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Information on EC 1.1.1.159 - 7alpha-hydroxysteroid dehydrogenase
for references in articles please use BRENDA:EC1.1.1.159
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.159 7alpha-hydroxysteroid dehydrogenase
IUBMB Comments
Catalyses the oxidation of the 7α-hydroxy group of bile acids and alcohols both in their free and conjugated forms. The Bacteroides fragilis and Clostridium enzymes can also utilize NADP+.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.159
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chenodeoxycholic
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cholic
- testosteroni
- bacteroides
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thin-layer
-
3alpha-hydroxysteroid
- synthesis
- fragilis
-
7alpha-oh
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glycochenodeoxycholic
-
nadp-dependent
-
ursodeoxycholic
- perfringens
- degradation
- analysis
Reaction Schemes
showSynonyms
7alpha-hydroxysteroid dehydrogenase, 7alpha-hsdh, j-1-1, 7alpha-hsd, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
7-alpha-HSDH
-
-
-
-
7alpha-HSD
7alpha-HSDH
7alpha-hydroxy steroid dehydrogenase
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-
-
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7alpha-hydroxysteroid dehydrogenase
Bile acid-inducible protein
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-
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dehydrogenase, 7alpha-hydroxy steroid
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-
-
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NADP+-dependent 7alpha-HSDH
nicotinamide adenine dinucleotide phosphate-dependent 7alpha-hydroxysteroid dehydrogenase
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7alpha-HSDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cholate + NAD+ = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADH + H+
Tyr159 acts as basic catalyst, Lys163 binds to NAD(H) and lowers the pKa value of Tyr159, Ser146 stabilizes the substrate, reaction intermediate and product in catalysis
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cholate + NAD+ = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADH + H+
belongs to the short-chain dehydrogenase/reductase 1 familiy (SDR), mechanism
cholate + NAD+ = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADH + H+
short-chain dehydrogenase group
-
cholate + NAD+ = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADH + H+
catalyses the oxidation of the 7alpha-hydroxyl group of bile acids and alcohols both in their free and conjugated forms. The Bacteroides fragilis and Clostridium enzymes can also utilize NADP+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
MetaCyc
bile acids 7-O epimerization, ursodeoxycholate biosynthesis (bacteria)
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SYSTEMATIC NAME
IUBMB Comments
7alpha-hydroxysteroid:NAD+ 7-oxidoreductase
Catalyses the oxidation of the 7alpha-hydroxy group of bile acids and alcohols both in their free and conjugated forms. The Bacteroides fragilis and Clostridium enzymes can also utilize NADP+.
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CAS REGISTRY NUMBER
COMMENTARY
39361-64-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3alpha,5beta)-3-hydroxy-7,12-dioxocholan-24-oic acid + NADH
(3alpha,5beta,7alpha)-3,7-dihydroxy-12-oxocholan-24-oic acid + NAD+
3alpha,7alpha,12alpha-trihydroxycholanoyl taurine + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanoyl taurine NADH + H+ +
-
Substrates: -
Products: -
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r
3alpha,7alpha-dihydroxy-5beta-cholanoyl taurine + NAD+
3alpha-hydroxy-7-oxo-5beta-cholanoyl taurine + NADH + H+
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Substrates: i.e. chenodeoxycholic acid
Products: -
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r
6-fluoro-7-ketohyocholic acid + NADH
6-fluoro-3alpha,6alpha,7alpha-trihydroxy-5beta-cholan-24-oic acid + NAD+ + NAD+
-
Substrates: -
Products: -
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r
7,12-diketolithocholic acid + NADH
12-ketochenodeoxycholic acid + NAD+
-
Substrates: -
Products: -
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r
7-ketochenodeoxycholic acid + NADH
3alpha,7alpha-dihydroxy-5beta-cholanoic acid + NAD+
-
Substrates: -
Products: -
Products: -
r
7-ketohyocholic acid + NADH
3alpha,6alpha,7alpha-trihydroxy-5beta-cholan-24-oic acid + NAD+
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADH + H+
-
Substrates: -
Products: -
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r
chenodeoxycholic acid + NAD+
7-oxolithocholic acid + NADH + H+
-
Substrates: -
Products: -
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?
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADH + H+
-
Substrates: -
Products: -
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r
cholic acid + NADP+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADPH + H+
-
Substrates: -
Products: -
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r
dehydrocholic acid + NADH
3,12-diketolithocholic acid + NAD+
-
Substrates: -
Products: -
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r
ethyl (R)-2-hydroxy-2-(3,5-difluorophenyl)acetate + NAD+
ethyl 2-oxo-2-(3,5-difluorophenyl)acetate + NADH
-
Substrates: -
Products: -
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ethyl (R)-2-hydroxy-3,3-dimethylbutyrate + NAD+
ethyl 2-oxo-3,3-dimethylbutyrate + NADH
-
Substrates: -
Products: -
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?
ethyl (R)-2-hydroxy-3-methylbutyrate + NAD+
ethyl 2-oxo-3-methylbutyrate + NADH
-
Substrates: -
Products: -
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?
ethyl 2-hydroxy-2-(3,4-dichlorophenyl)acetate + NAD+
ethyl 2-oxo-2-(3,4-dichlorophenyl)acetate + NADH
-
Substrates: -
Products: -
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?
ethyl 2-hydroxy-2-(4-bromophenyl)acetate + NAD+
ethyl 2-oxo-2-(4-bromophenyl)acetate + NADH
-
Substrates: -
Products: -
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?
ethyl 2-hydroxy-2-(4-chlorophenyl)acetate + NAD+
ethyl 2-oxo-2-(4-chlorophenyl)acetate + NADH
-
Substrates: -
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?
ethyl 2-hydroxy-2-(4-cyanophenyl)acetate + NAD+
ethyl 2-oxo-2-(4-cyanophenyl)acetate + NADH
-
Substrates: high activity
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?
ethyl 2-hydroxy-2-(4-fluorophenyl)acetate + NAD+
ethyl 2-oxo-2-(4-fluorophenyl)acetate + NADH
-
Substrates: -
Products: -
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?
ethyl 2-hydroxy-2-(4-methylphenyl)acetate + NAD+
ethyl 2-oxo-2-(4-methylphenyl)acetate + NADH
-
Substrates: -
Products: -
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?
ethyl 2-hydroxy-2-cyclohexylacetate + NAD+
ethyl 2-oxo-2-cyclohexylacetate + NADH
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Substrates: best substrate
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?
ethyl 2-hydroxy-2-phenylacetate + NAD+
ethyl 2-oxo-2-phenylacetate + NADH
-
Substrates: -
Products: -
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?
glycochenodeoxycholic acid + NAD(P)+
?
-
Substrates: -
Products: -
Products: -
?
glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
methyl 2-hydroxy-2-phenylacetate + NAD+
methyl 2-oxo-2-phenylacetate + NADH
-
Substrates: -
Products: -
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?
taurochenodeoxycholic acid + NAD(P)+
tauroursodeoxycholic acid + NAD(P)H + H+
-
Substrates: -
Products: -
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?
taurochenodeoxycholic acid + NAD+
2[[3alpha-hydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
taurochenodeoxycholic acid + NADP+
tauro-7-ketolithocholic acid + NADPH + H+
Substrates: -
Products: -
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?
taurocholic acid + NAD+
2[[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
ursodeoxycholic acid + NAD+
7-oxolithocholic acid + NADH + H+
-
Substrates: -
Products: -
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?
(3alpha,5beta)-3-hydroxy-7,12-dioxocholan-24-oic acid + NADH
(3alpha,5beta,7alpha)-3,7-dihydroxy-12-oxocholan-24-oic acid + NAD+
-
Substrates: -
Products: -
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r
(3alpha,5beta)-3-hydroxy-7,12-dioxocholan-24-oic acid + NADH
(3alpha,5beta,7alpha)-3,7-dihydroxy-12-oxocholan-24-oic acid + NAD+
-
Substrates: -
Products: -
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r
12-ketochenodeoxycholic acid + NAD+
7,12-diketochenodeoxycholic acid + NADH
-
Substrates: -
Products: -
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r
12-ketochenodeoxycholic acid + NAD+
7,12-diketochenodeoxycholic acid + NADH
-
Substrates: -
Products: -
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?
3,7-diketocholic acid + NADH
3-ketocholic acid + NAD+
-
Substrates: high activity
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r
3,7-diketocholic acid + NADH
3-ketocholic acid + NAD+
-
Substrates: high activity
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r
7-keto-lithocholic acid + NADH
cheno-deoxycholic acid + NAD+
-
Substrates: in the gastrointestinal tract of host organisms
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?
7-keto-lithocholic acid + NADH
cheno-deoxycholic acid + NAD+
-
Substrates: -
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?
7-ketohyocholic acid + NADH
3alpha,6alpha,7alpha-trihydroxy-5beta-cholan-24-oic acid + NAD+
-
Substrates: low activity
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r
7-ketohyocholic acid + NADH
3alpha,6alpha,7alpha-trihydroxy-5beta-cholan-24-oic acid + NAD+
-
Substrates: low activity
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r
bile acids + NAD(P)+
?
-
Substrates: serve as energy sources in absence of glucose
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?
bile acids + NAD(P)+
?
Substrates: dehydrogenation of hydroxyl group at position 7, wide variety of substrate binding specificities in short-chain dehydrogenase enzyme family
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?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
Substrates: preferred substrate with NAD+ as coenzyme
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?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
Substrates: i.e. 3alpha,7alpha-dihydroxy-5beta-cholan-24-oic acid
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?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
Substrates: i.e. 3alpha,7alpha-dihydroxy-5beta-cholan-24-oic acid
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?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
Substrates: -
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?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
Substrates: i.e. 3alpha,7alpha-dihydroxy-5beta-cholan-24-oic acid
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?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
Substrates: inducible by growth on bile acids, 10fold higher enzyme activity on substrate than without induction
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?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
Products: -
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?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
Q9S3U5
Substrates: -
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r
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
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?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
Products: -
Products: -
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
Products: -
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?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
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?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
Products: -
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r
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
Products: -
Products: -
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
Products: -
Products: -
r
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
Products: -
Products: -
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
Products: -
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r
chenodeoxycholic acid + NADP+
7-ketolithocholic acid + NADPH + H+
Substrates: -
Products: -
Products: -
r
chenodeoxycholic acid + NADP+
7-ketolithocholic acid + NADPH + H+
Clostridium sardiniense DSM 1599
Substrates: -
Products: -
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r
chenodeoxycholic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
Substrates: in combination with a second reaction step with EC 1.1.1.201, 7beta-hydroxysteroid dehydrogenase, to ursodeoxycholic acid
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r
chenodeoxycholic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
Substrates: in combination with a second reaction step with EC 1.1.1.201, 7beta-hydroxysteroid dehydrogenase, to ursodeoxycholic acid
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r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
Substrates: -
Products: -
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r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
Substrates: -
Products: -
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r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
Substrates: -
Products: -
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r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
Substrates: -
Products: -
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r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
Substrates: -
Products: -
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r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
Substrates: -
Products: -
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r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
Substrates: -
Products: -
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r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
Substrates: -
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cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: preferred substrate with NADP+ as coenzyme
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?
cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
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Substrates: i.e. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate
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cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: i.e. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate
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cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
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?
cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: inducible by cholic acid
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cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
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Substrates: inducible by cholic acid
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cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
Q9S3U5
Substrates: -
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Products: -
r
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: in liquid culture, Bacteroides intestinalis AM-1 shows a relatively higher productivity than Escherichia coli HB101 and Bacteroides fragilis JCM11019T. Level of 7alpha-HSDH activity is higher in Bacteroides intestinalis AM-1 than in the other two strains
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cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: in liquid culture, Bacteroides intestinalis AM-1 shows a relatively higher productivity than Escherichia coli HB101 and Bacteroides fragilis JCM11019T. Level of 7alpha-HSDH activity is higher in Bacteroides intestinalis AM-1 than in the other two strains
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cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: in liquid culture, Bacteroides intestinalis AM-1 shows a relatively higher productivity than Escherichia coli HB101 and Bacteroides fragilis JCM11019T. Level of 7alpha-HSDH activity is higher in Bacteroides intestinalis AM-1 than in the other two strains
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cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: in liquid culture, Bacteroides intestinalis AM-1 shows a relatively higher productivity than Escherichia coli HB101 and Bacteroides fragilis JCM11019T. Level of 7alpha-HSDH activity is higher in Bacteroides intestinalis AM-1 than in the other two strains
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cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
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cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: in liquid culture, Bacteroides intestinalis AM-1 shows a relatively higher productivity than Escherichia coli HB101 and Bacteroides fragilis JCM11019T. Level of 7alpha-HSDH activity is higher in Bacteroides intestinalis AM-1 than in the other two strains
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cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
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cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
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cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
Substrates: -
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cholic acid + NADH
7-ketocholic acid + NAD+
-
Substrates: low activity in the reverse reaction
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cholic acid + NADH
7-ketocholic acid + NAD+
-
Substrates: low activity in the reverse reaction
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glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
Substrates: -
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glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
Substrates: -
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glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
Substrates: -
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glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
Substrates: i.e. N-[3alpha,7alpha-dihydroxy-24-oxocholan-24-yl]glycine, no reaction
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glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
Substrates: -
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glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
Substrates: -
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glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
-
Substrates: i.e. N-[3alpha,7alpha,12alpha-trihydroxy-24-oxocholan-24-yl]glycine
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glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
-
Substrates: -
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glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
-
Substrates: i.e. N-[3alpha,7alpha,12alpha-trihydroxy-24-oxocholan-24-yl]glycine
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glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
-
Substrates: -
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glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
-
Substrates: i.e. N-[3alpha,7alpha,12alpha-trihydroxy-24-oxocholan-24-yl]glycine
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lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
Substrates: presence of both 7alpha-HSDH and 7beta-HSDH (EC 1.1.1.201) in one organism allows epimerization by a single bacterium
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lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
Substrates: presence of both 7alpha-HSDH and 7beta-HSDH (EC 1.1.1.201) in one organism allows epimerization by a single bacterium
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Products: -
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
Substrates: presence of both 7alpha-HSDH and 7beta-HSDH (EC 1.1.1.201) in one organism allows epimerization by a single bacterium
Products: -
Products: -
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
Substrates: presence of both 7alpha-HSDH and 7beta-HSDH (EC 1.1.1.201) in one organism allows epimerization by a single bacterium
Products: -
Products: -
?
taurochenodeoxycholic acid + NAD+
2[[3alpha-hydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
Substrates: -
Products: -
Products: -
?
taurochenodeoxycholic acid + NAD+
2[[3alpha-hydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
Substrates: -
Products: -
Products: -
?
taurochenodeoxycholic acid + NADP+
? + NADPH + H+
Substrates: -
Products: -
Products: -
r
taurochenodeoxycholic acid + NADP+
? + NADPH + H+
Substrates: -
Products: -
Products: -
?
taurocholic acid + NAD+
2[[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
Substrates: i.e. 2[[3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholan-24-yl]amino]ethane sulfonic acid
Products: -
Products: -
?
taurocholic acid + NAD+
2[[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
Substrates: i.e. 2[[3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholan-24-yl]amino]ethane sulfonic acid
Products: -
Products: -
?
taurocholic acid + NAD+
2[[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
Substrates: -
Products: -
Products: -
?
taurocholic acid + NAD+
2[[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
Substrates: i.e. 2[[3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholan-24-yl]amino]ethane sulfonic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity and stereoselectivity towards various ketones, product determination, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: bile acid-induction, e.g. deoxycholate and chenodeoxycholate, is necessary for measurable activity, induction is inhibited by ursodeoxycholate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with deoxycholic acid and taurodeoxycholic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: wide variety of 5alpha- or 5beta-cholanoic acids, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: cholic acid inducible
Products: -
Products: -
?
additional information
?
-
-
Substrates: bile acid-inducible to 10fold higher activity on substrate compared to uninduced cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes the oxido-reduction of 7alpha-hydroxy bile acids including glycine and taurine conjugates
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity and cycles in bile acid pathways, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity and cycles in bile acid pathways, overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
7-keto-lithocholic acid + NADH
cheno-deoxycholic acid + NAD+
-
Substrates: in the gastrointestinal tract of host organisms
Products: -
Products: -
?
taurochenodeoxycholic acid + NADP+
tauro-7-ketolithocholic acid + NADPH + H+
Substrates: -
Products: -
Products: -
?
bile acids + NAD(P)+
?
-
Substrates: serve as energy sources in absence of glucose
Products: -
Products: -
?
bile acids + NAD(P)+
?
Substrates: dehydrogenation of hydroxyl group at position 7, wide variety of substrate binding specificities in short-chain dehydrogenase enzyme family
Products: -
Products: -
?
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
Substrates: -
Products: -
Products: -
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
Substrates: -
Products: -
Products: -
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
Substrates: -
Products: -
Products: -
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: bile acid-induction, e.g. deoxycholate and chenodeoxycholate, is necessary for measurable activity, induction is inhibited by ursodeoxycholate
Products: -
Products: -
?
additional information
?
-
-
Substrates: cholic acid inducible
Products: -
Products: -
?
additional information
?
-
-
Substrates: bile acid-inducible to 10fold higher activity on substrate compared to uninduced cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity and cycles in bile acid pathways, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity and cycles in bile acid pathways, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
the enzyme sequence contains an N-terminal Gly-X-X-X-Gly-X-Gly cofactor-binding motif
NADP+
-
one enzyme form specific for NADP+, other form specific for NAD+
NADP+
cofactor binding site structure and active state structure of the NADP+ bound to the enzyme and enzyme mutants, overview. Residue Arg38 can form the stable cation-Pi interaction with the adenine ring of NADP+, and the cation-Pi interaction and hydrogen bonds between Arg38 and NADP+ have a significant anchor effect on the cofactor binding to CA 7alpha-HSDH. Residues Arg16, Arg38 and Arg194 mediate the cofactor specificity and recognition in right orientation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
MnCl2
Mg2+
-
magnesium ion significantly enhances activity and thermostability of the enzyme. The enzymatic activity increases 40fold in the presence of 50 mM Mg2+, and T0.5 increases by approximately 6°C
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
activity is not induced by cholic acid, it is regulated in a growth phase-dependent manner
-
additional information
-
activity is not induced by cholic acid, it is regulated in a growth phase-dependent manner. No NADP-dependent activity at either growth phase
-
additional information
-
activity is not induced by cholic acid, it is regulated in a growth phase-dependent manner
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neoplasms
Fecal hydroxysteroid dehydrogenase activities in vegetarian Seventh-Day Adventists, control subjects, and bowel cancer patients.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.32 - 0.34
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl glycine
-
-
0.0601
chenodeoxycholic acid
mutant enzyme Q255L/C260S, at pH 8.0 and 25°C
0.0661
chenodeoxycholic acid
wild type enzyme, at pH 8.0 and 25°C
0.34
NADP+
wild-type enzyme, pH and temperature not specified in the publication
0.69
NADP+
wild type enzyme, pH and temperature not specified in the publication
0.72
NADP+
mutant R194G, pH and temperature not specified in the publication
0.96
NADP+
mutant enzyme R16A/R194A, pH and temperature not specified in the publication
1.77
NADP+
mutant R16G, pH and temperature not specified in the publication
2.95
NADP+
mutant enzyme T15A/R16A/R194A, pH and temperature not specified in the publication
4.25
NADP+
mutant enzyme R16A, pH and temperature not specified in the publication
4.71
NADP+
mutant enzyme R194A, pH and temperature not specified in the publication
12.33
NADP+
mutant enzyme T15A, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.34
chenodeoxycholic acid
wild type enzyme, at pH 8.0 and 25°C
21
chenodeoxycholic acid
mutant enzyme Q255L/C260S, at pH 8.0 and 25°C
3.23
NADP+
mutant enzyme T15A/R16A/R194A, pH and temperature not specified in the publication
3.86
NADP+
mutant enzyme R16A/R194A, pH and temperature not specified in the publication
4.89
NADP+
wild type enzyme, pH and temperature not specified in the publication
13.76
NADP+
wild-type enzyme, pH and temperature not specified in the publication
15.85
NADP+
mutant enzyme T15A, pH and temperature not specified in the publication
25.26
NADP+
mutant enzyme R16A, pH and temperature not specified in the publication
28.66
NADP+
mutant R194G, pH and temperature not specified in the publication
58.55
NADP+
mutant R16G, pH and temperature not specified in the publication
111.7
NADP+
mutant enzyme R194A, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
35.4
chenodeoxycholic acid
wild type enzyme, at pH 8.0 and 25°C
349.4
chenodeoxycholic acid
mutant enzyme Q255L/C260S, at pH 8.0 and 25°C
1.09
NADP+
mutant enzyme T15A/R16A/R194A, pH and temperature not specified in the publication
1.29
NADP+
mutant enzyme T15A, pH and temperature not specified in the publication
4.02
NADP+
mutant enzyme R16A/R194A, pH and temperature not specified in the publication
5.95
NADP+
mutant enzyme R16A, pH and temperature not specified in the publication
7.1
NADP+
wild type enzyme, pH and temperature not specified in the publication
23.72
NADP+
mutant enzyme R194A, pH and temperature not specified in the publication
33.18
NADP+
mutant R16G, pH and temperature not specified in the publication
39.78
NADP+
mutant R194G, pH and temperature not specified in the publication
40.1
NADP+
wild-type enzyme, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
188.3
-
with taurochenodeoxycholic acid as substrate, at pH 10.5, temperature not specified in the publication
20
-
with ethyl benzoylacetate as substrate, at pH 10.5, temperature not specified in the publication
217.6
-
with glycochenodeoxycholic acid as substrate, at pH 10.5, temperature not specified in the publication
70
additional information
additional information
-
activity in crude extracts of different strains
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
additional information
-
value for reduction of dehydrocholic acid below 5.2, not measurable due to insolubility of substrate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Clostridium sardiniense DSM 1599
formerly known as Clostridium sardiniense strain DSM599
UniProt
brenda
formerly known as Clostridium sardiniense strain DSM599
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
Comamonas testosteroni strain ATCC11996 is a Gram-negative bacterium which can use steroids as carbon and energy source
brenda
additional information
-
Comamonas testosteroni strain ATCC11996 is a Gram-negative bacterium which can use steroids as carbon and energy source
brenda
additional information
-
Comamonas testosteroni strain ATCC11996 is a Gram-negative bacterium which can use steroids as carbon and energy source
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
7alpha-hydroxysteroid dehydrogenase is a member of the short-chain dehydrogenase/reductase superfamily
evolution
the enzyme is a member of the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
7alpha-HSDHs is a member of SDR superfamily and belongs to the classical subfamily with the cofactor binding site sequence motif TA/G/SxxxGIG and the active site sequence motif YxxxK (x = any amino acid residue)
evolution
-
the enzyme is a member of the short-chain dehydrogenase/reductase (SDR) superfamily
-
malfunction
a 7alpha -HSD knockout mutant shows decreased degradation of testosterone, estradiol and cholesterol compared to the wild-type
malfunction
-
a 7alpha -HSD knockout mutant shows decreased degradation of testosterone, estradiol and cholesterol compared to the wild-type
-
physiological function
the enzyme catalyzes the dehydrogenation of C7 hydroxyl group of the steroid skeleton of bile acids
physiological function
the enzyme CA 7alpha-HSDH is responsible for reversibly catalysing the oxidation of C7alpha-oriented hydroxyl of the steroid nucleus in the bile acid metabolism
additional information
the C-terminus and residue Arg38 are essential for activity of the 7alpha-hydroxysteroid dehydrogenase from Clostridium absonum
additional information
-
the C-terminus and residue Arg38 are essential for activity of the 7alpha-hydroxysteroid dehydrogenase from Clostridium absonum
additional information
the enzyme sequence contains a Tyr-X-X-X-Lys segment, residues 161-165, that is essential for catalytic activity of SDR proteins
additional information
-
the enzyme sequence contains a Tyr-X-X-X-Lys segment, residues 161-165, that is essential for catalytic activity of SDR proteins
additional information
molecular dynamics simulation of cofactor NADPH and taurochenodeoxycholic acid bound to the enzyme, overview. The C-terminal structure of CA 7alpha-HSDH does not directly surround the substrate-binding pocket but stretch outward. The Ser-Tyr-Lys triad is well conserved in other 7alpha-HSDHs but not in the CA 7alpha-HSDH
additional information
-
the enzyme sequence contains a Tyr-X-X-X-Lys segment, residues 161-165, that is essential for catalytic activity of SDR proteins
-
Show AA Sequence and Transmembrane Helices (616 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
27000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
Q9S3U5
4 * 27400, subunit mass by SDS-PAGE, native mass by gel filtration
tetramer
the enzyme possesses the typical alpha/beta folding pattern. The residues Glu258, Gln255 and Thr253 in one subunit form hydrogen bonds with the residues His211/Ser207, Ser207, Pro151 in the other subunit, respectively
tetramer
-
4 * 25000, subunit mass by SDS-PAGE, native mass by gel filtration
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complexed with taurochenodeoxycholic acid and NADP+, sitting drop vapour diffusion method, mixing of 200 nl of 1.12 mM protein in 50 mM Tris-HCl, pH 8.0, 200 mM NaCl,and 5.6 mM of NADP+ and taurochenodeoxycholic acid, with 200 nl of reservoir solution containing 0.1 M HEPES, pH 7.5, and 25% PEG-3350, and equilibration against 0.03 ml reservoir solution, at 20°C, X-ray diffraction structure determination and analysis at 2.0 A resolution
binary complex with NAD+, ternary complex with NADH and 7-oxoglycochenodeoxycholic acid as product, as well as possibly partially glycochenodeoxycholic acid as substrat
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C260S
the mutant shows 2fold higher specific activity as compared to the wild type enzyme
L26M
the mutant shows 1.26fold higher specific activity as compared to the wild type enzyme
Q255L
the mutant shows 4.2fold higher specific activity as compared to the wild type enzyme
Q255L/C260S
the mutant shows 6.5fold higher specific activity and exhibits 10fold higher and 14fold higher catalytic efficiencies toward chenodeoxycholic acid and NADP+, respectively, as compared to the wild type enzyme. The mutant also displays significantly enhanced tolerance in the presence of high concentrations of substrate compared to the wild type
Q255R
the mutant shows 1.3fold higher specific activity as compared to the wild type enzyme
R16A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R16A/R194A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R16G
site-directed mutagenesis, kcat and Km of the R16G mutant increase by more than 4times and 5times compared with wild-type values, respectively, while the catalytic efficiency (kcat/Km) of R16G mutant decreases by 17.26% compared to the wild-type enzyme. The increase in Km indicates that affinity of R16G mutant toward NADP+ becomes weak, while the cofactor NADP(H) dissociates more easily from the binding site resulting in the increase in kcat
R194A
mutant with increased catalytic efficiency toward NADP+, as compared to the wild type enzyme
R194G
site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared with NADP+ compared to the wild-type enzyme
T15A
the catalytic efficiency of the mutant decreases by more than 4.5times, compared to the wild type and the affinity drops dramatically (Km value increases by nearly 17times)
T15A/R16A/R194A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
C260S
Clostridium sardiniense DSM 1599
-
the mutant shows 2fold higher specific activity as compared to the wild type enzyme
-
L26M
Clostridium sardiniense DSM 1599
-
the mutant shows 1.26fold higher specific activity as compared to the wild type enzyme
-
Q255L
Clostridium sardiniense DSM 1599
-
the mutant shows 4.2fold higher specific activity as compared to the wild type enzyme
-
Q255L/C260S
Clostridium sardiniense DSM 1599
-
the mutant shows 6.5fold higher specific activity and exhibits 10fold higher and 14fold higher catalytic efficiencies toward chenodeoxycholic acid and NADP+, respectively, as compared to the wild type enzyme. The mutant also displays significantly enhanced tolerance in the presence of high concentrations of substrate compared to the wild type
-
Q255R
Clostridium sardiniense DSM 1599
-
the mutant shows 1.3fold higher specific activity as 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
generation of a C-terminaly truncation enzyme mutant. When 2 and 6 amino acids of C-terminal are removed, the catalytic efficiency of Ca7alpha-HSDH remains 19.1% and 2.5%, respectively. No activity remains after deletion of 8, 14 and 17 amino acids
additional information
-
generation of a C-terminaly truncation enzyme mutant. When 2 and 6 amino acids of C-terminal are removed, the catalytic efficiency of Ca7alpha-HSDH remains 19.1% and 2.5%, respectively. No activity remains after deletion of 8, 14 and 17 amino acids
additional information
construction of a 7alpha -HSD knockout mutant that shows decreased degradation of testosterone, estradiol and cholesterol compared to the wild-type
additional information
-
construction of a 7alpha -HSD knockout mutant that shows decreased degradation of testosterone, estradiol and cholesterol compared to the wild-type
additional information
-
construction of a 7alpha -HSD knockout mutant that shows decreased degradation of testosterone, estradiol and cholesterol compared to the wild-type
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
the optimum conditions for the immobilization of the enzyme on both amino-epoxy resin and epoxy resin are pH 9.0 and 20°C for 2 h
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 65
the relative activity of the free enzyme drastically decreases at temperatures over 35°C, with minimal activity observed at 45°C. In contrast, the immobilized preparations are relatively stable at temperatures ranging from 15 to 35°C, with the relative activities of enzyme immobilized on the amino-epoxy resin and epoxy resin at 56.4% and 61.0%, respectively, after 2 h at 65°C
4 - 37
purified recombinant enzyme, no change in activity after incubation at 4°C or 25°C for 108 h, but dramatic decrease in activity at 37°C
40
65
40
-
73% of the enzyme activity is maintained after heat treatment at 40°C for 100 h
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NAD+-dependent form lyophilized is stable to freezing/thawing, NADP+-dependent form lyophilized is unstable
-
the relative activity of immobilized enzyme on aminoepoxy resin increases by approximately 80%. After 6 cycles, the residual activities of the enzyme immobilized on the amino-epoxy resin and epoxy resin are 81.4% and 89.5%, respectively
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tris-HCl (pH 9.0), 2 weeks, 24.9% loss of activity, immobilized enzyme
4°C, 50 mM Tris-HCl (pH 9.0), 5 weeks, 60.3% loss of activity, immobilized enzyme
4°C, purified enzyme, 50 mM sodium phosphate, pH 7.5, stable for 2 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 175fold by anion exchange chromatography, ammonium sulfate fractionation, hydrophobic interaction and affinity chromatography
-
recombinant enzyme from Escherichia coli by heat treatment at 55-60°C, polyethyleneimine treatment, ammonium sulfate fractionation, and gel filtration, followed by lyophilization
-
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, anion exchange chromatography, and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by metal affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CA 7alpha-HSDH, recombinant overexpression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli
expression in Escherichia coli DH5alpha-MCR, DNA and amino acid sequence analysis
-
gene 7alpha-HSD, located 11.9 kb upstream of the hsdA gene, DNA and amino acid sequence determination and analysis, phylogenetic analysis, subcloning in Escherichia coli strain HB101, sequence comparisons, recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS
gene from strain HB101 cloned in plasmid pSD1 and expressed in Escherichia coli strain DH1
-
overexpression in Escherichia coli DH5alpha, amino acid sequence analysis and comparison with other dehydrogenases
-
recombinant expression of wild-type and truncation mutant enzymes in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
new integrated chemo-enzymatic synthesis of ursodeoxycholic acid starting from sodium cholate by 7alpha- and 12alpha-hydroxysteroid dehydrogenases
synthesis
synthesis
-
the enzyme is useful as biocatalyst in the reduction of 7-keto bile acids, co-operation with cholylglycine hydrolase, EC 3.5.1.24, overview
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 as biocatalyst in the reduction of 7-keto bile acids, co-operation with cholylglycine hydrolase, EC 3.5.1.24, overview
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Prabha, V.; Gupta, M.; Seiffge, D.; Gupta, K.G.
Purification of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli strain 080
Can. J. Microbiol.
36
131-135
1990
Escherichia coli
brenda
Prabha, V.; Gupta, M.; Gupta, K.G.
Kinetic properties of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli 080
Can. J. Microbiol.
35
1076-1080
1989
Escherichia coli
brenda
Ottolina, G.; Riva, S.; Carrea, G.; Danieli, B.; Buckmann, A.F.
Enzymatic synthesis of [4R-2H]NAD (P)H and [4S-2H]NAD(P)H and determination of the stereospecificity of 7alpha- and 12alpha hydroxysteroid dehydrogenase
Biochim. Biophys. Acta
998
173-178
1989
Escherichia coli
brenda
Kinoshita, S.; Kadota, K.; Inoue, T.; Sawada, H.; Taguchi, H.
Purification and properties of three kinds of alpha-hydroxysteroid dehydrogenase from Brevibacterium fuscum DC33
J. Ferment. Technol.
66
145-152
1988
Brevibacterium fuscum
-
brenda
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
Haslewood, E.S.; Haslewood, G.A.D.
The specificity of a 7alpha-hydroxy steroid dehydrogenase from Escherichia coli
Biochem. J.
157
207-210
1976
Escherichia coli
brenda
Hylemon, P.B.; Sherrod, J.A.
Multiple forms of 7-alpha-hydroxysteroid dehydrogenase in selected strains of Bacteroides fragilis
J. Bacteriol.
122
418-424
1975
Bacteroides fragilis
brenda
MacDonald, I.A.; Williams, C.N.; Mahony, D.E.; Christie, W.M.
NAD- and NADP-dependent 7alpha-hydroxysteroid dehydrogenases from bacteroides fragilis
Biochim. Biophys. Acta
384
12-24
1975
Bacteroides fragilis
brenda
MacDonald, I.A.; Williams, C.N.; Mahony, D.E.
7alpha-hydroxysteroid dehydrogenase from Escherichia coli B: preliminary studies
Biochim. Biophys. Acta
309
243-253
1973
Escherichia coli
brenda
Tanaka, N.; Nonaka, T.; Tanabe, T.; Yoshimoto, T.; Tsuru, D.; Mitsui, Y.
Crystal structures of the binary and ternary complexes of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli
Biochemistry
35
7715-7730
1996
Escherichia coli (P0AET8), Escherichia coli
brenda
Baron, S.F.; Franklund, C.V.; Hylemon, P.B.
Cloning, sequencing, and expression of the gene coding for bile acid 7alpha-hydroxysteroid dehydrogenase from Eubacterium sp. strain VPI 12708
J. Bacteriol.
173
4558-4569
1991
Eubacterium sp., Eubacterium sp. VPI 12708
brenda
Tanabe, T.; Tanaka, N.; Uchikawa, K.; Kabashima, T.; Ito, K.; Nonaka, T.; Mitsui, Y.; Tsuru, M.; Yoshimoto, T.
Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli
J. Biochem.
124
634-641
1998
Escherichia coli
brenda
Coleman, J.P.; Hudson, L.L.; Adams, M.J.
Characterization and regulation of the NADP-linked 7alpha-hydroxysteroid dehydrogenase gene from Clostridium sordellii
J. Bacteriol.
176
4865-4874
1994
Paraclostridium sordellii
brenda
Yoshimoto, T.; Higashi, H.; Kanatani, A.; Lin, X.S.; Nagai, H.; Oyama, H.; Kurazono, K.; Tsuru, D.
Cloning and sequencing of the 7alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme
J. Bacteriol.
173
2173-2179
1991
Escherichia coli
brenda
Bennett, M.J.; McKnight, S.L.; Coleman, J.P.
Cloning and characterization of the NAD-dependent 7alpha-Hydroxysteroid dehydrogenase from Bacteroides fragilis
Curr. Microbiol.
47
475-484
2003
Bacteroides fragilis (Q9S3U5), Bacteroides fragilis, Escherichia coli, Paraclostridium sordellii, [Clostridium] scindens
brenda
Ueda, S.; Oda, M.; Imamura, S.; Ohnishi, M.
Molecular and enzymatic properties of 7alpha-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831
J. Biol. Macromol.
4
33-38
2004
Pseudomonas sp.
-
brenda
Pedrini, P.; Andreotti, E.; Guerrini, A.; Dean, M.; Fantin, G.; Giovannini, P.P.
Xanthomonas maltophilia CBS 897.97 as a source of new 7beta- and 7alpha-hydroxysteroid dehydrogenases and cholylglycine hydrolase: improved biotransformations of bile acids
Steroids
71
189-198
2006
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia CBS 897.97
brenda
Zhu, D.; Stearns, J.E.; Ramirez, M.; Hua, L.
Enzymatic enantioselective reduction of alpha-ketoesters by a thermostable 7alpha-hydroxysteroid dehydrogenase from Bacteroides fragilis
Tetrahedron
62
4535-4539
2006
Bacteroides fragilis
-
brenda
Fukiya, S.; Arata, M.; Kawashima, H.; Yoshida, D.; Kaneko, M.; Minamida, K.; Watanabe, J.; Ogura, Y.; Uchida, K.; Itoh, K.; Wada, M.; Ito, S.; Yokota, A.
Conversion of cholic acid and chenodeoxycholic acid into their 7-oxo derivatives by Bacteroides intestinalis AM-1 isolated from human feces
FEMS Microbiol. Lett.
293
263-270
2009
Bacteroides fragilis, Bacteroides fragilis NCTC 9343, Bacteroides intestinalis, Bacteroides intestinalis am-1, Escherichia coli HB101
brenda
Giovannini, P.P.; Grandini, A.; Perrone, D.; Pedrini, P.; Fantin, G.; Fogagnolo, M.
7alpha- and 12alpha-Hydroxysteroid dehydrogenases from Acinetobacter calcoaceticus lwoffii: a new integrated chemo-enzymatic route to ursodeoxycholic acid
Steroids
73
1385-1390
2008
Acinetobacter lwoffii
brenda
Eggert, T.; Bakonyi, D.; Hummel, W.
Enzymatic routes for the synthesis of ursodeoxycholic acid
J. Biotechnol.
191
11-21
2014
Acinetobacter calcoaceticus, Bacteroides fragilis, Clostridium sardiniense (G9FRD7), Escherichia coli, Pseudomonas sp., Stenotrophomonas maltophilia
brenda
Ji, W.; Chen, Y.; Zhang, H.; Zhang, X.; Li, Z.; Yu, Y.
Cloning, expression and characterization of a putative 7alpha-hydroxysteroid dehydrogenase in Comamonas testosteroni
Microbiol. Res.
169
148-154
2014
Comamonas testosteroni (S5U393), Comamonas testosteroni, Comamonas testosteroni ATCC 11996 (S5U393)
brenda
Lou, D.; Wang, B.; Tan, J.; Zhu, L.
Carboxyl-terminal and Arg38 are essential for activity of the 7alpha-hydroxysteroid dehydrogenase from Clostridium absonum
Protein Pept. Lett.
21
894-900
2014
Clostridium sardiniense (G9FRD7), Clostridium sardiniense
brenda
Yang, Q.; Li, L.; Wang, B.; Zhu, L.; Tan, J.
Modifying the microenvironment of epoxy resin to improve the activity of immobilized 7alpha-hydroxysteroid dehydrogenases
Appl. Biochem. Biotechnol.
193
925-939
2020
Clostridium sardiniense (G9FRD7)
brenda
Huang, B.; Zhao, Q.; Zhou, J.H.; Xu, G.
Enhanced activity and substrate tolerance of 7alpha-hydroxysteroid dehydrogenase by directed evolution for 7-ketolithocholic acid production
Appl. Microbiol. Biotechnol.
103
2665-2674
2019
Clostridium sardiniense (G9FRD7), Clostridium sardiniense DSM 1599 (G9FRD7)
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
Clostridium sardiniense (G9FRD7), Clostridium sardiniense DSM 599 (G9FRD7)
brenda
Lou, D.; Wang, Y.; Tan, J.; Zhu, L.; Ji, S.; Wang, B.
Functional contribution of coenzyme specificity-determining sites of 7alpha-hydroxysteroid dehydrogenase from Clostridium absonum
Comput. Biol. Chem.
70
89-95
2017
Clostridium sardiniense (G9FRD7)
brenda
Ji, S.; Pan, Y.; Zhu, L.; Tan, J.; Tang, S.; Yang, Q.; Zhang, Z.; Lou, D.; Wang, B.
A novel 7alpha-hydroxysteroid dehydrogenase Magnesium ion significantly enhances its activity and thermostability
Int. J. Biol. Macromol.
177
111-118
2021
unidentified microorganism
brenda
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