Information on EC 1.1.1.201 - 7beta-hydroxysteroid dehydrogenase (NADP+)

additional information

Substrates: enzyme might also show 11beta-hydroxysteroid dehydrogenase activity, no activity with cholesterol, 7alpha-hydroxycholesterol, 25-hydroxycholesterol, pregnenolone, dehydroepiandrosterone, chenodoxycolic acid, and ursodeoxycholic acid
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
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+

Substrates: -
Products: -

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,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

11 entries

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+

7beta-hydroxycholesterol + NADP+

7-oxocholesterol + NADPH

Substrates: -
Products: -

7beta-hydroxysteroid + NADP+

7-oxosteroid + NADPH + H+

chenodeoxycholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

lithocholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

ursodeoxycholic acid + NADP+

7-oxo-lithocholic acid + NADPH + H+

additional information

3,7,12-triketo-5beta-cholanoic acid + NADPH

7beta-hydroxy-3,12-diketo-5beta-cholanoic acid + NADP+

Substrates: -
Products: -

3,7,12-triketo-5beta-cholanoic acid + NADPH

7beta-hydroxy-3,12-diketo-5beta-cholanoic acid + NADP+

Substrates: -
Products: -

3,7-diketo-5beta-cholanoic acid + NADPH

7beta-hydroxy-3-keto-5beta-cholanoic acid + NADP+

Substrates: -
Products: -

3,7-diketo-5beta-cholanoic acid + NADPH

7beta-hydroxy-3-keto-5beta-cholanoic acid + NADP+

Substrates: -
Products: -

3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH

3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+

Substrates: -
Products: -

3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH

3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+

Substrates: -
Products: -

3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+

3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH

Substrates: partially reversible, poor substrate
Products: -

3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+

3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH

Substrates: ursocholic acid
Products: -

3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid + NADP+

3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid + NADPH

Substrates: ursocholic acid
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

286226, 286228

Substrates: ursodeoxycholic acid
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

Substrates: only active on free and conjugated bile salts
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

Substrates: ursodeoxycholic acid
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

Substrates: activity only in the reductive reaction
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

Clostridium sp. 25.11.c

Substrates: activity only in the reductive reaction
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

Substrates: ursodeoxycholic acid
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

Substrates: ursodeoxycholic acid
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

Substrates: only active on free and conjugated bile salts
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

Substrates: partially reversible
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

Substrates: ursodeoxycholic acid
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoic acid + NADP+

3alpha-hydroxy-7-oxo-5beta-cholanoic acid + NADPH

Substrates: active on both free and conjugated bile salts
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoyl glycine + NADP+

3alpha-hydroxy-7-keto-5beta-cholanoyl glycine + NADPH

Substrates: -
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoyl glycine + NADP+

3alpha-hydroxy-7-keto-5beta-cholanoyl glycine + NADPH

Substrates: -
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+

3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH

Substrates: -
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+

3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH

Substrates: -
Products: -

3alpha,7beta-dihydroxy-5beta-cholanoyl taurine + NADP+

3alpha-hydroxy-7-keto-5beta-cholanoyl taurine + NADPH

Substrates: partially reversible, poore substrate
Products: -

3alpha-hydroxy-7,12-diketo-5beta-cholanoic acid + NADPH

3alpha,7beta-dihydroxy-12-keto-5beta-cholanoic acid + NADP+

Substrates: -
Products: -

3alpha-hydroxy-7,12-diketo-5beta-cholanoic acid + NADPH

3alpha,7beta-dihydroxy-12-keto-5beta-cholanoic acid + NADP+

Substrates: -
Products: -

3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADPH + H+

3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+

Substrates: i.e. 7-oxo-lithocholic acid
Products: i.e. ursodeoxycholic acid

3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADPH + H+

3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid + NADP+

Substrates: i.e. 7-oxo-lithocholic acid
Products: i.e. ursodeoxycholic acid

7,12-diketo-5beta-cholanoic acid + NADPH

7beta-hydroxy-12-keto-5beta-cholanoic acid + NADP+

Substrates: -
Products: -

7,12-diketo-5beta-cholanoic acid + NADPH

7beta-hydroxy-12-keto-5beta-cholanoic acid + NADP+

Substrates: -
Products: -

7beta-hydroxysteroid + NADP+

7-oxosteroid + NADPH + H+

Substrates: -
Products: -

7beta-hydroxysteroid + NADP+

7-oxosteroid + NADPH + H+

Substrates: -
Products: -

chenodeoxycholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

Substrates: -
Products: -

chenodeoxycholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

Substrates: -
Products: -

chenodeoxycholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

Substrates: -
Products: -

chenodeoxycholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

Substrates: -
Products: -

chenodeoxycholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

Substrates: -
Products: -

lithocholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

Substrates: presence of both 7alpha-HSDH (EC 1.1.1.159) and 7beta-HSDH in one organism allows epimerization by a single bacterium
Products: -

lithocholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

Substrates: -
Products: -

lithocholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

Substrates: -
Products: -

lithocholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

Substrates: -
Products: -

lithocholic acid + NADPH + H+

ursodeoxycholic acid + NADP+

Substrates: -
Products: -

ursodeoxycholic acid + NADP+

7-oxo-lithocholic acid + NADPH + H+

Substrates: -
Products: -

ursodeoxycholic acid + NADP+

7-oxo-lithocholic acid + NADPH + H+

Substrates: -
Products: -

additional information

additional information

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

NADP+

15 entries

NADPH

additional information

the enzyme shows specificity toward NADPH/NADP+ against NADH/NAD+

NADP+

NADP+

NADP+

no activity with NAD+

286224, 286226

NADP+

no activity with NAD+

286226, 286228

NADP+

no activity with NAD+

NADP+

beta-form is preferred

NADP+

binding site structure analysis

NADP+

NADP+

NADP+-dependent

NADP+

NADP+-dependent

NADP+

NADP+-dependent

NADP+

NADP+-dependent

NADP+

NADP+-dependent

NADP+

dependent on

NADP+

761334, 760712

NADPH

NADPH

NADPH

dependent on

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

iodoacetate

complete inhibition at 0.05 mM

p-chloromercuribenzoic acid

complete inhibition at 0.001 mM

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.07

3,12-diketocholanoic acid

0.123

3,7,12-Triketo-5beta-cholanoic acid

0.145

3,7,12-triketo-5beta-cholanoyl taurine

0.087

3,7-Diketo-5beta-cholanoic acid

0.142

3alpha,12alpha-dihydroxy-7-keto-5beta-cholanoic acid

0.076

3alpha,7beta,12alpha-trihydroxy-5beta-cholanoic acid

0.974

3alpha,7beta-dihydroxy-5beta-cholan-24-oic acid

pH 10.0, 37°C, recombinant enzyme

0.009 - 0.108

3alpha,7beta-dihydroxy-5beta-cholanoic acid

4 entries

0.238 - 0.909

3alpha,7beta-dihydroxy-5beta-cholanoyl glycine

0.286 - 1.639

3alpha,7beta-dihydroxy-5beta-cholanoyl taurine

0.124

3alpha-Hydroxy-7,12-diketo-5beta-cholanoic acid

0.055

3alpha-hydroxy-7-keto-5beta-cholanoic acid

0.0388

3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid

pH 6.0, 37°C, recombinant enzyme

0.0052

7-ketolithocholic acid

pH 8.0, 25°C

0.021 - 0.19

7-oxo-lithocholic acid

10 entries

0.0092

Dehydrocholic acid

pH 8.0, 25°C

0.0053 - 0.4

NADP+

0.0045 - 0.047

NADPH

0.0062

Ursodeoxycholic acid

pH 8.0, 25°C

0.009

3alpha,7beta-dihydroxy-5beta-cholanoic acid

0.018

3alpha,7beta-dihydroxy-5beta-cholanoic acid

0.022

3alpha,7beta-dihydroxy-5beta-cholanoic acid

0.108

3alpha,7beta-dihydroxy-5beta-cholanoic acid

0.238

3alpha,7beta-dihydroxy-5beta-cholanoyl glycine

0.909

3alpha,7beta-dihydroxy-5beta-cholanoyl glycine

0.286

3alpha,7beta-dihydroxy-5beta-cholanoyl taurine

1.639

3alpha,7beta-dihydroxy-5beta-cholanoyl taurine

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

wild type enzyme, 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

0.0053

NADP+

pH 8.0, 25°C

0.072

NADP+

0.1

NADP+

0.14

NADP+

0.4

NADP+

0.0045

NADPH

pH 8.0, 25°C

0.0078

NADPH

wild type enzyme, at pH 8.0 and 30°C

0.047

NADPH

mutant enzyme T189V/V207M, at pH 8.0 and 30°C

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

15.8

7-ketolithocholic acid

pH 8.0, 25°C

3.3 - 31

7-oxo-lithocholic acid

10 entries

14.6

Dehydrocholic acid

pH 8.0, 25°C

15.7

NADP+

pH 8.0, 25°C

4.3 - 25.1

NADPH

19.6

Ursodeoxycholic acid

pH 8.0, 25°C

3.3

7-oxo-lithocholic acid

mutant enzyme I112V/T189I/N240D, at pH 8.0 and 30°C

4.2

7-oxo-lithocholic acid

wild type enzyme, at pH 8.0 and 30°C

7.8

7-oxo-lithocholic acid

mutant enzyme K44E/T189I, at pH 8.0 and 30°C

13.4

7-oxo-lithocholic acid

mutant enzyme N240I, at pH 8.0 and 30°C

17.3

7-oxo-lithocholic acid

mutant enzyme V207M, 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

20.1

7-oxo-lithocholic acid

mutant enzyme T189V, at pH 8.0 and 30°C

21.4

7-oxo-lithocholic acid

mutant enzyme I112V/N240D, at pH 8.0 and 30°C

7-oxo-lithocholic acid

mutant enzyme T189V/V207M, at pH 8.0 and 30°C

7-oxo-lithocholic acid

mutant enzyme G57S/I163V/V207M, at pH 8.0 and 30°C

4.3

NADPH

wild type enzyme, at pH 8.0 and 30°C

17.2

NADPH

pH 8.0, 25°C

25.1

NADPH

mutant enzyme T189V/V207M, at pH 8.0 and 30°C

show all columns Go to kcat/KM Value Search

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

17 - 910

7-oxo-lithocholic acid

10 entries

530 - 550

NADPH

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

180

7-oxo-lithocholic acid

wild type enzyme, at pH 8.0 and 30°C

480

7-oxo-lithocholic acid

mutant enzyme V207M, at pH 8.0 and 30°C

580

7-oxo-lithocholic acid

mutant enzyme N240I, at pH 8.0 and 30°C

580

7-oxo-lithocholic acid

mutant enzyme T189V/V207M, at pH 8.0 and 30°C

640

7-oxo-lithocholic acid

mutant enzyme T189V, 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

530

NADPH

mutant enzyme T189V/V207M, at pH 8.0 and 30°C

550

NADPH

wild type enzyme, at pH 8.0 and 30°C

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.1

crude cell extract

0.17

0.276

purified enzyme

1.06

350

350

pH and temperature not specified in the publication

350

pH and temperature not specified in the publication

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glycine-NaOH buffer

assay at, ursodeoxycholic acid formation

6.5

7.7

potassium buffer

8.6

9.1 - 11

9.5

9.5 - 10.5

9.8 - 10.3

9.8 - 10.5

assay at, 7-oxo-lithocholic acid formation

show all columns Go to pH Range Search

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 - 11.5

activity range

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

assay at

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

286226, 286228

brenda

286076, 740787

brenda

brenda

Clostridium sp. 25.11.c

brenda

Collinsella aerofaciens DSM 3979

brenda

brenda

brenda

isolated from human feces

UniProt

brenda

isolated from human feces

UniProt

brenda

brenda

brenda

formerly Eubacterium sp.

brenda

760712, 761334

brenda

[Ruminococcus] torques ATCC 35915

760712, 761334

brenda

286224, 286226, 724054, 740787

brenda

UniProt

brenda

brenda

UniProt

brenda

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

7 entries

liver

brenda

additional information

brenda

brenda

bile salt induction of enzymes synthesis

brenda

brenda

Clostridium sp. 25.11.c

brenda

286224, 286226

brenda

bile salt induction of enzymes synthesis

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

additional information

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

brenda

brenda

brenda

brenda

16020

brenda

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Highest Expressing Human Cell Lines

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show all columns Go to General Information Search

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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

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Show AA Sequence and Transmembrane Helices (997 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.

Go to PDB and Structure Links Search

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PDB

SCOP

CATH

UNIPROT

ORGANISM

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

115000

gel filtration

30000

2 * 30000, SDS-PAGE

34000

x * 34000, SDS-PAGE

45000

gel filtration

53000

gel filtration

56100

show all columns Go to Subunit Search

gel filtration

82000

gel filtration

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dimer

homodimer

additional information

x * 34000, SDS-PAGE

x * 30000, SDS-PAGE

760712

[Ruminococcus] torques ATCC 35915

x * 30000, SDS-PAGE

dimer

2 * 30000, SDS-PAGE

Collinsella aerofaciens DSM 3979

dimer

2 * 30000, SDS-PAGE

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

Go to Crystallization (commentary) Search

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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

show all columns Go to Protein Variants Search

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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

additional information

additional information

additional information

show all columns Go to Temperature Stability Search

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

50% loss of activity within 60 min

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

melting temperature

50% loss of activity within 30 min

complete inactivation within 400 min

90% loss of activity within 3 min

complete inactivation within 5 min

Go to General Stability Search

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

heat-sensitive

presence of reducing agents protects against thermal denaturation

Go to Storage Stability Search

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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

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

GST-Sefinose affinity column chromatography

760712

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

to homogeneity, chromatography techniques

to homogeneity, chromatography techniques

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Escherichia coli BL21(DE3) cells

expression in Escherichia coli

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)

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells

761334, 760712

show all columns Go to Application Search

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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

top print hide References Search

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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

6945134

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.

1187-1195

1982

Collinsella aerofaciens

6758698

brenda

Hirano, S.; Masuda, N.

Characterization of NADP-dependent 7beta-hydroxysteroid dehydrogenases from Peptostreptococcus productus and Eubacterium aerofaciens

Appl. Environ. Microbiol.

1057-1063

1982

Collinsella aerofaciens, Blautia producta

6954878

brenda

Sutherland, J.D.; Williams, C.N.

Bile acid induction of 7alpha- and 7beta-hydroxysteroid dehydrogenases in Clostridium limosum

J. Lipid Res.

344-350

1985

Hathewaya limosa

3857290

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

2752021

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

2923864

brenda

Shiotsuki, H.; Maeda, Y.; Chijiiwa, K.

Purification and characterization of 7beta-hydroxysteroid dehydrogenase from rabbit liver microsomes

J. Steroid Biochem. Mol. Biol.

185-190

2004

Oryctolagus cuniculus

15276626

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.

127-135

2011

Collinsella aerofaciens, Collinsella aerofaciens DSM 3979

21181147

brenda

Eggert, T.; Bakonyi, D.; Hummel, W.

Enzymatic routes for the synthesis of ursodeoxycholic acid

J. Biotechnol.

191

11-21

2014

Clostridium sardiniense, Collinsella aerofaciens, Fusarium equiseti, Paraclostridium sordellii, [Clostridium] scindens

25131646

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.

3062-3069

2013

Mediterraneibacter gnavus (A7B4V1), Mediterraneibacter gnavus ATCC 29149 (A7B4V1)

23729502

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

859-865

2016

Collinsella aerofaciens (A4ECA9), Collinsella aerofaciens ATCC 25986 (A4ECA9)

27006087

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

246-252

2017

Collinsella aerofaciens, Collinsella aerofaciens ATCC 25986

28471355

brenda

760712

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.

1537-1545

2019

[Ruminococcus] torques, [Ruminococcus] torques ATCC 35915

31152232

brenda