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Information on EC 1.1.1.159 - 7alpha-hydroxysteroid dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P0AET8

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IUBMB Comments
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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This record set is specific for:
Escherichia coli
UNIPROT: P0AET8
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
7alpha-hydroxysteroid dehydrogenase, 7alpha-hsdh, j-1-1, 7alpha-hsd, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7-alpha-HSDH
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-
-
-
7alpha-HSDH
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-
-
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7alpha-hydroxy steroid dehydrogenase
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-
-
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7alpha-hydroxysteroid dehydrogenase
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Bile acid-inducible protein
-
-
-
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dehydrogenase, 7alpha-hydroxy steroid
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cholate + NAD+ = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADH + H+
show the reaction diagram
belongs to the short-chain dehydrogenase/reductase 1 familiy (SDR), mechanism
cholate + NAD+ = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADH + H+
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
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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+.
CAS REGISTRY NUMBER
COMMENTARY hide
39361-64-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
bile acids + NAD(P)+
?
show the reaction diagram
dehydrogenation of hydroxyl group at position 7, wide variety of substrate binding specificities in short-chain dehydrogenase enzyme family
-
-
?
12-ketochenodeoxycholic acid + NAD+
7,12-diketochenodeoxycholic acid + NADH
show the reaction diagram
-
-
-
-
?
bile acids + NAD(P)+
?
show the reaction diagram
-
-
-
-
?
chenodeoxycholic acid + NAD(P)+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NAD(P)H
show the reaction diagram
chenodeoxycholic acid + NAD+
3alpha-hydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
show the reaction diagram
-
-
-
-
r
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
show the reaction diagram
-
-
-
-
r
cholic acid + NAD(P)+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
show the reaction diagram
-
-
-
-
?
cholic acid + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oic acid + NADH
show the reaction diagram
-
-
-
-
r
glycochenodeoxycholic acid + NAD(P)+
N-[3alpha-hydroxy-7,24-dioxocholan-24-yl]glycine + NAD(P)H
show the reaction diagram
glycocholic acid + NAD+
N-[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]glycine + NADH
show the reaction diagram
lithocholic acid + NADPH + H+
ursodeoxycholic acid + NADP+
show the reaction diagram
-
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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-
?
taurochenodeoxycholic acid + NAD+
2[[3alpha-hydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
show the reaction diagram
-
-
-
-
?
taurocholic acid + NAD+
2[[3alpha,12alpha-dihydroxy-7,24-dioxo-5beta-cholan-24-yl]amino]ethane sulfonic acid + NADH
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
bile acids + NAD(P)+
?
show the reaction diagram
dehydrogenation of hydroxyl group at position 7, wide variety of substrate binding specificities in short-chain dehydrogenase enzyme family
-
-
?
bile acids + NAD(P)+
?
show the reaction diagram
-
-
-
-
?
cholate + NAD+
3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
B-stereospecific
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
activation
KCl
-
activation
MnCl2
-
activation
NaCl
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activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
-
-
chenodeoxycholate
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substrate inhibition at concentration above 1 mM
CoCl2
CuCl2
diethyl dicarbonate
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complete
FeCl3
glycochenodeoxycholate
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substrate inhibition at concentration above 1 mM
iodoacetic acid
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70% remaining activity at concentration 1 mM
N-bromosuccinimide
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complete
o-phenanthroline
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70% remaining acitvity at concentration 1 mM
p-chloromercuribenzoate
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80% remaining activity at concentration 0.3 mM
potassium oxalate
-
-
Sodium citrate
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sodium lauryl sulfate
-
-
Sodium perchlorate
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Sodium periodate
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Sodium persulfate
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taurochenodeoxycholate
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substrate inhibition at concentration above 1 mM
Triton X-100
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-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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activation
dithiothreitol
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activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.43
chenodeoxycholic acid
0.223 - 1.2
cholic acid
0.085
glycochenodeoxycholic acid
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-
1 - 1.25
glycocholic acid
0.159 - 0.386
NAD+
0.19 - 0.24
taurochenodeoxycholic acid
1 - 2
taurocholic acid
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.18
chenodeoxycholic acid
-
-
7.92 - 151
cholic acid
0.417
glycocholic acid
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-
3.43
taurochenodeoxycholic acid
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-
3.13
taurocholic acid
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2348
-
taurocholic acid
2916
-
glycocholic acid
3486
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cholic acid
3743
-
taurochenodeoxycholic acid
3856
-
glycochenodeoxycholic acid
4164
-
chenodeoxycholic acid
45
-
deoxycholic acid or lithocholic acid
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
oxidation of cholic acid
9 - 10
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oxidation of cholic acid
9.4 - 9.6
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-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
107100
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sequence determination
120000
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gel filtration
28000
-
4 * 28000, SDS-PAGE
54000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
4 * 28000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
binary complex with NAD+, ternary complex with NADH and 7-oxoglycochenodeoxycholic acid as product, as well as possibly partially glycochenodeoxycholic acid as substrat
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K163I
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5.25% activity of wild-type activity
K163R
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63.7% activity of wild-type activity
S146A
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20.3% activity of wild-type activity
S146H
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35.6% activity of wild-type activity
Y159F
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no activity
Y159H
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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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9
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-
286085
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
10 min stable
65
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complete loss of activity within 30 min
80
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10 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation by freezing
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stabilization by glutathione, EDTA
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from Escherichia coli, high yield
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene from strain HB101 cloned in plasmid pSD1 and expressed in Escherichia coli strain DH1
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site directed mutagenesis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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assay for stereospecific labeling of coenzymes NADP+ and NADPH
synthesis
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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
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Paeniclostridium sordellii, [Clostridium] scindens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team