clostridium species 25.11.c
Biochim. Biophys. Acta
1002
37-44
1989
Clostridium sp., Clostridium sp. 25.11.c
brenda
Shiotsuki, H.; Maeda, Y.; Chijiiwa, K.
Purification and characterization of 7beta-hydroxysteroid dehydrogenase from rabbit liver microsomes
J. Steroid Biochem. Mol. Biol.
91
185-190
2004
Oryctolagus cuniculus
brenda
Liu, L.; Aigner, A.; Schmid, R.D.
Identification, cloning, heterologous expression, and characterization of a NADPH-dependent 7beta-hydroxysteroid dehydrogenase from Collinsella aerofaciens
Appl. Microbiol. Biotechnol.
90
127-135
2011
Collinsella aerofaciens, Collinsella aerofaciens DSM 3979
brenda
Eggert, T.; Bakonyi, D.; Hummel, W.
Enzymatic routes for the synthesis of ursodeoxycholic acid
J. Biotechnol.
191
11-21
2014
Clostridium sardiniense, [Clostridium] scindens, Paeniclostridium sordellii, Collinsella aerofaciens, Fusarium equiseti
brenda
Lee, J.Y.; Arai, H.; Nakamura, Y.; Fukiya, S.; Wada, M.; Yokota, A.
Contribution of the 7beta-hydroxysteroid dehydrogenase from Ruminococcus gnavus N53 to ursodeoxycholic acid formation in the human colon
J. Lipid Res.
54
3062-3069
2013
[Ruminococcus] gnavus (A7B4V1), [Ruminococcus] gnavus ATCC 29149 (A7B4V1)
brenda
Savino, S.; Ferrandi, E.E.; Forneris, F.; Rovida, S.; Riva, S.; Monti, D.; Mattevi, A.
Structural and biochemical insights into 7beta-hydroxysteroid dehydrogenase stereoselectivity
Proteins
84
859-865
2016
Collinsella aerofaciens (A4ECA9), Collinsella aerofaciens ATCC 25986 (A4ECA9)
brenda
Wang, R.; Wu, J.; Jin, D.K.; Chen, Y.; Lv, Z.; Chen, Q.; Miao, Q.; Huo, X.; Wang, F.
Structure of NADP+-bound 7beta-hydroxysteroid dehydrogenase reveals two cofactor-binding modes
Acta Crystallogr. Sect. F
73
246-252
2017
Collinsella aerofaciens, Collinsella aerofaciens ATCC 25986
brenda
Zhang, X.; Fan, D.; Hua, X.; Zhang, T.
Large-scale production of ursodeoxycholic acid from chenodeoxycholic acid by engineering 7alpha- and 7beta-hydroxysteroid dehydrogenase
Bioprocess Biosyst. Eng.
42
1537-1545
2019
[Ruminococcus] torques, [Ruminococcus] torques ATCC 35915
brenda
Zheng, M.M.; Chen, K.C.; Wang, R.F.; Li, H.; Li, C.X.; Xu, J.H.
Engineering 7beta-hydroxysteroid dehydrogenase for enhanced ursodeoxycholic acid production by multiobjective directed evolution
J. Agric. Food Chem.
65
1178-1185
2017
[Ruminococcus] torques, [Ruminococcus] torques ATCC 35915
brenda
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