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UniProt functional annotation for P0AET8 | ||
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| UniProt code: P0AET8. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
7alpha-hydroxysteroid dehydrogenase involved in the metabolism of bile acids. Catalyzes the NAD(+)-dependent oxidation of the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as the major human bile acids cholate and chenodeoxycholate, to the corresponding 7- oxosteroids. To a lesser extent, can also act on taurochenodeoxycholate, taurocholate and glycocholate (PubMed:2007545). Can also use glycochenodeoxycholate as substrate (PubMed:8672472). Is not able to use NADP(+) instead of NAD(+) as the electron acceptor (PubMed:2007545). {ECO:0000269|PubMed:2007545, ECO:0000269|PubMed:8672472}. |
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| Catalytic activity: | |
Reaction=cholate + NAD(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta- cholanate + H(+) + NADH; Xref=Rhea:RHEA:19409, ChEBI:CHEBI:11893, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.159; Evidence={ECO:0000269|PubMed:2007545, ECO:0000269|PubMed:9722677}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19410; Evidence={ECO:0000305|PubMed:2007545}; |
| Catalytic activity: | |
Reaction=chenodeoxycholate + NAD(+) = 7-oxolithocholate + H(+) + NADH; Xref=Rhea:RHEA:42036, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78605; Evidence={ECO:0000269|PubMed:2007545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42037; Evidence={ECO:0000305|PubMed:2007545}; |
| Catalytic activity: | |
Reaction=NAD(+) + taurochenodeoxycholate = 7-oxotaurolithocholate + H(+) + NADH; Xref=Rhea:RHEA:53824, ChEBI:CHEBI:9407, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:137724; Evidence={ECO:0000269|PubMed:2007545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53825; Evidence={ECO:0000305|PubMed:2007545}; |
| Catalytic activity: | |
Reaction=NAD(+) + taurocholate = 7-oxo-taurodeoxycholate + H(+) + NADH; Xref=Rhea:RHEA:53848, ChEBI:CHEBI:15378, ChEBI:CHEBI:36257, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:137820; Evidence={ECO:0000269|PubMed:2007545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53849; Evidence={ECO:0000305|PubMed:2007545}; |
| Catalytic activity: | |
Reaction=glycocholate + NAD(+) = 7-oxo-glycodeoxycholate + H(+) + NADH; Xref=Rhea:RHEA:53852, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:137824; Evidence={ECO:0000269|PubMed:2007545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53853; Evidence={ECO:0000305|PubMed:2007545}; |
| Catalytic activity: | |
Reaction=glycochenodeoxycholate + NAD(+) = 7-oxoglycolithocholate + H(+) + NADH; Xref=Rhea:RHEA:53844, ChEBI:CHEBI:15378, ChEBI:CHEBI:36252, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:137818; Evidence={ECO:0000269|PubMed:8672472}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53845; Evidence={ECO:0000305|PubMed:8672472}; |
| Activity regulation: | |
Inhibited by N-bromosuccinimide, diethyl pyrocarbonate, and some metal ions such as Co(2+), Fe(2+) and Cu(2+). {ECO:0000269|PubMed:2007545}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.19 mM for taurochenodeoxycholate {ECO:0000269|PubMed:2007545}; KM=0.43 mM for chenodeoxycholate {ECO:0000269|PubMed:2007545}; KM=1.2 mM for cholate {ECO:0000269|PubMed:2007545}; KM=1.25 mM for glycocholate {ECO:0000269|PubMed:2007545}; KM=2.0 mM for taurocholate {ECO:0000269|PubMed:2007545}; KM=0.279 mM for NAD(+) {ECO:0000269|PubMed:9722677}; KM=0.361 mM for cholate {ECO:0000269|PubMed:9722677}; Note=kcat is 3798 sec(-1) with cholate as substrate (PubMed:2007545). kcat is 491 sec(-1) with chenodeoxycholate as substrate (PubMed:2007545). kcat is 206 sec(-1) with taurochenodeoxycholate as substrate (PubMed:2007545). kcat is 188 sec(-1) with taurocholate as substrate (PubMed:2007545). kcat is 25 sec(-1) with glycocholate as substrate (PubMed:2007545). kcat is 151 sec(-1) with cholate as substrate (PubMed:9722677). {ECO:0000269|PubMed:2007545, ECO:0000269|PubMed:9722677}; pH dependence: Optimum pH is 8.5 (PubMed:2007545). The enzyme is stable between pH 8 and 9 (PubMed:2007545). {ECO:0000269|PubMed:2007545}; |
| Subunit: | |
Homotetramer. {ECO:0000269|PubMed:2007545, ECO:0000269|PubMed:8672472}. |
| Similarity: | |
Belongs to the short-chain dehydrogenases/reductases (SDR) family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.