Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3alpha,5beta)-3-hydroxy-7,12-dioxocholan-24-oic acid + NADH
(3alpha,5beta,7alpha)-3,7-dihydroxy-12-oxocholan-24-oic acid + NAD+
-
-
-
-
r
12-ketochenodeoxycholic acid + NAD+
7,12-diketochenodeoxycholic acid + NADH
12-oxolithocholic acid + NAD+
?
-
-
-
-
r
3,7-diketocholic acid + NADH
3-ketocholic acid + NAD+
-
high activity
-
-
r
3alpha,7alpha,12alpha-trihydroxycholanoyl taurine + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanoyl taurine NADH + H+ +
-
-
-
-
r
3alpha,7alpha-dihydroxy-5beta-cholanoyl taurine + NAD+
3alpha-hydroxy-7-oxo-5beta-cholanoyl taurine + NADH + H+
-
i.e. chenodeoxycholic acid
-
-
r
6-fluoro-7-ketohyocholic acid + NADH
6-fluoro-3alpha,6alpha,7alpha-trihydroxy-5beta-cholan-24-oic acid + NAD+ + NAD+
-
-
-
-
r
7,12-diketolithocholic acid + NADH
12-ketochenodeoxycholic acid + NAD+
-
-
-
r
7-keto-lithocholic acid + NADH
cheno-deoxycholic acid + NAD+
7-ketochenodeoxycholic acid + NADH
3alpha,7alpha-dihydroxy-5beta-cholanoic acid + NAD+
-
-
-
-
r
7-ketohyocholic acid + NADH
3alpha,6alpha,7alpha-trihydroxy-5beta-cholan-24-oic acid + NAD+
-
low activity
-
-
r
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADH + H+
-
-
-
-
r
chenodeoxycholic acid + NAD+
7-oxolithocholic acid + NADH + H+
-
-
-
-
?
chenodeoxycholic acid + NADP+
7-ketolithocholic acid + NADPH + H+
chenodeoxycholic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADH + H+
-
-
-
-
r
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
cholic acid + NADH
7-ketocholic acid + NAD+
-
low activity in the reverse reaction
-
-
r
cholic acid + NADP+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADPH + H+
-
-
-
-
r
dehydrocholic acid + NADH
3,12-diketolithocholic acid + NAD+
-
-
-
r
ethyl (R)-2-hydroxy-2-(3,5-difluorophenyl)acetate + NAD+
ethyl 2-oxo-2-(3,5-difluorophenyl)acetate + NADH
-
-
-
-
?
ethyl (R)-2-hydroxy-3,3-dimethylbutyrate + NAD+
ethyl 2-oxo-3,3-dimethylbutyrate + NADH
-
-
-
-
?
ethyl (R)-2-hydroxy-3-methylbutyrate + NAD+
ethyl 2-oxo-3-methylbutyrate + NADH
-
-
-
-
?
ethyl 2-hydroxy-2-(3,4-dichlorophenyl)acetate + NAD+
ethyl 2-oxo-2-(3,4-dichlorophenyl)acetate + NADH
-
-
-
-
?
ethyl 2-hydroxy-2-(4-bromophenyl)acetate + NAD+
ethyl 2-oxo-2-(4-bromophenyl)acetate + NADH
-
-
-
-
?
ethyl 2-hydroxy-2-(4-chlorophenyl)acetate + NAD+
ethyl 2-oxo-2-(4-chlorophenyl)acetate + NADH
-
-
-
-
?
ethyl 2-hydroxy-2-(4-cyanophenyl)acetate + NAD+
ethyl 2-oxo-2-(4-cyanophenyl)acetate + NADH
-
high activity
-
-
?
ethyl 2-hydroxy-2-(4-fluorophenyl)acetate + NAD+
ethyl 2-oxo-2-(4-fluorophenyl)acetate + NADH
-
-
-
-
?
ethyl 2-hydroxy-2-(4-methylphenyl)acetate + NAD+
ethyl 2-oxo-2-(4-methylphenyl)acetate + NADH
-
-
-
-
?
ethyl 2-hydroxy-2-cyclohexylacetate + NAD+
ethyl 2-oxo-2-cyclohexylacetate + NADH
-
best substrate
-
-
?
ethyl 2-hydroxy-2-phenylacetate + NAD+
ethyl 2-oxo-2-phenylacetate + NADH
-
-
-
-
?
ethyl benzoylacetate + NAD(P)+
?
-
-
-
-
?
glycochenodeoxycholic acid + NAD(P)+
?
-
-
-
-
?
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
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
methyl 2-hydroxy-2-phenylacetate + NAD+
methyl 2-oxo-2-phenylacetate + NADH
-
-
-
-
?
methyl benzoylformate + NADH
?
-
-
-
-
?
taurochenodeoxycholic + NADP+
? + NADPH + H+
-
-
-
?
taurochenodeoxycholic acid + NAD(P)+
tauroursodeoxycholic acid + NAD(P)H + H+
-
-
-
-
?
taurochenodeoxycholic acid + NAD+
2[[3alpha-hydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
taurochenodeoxycholic acid + NADP+
? + NADPH + H+
-
-
-
r
taurochenodeoxycholic acid + NADP+
tauro-7-ketolithocholic acid + NADPH + H+
-
-
-
?
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+
-
-
-
-
?
additional information
?
-
12-ketochenodeoxycholic acid + NAD+
7,12-diketochenodeoxycholic acid + NADH
-
-
-
r
12-ketochenodeoxycholic acid + NAD+
7,12-diketochenodeoxycholic acid + NADH
-
-
-
-
?
7-keto-lithocholic acid + NADH
cheno-deoxycholic acid + NAD+
-
-
-
-
?
7-keto-lithocholic acid + NADH
cheno-deoxycholic acid + NAD+
-
in the gastrointestinal tract of host organisms
-
-
?
bile acids + NAD(P)+
?
-
serve as energy sources in absence of glucose
-
-
?
bile acids + NAD(P)+
?
-
-
-
-
?
bile acids + NAD(P)+
?
dehydrogenation of hydroxyl group at position 7, wide variety of substrate binding specificities in short-chain dehydrogenase enzyme family
-
-
?
bile acids + NAD(P)+
?
-
-
-
-
r
bile acids + NAD(P)+
?
-
-
-
-
r
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
preferred substrate with NAD+ as coenzyme
-
-
?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
i.e. 3alpha,7alpha-dihydroxy-5beta-cholan-24-oic acid
-
-
?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
i.e. 3alpha,7alpha-dihydroxy-5beta-cholan-24-oic acid
-
-
?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
-
-
-
?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
i.e. 3alpha,7alpha-dihydroxy-5beta-cholan-24-oic acid
-
-
?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
inducible by growth on bile acids, 10fold higher enzyme activity on substrate than without induction
-
-
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
r
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
r
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
r
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
?
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
r
chenodeoxycholic acid + NADP+
7-ketolithocholic acid + NADPH + H+
-
-
-
r
chenodeoxycholic acid + NADP+
7-ketolithocholic acid + NADPH + H+
-
-
-
r
chenodeoxycholic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
in combination with a second reaction step with EC 1.1.1.201, 7beta-hydroxysteroid dehydrogenase, to ursodeoxycholic acid
-
-
r
chenodeoxycholic acid + NADP+
7-oxo-lithocholic acid + NADPH + H+
in combination with a second reaction step with EC 1.1.1.201, 7beta-hydroxysteroid dehydrogenase, to ursodeoxycholic acid
-
-
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
-
-
-
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
-
-
-
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
-
-
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
-
-
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
-
-
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
-
-
-
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
-
-
-
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
-
-
-
-
r
cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
preferred substrate with NADP+ as coenzyme
-
-
?
cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
i.e. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate
-
-
?
cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
i.e. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate
-
r
cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
?
cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
inducible by cholic acid
-
-
r
cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
inducible by cholic acid
-
-
r
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
r
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
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
-
-
?
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
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
-
-
?
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
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
-
-
?
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
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
-
-
?
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
r
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
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
-
-
?
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
r
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
?
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
-
r
glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
-
-
-
?
glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
-
-
-
?
glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
-
-
-
?
glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
i.e. N-[3alpha,7alpha-dihydroxy-24-oxocholan-24-yl]glycine, no reaction
-
-
?
glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
-
-
-
r
glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
-
-
-
-
r
glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
-
-
-
-
?
glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
-
i.e. N-[3alpha,7alpha,12alpha-trihydroxy-24-oxocholan-24-yl]glycine
-
?
glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
-
i.e. N-[3alpha,7alpha,12alpha-trihydroxy-24-oxocholan-24-yl]glycine
-
-
?
glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
-
-
-
-
?
glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
-
i.e. N-[3alpha,7alpha,12alpha-trihydroxy-24-oxocholan-24-yl]glycine
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
presence of both 7alpha-HSDH and 7beta-HSDH (EC 1.1.1.201) in one organism allows epimerization by a single bacterium
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
presence of both 7alpha-HSDH and 7beta-HSDH (EC 1.1.1.201) in one organism allows epimerization by a single bacterium
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
presence of both 7alpha-HSDH and 7beta-HSDH (EC 1.1.1.201) in one organism allows epimerization by a single bacterium
-
-
?
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
-
presence of both 7alpha-HSDH and 7beta-HSDH (EC 1.1.1.201) in one organism allows epimerization by a single bacterium
-
-
?
taurochenodeoxycholic acid + NAD+
2[[3alpha-hydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
-
-
-
?
taurochenodeoxycholic acid + NAD+
2[[3alpha-hydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
-
-
-
?
taurocholic acid + NAD+
2[[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
i.e. 2[[3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholan-24-yl]amino]ethane sulfonic acid
-
-
?
taurocholic acid + NAD+
2[[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
i.e. 2[[3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholan-24-yl]amino]ethane sulfonic acid
-
-
?
taurocholic acid + NAD+
2[[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
-
-
-
?
taurocholic acid + NAD+
2[[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
-
i.e. 2[[3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholan-24-yl]amino]ethane sulfonic acid
-
-
?
additional information
?
-
-
substrate specificity and stereoselectivity towards various ketones, product determination, overview
-
-
?
additional information
?
-
-
bile acid-induction, e.g. deoxycholate and chenodeoxycholate, is necessary for measurable activity, induction is inhibited by ursodeoxycholate
-
-
?
additional information
?
-
-
no activity with deoxycholic acid and taurodeoxycholic acid
-
-
?
additional information
?
-
-
wide variety of 5alpha- or 5beta-cholanoic acids, overview
-
-
?
additional information
?
-
-
cholic acid inducible
-
-
?
additional information
?
-
-
cholic acid inducible
-
-
?
additional information
?
-
-
bile acid-inducible to 10fold higher activity on substrate compared to uninduced cells
-
-
?
additional information
?
-
-
catalyzes the oxido-reduction of 7alpha-hydroxy bile acids including glycine and taurine conjugates
-
-
?
additional information
?
-
-
substrate specificity and cycles in bile acid pathways, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
R38D
site-directed mutagenesis, inactive mutant
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
-
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
-
K163I
-
5.25% activity of wild-type activity
K163R
-
63.7% activity of wild-type activity
S146A
-
20.3% activity of wild-type activity
S146H
-
35.6% activity of wild-type activity
Y159H
-
13.3% activity of wild-type activity
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Paeniclostridium 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
[Clostridium] scindens, Paeniclostridium sordellii, Escherichia coli, Bacteroides fragilis (Q9S3U5), Bacteroides fragilis
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 intestinalis, Escherichia coli HB101, Bacteroides fragilis NCTC 9343, Bacteroides intestinalis am-1
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, Escherichia coli, Pseudomonas sp., Stenotrophomonas maltophilia, Clostridium sardiniense (G9FRD7)
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