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7alpha-hydroxysteroid dehydrogenase

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7-alpha-hydroxysteroid dehydrogenase
Identifiers
EC no.1.1.1.159
CAS no.39361-64-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a 7alpha-hydroxysteroid dehydrogenase (EC 1.1.1.159) is an enzyme that catalyzes the chemical reaction

3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NAD+ 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+

Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate and NAD+, whereas its 3 products are 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate, NADH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7alpha-hydroxysteroid:NAD+ 7-oxidoreductase. Other names in common use include 7alpha-hydroxy steroid dehydrogenase, and 7alpha-HSDH.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1AHH, 1AHI, and 1FMC.

References

  • Haslewood ES; Haslewood GA (1976). "The specificity of a 7 alpha-hydroxy steroid dehydrogenase from Escherichia coli". Biochem. J. 157 (1): 207–10. PMC 1163832. PMID 786279.
  • MacDonald IA; Roach PD (1981). "Bile induction of 7 alpha- and 7 beta-hydroxysteroid dehydrogenases in Clostridium absonum". Biochim. Biophys. Acta. 665 (2): 262–9. doi:10.1016/0005-2760(81)90011-4. PMID 6945134.
  • Macdonald IA; Williams CN; Mahony DE (1973). "7Alpha-hydroxysteroid dehydrogenase from Escherichia coli B: preliminary studies". Biochim. Biophys. Acta. 309 (2): 243–53. doi:10.1016/0005-2744(73)90022-3. PMID 4581498.
  • Macdonald IA; Williams CN; Mahony DE; Christie WM (1975). "NAD- and NADP-dependent 7alpha-hydroxysteroid dehydrogenases from Bacteroides fragilis". Biochim. Biophys. Acta. 384 (1): 12–24. doi:10.1016/0005-2744(75)90091-1. PMID 236764.