1n5d: Difference between revisions
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:011279087 | <ref group="xtra">PMID:011279087</ref><references group="xtra"/><references/> | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Ghosh, D.]] | [[Category: Ghosh, D.]] | ||
Revision as of 18:06, 19 June 2013
CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASECRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE
Template:ABSTRACT PUBMED 11279087
FunctionFunction
[CBR1_PIG] NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione (By similarity).[1]
About this StructureAbout this Structure
1n5d is a 1 chain structure with sequence from Sus scrofa. This structure supersedes the now removed PDB entry 1hu4. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Ghosh D, Sawicki M, Pletnev V, Erman M, Ohno S, Nakajin S, Duax WL. Porcine carbonyl reductase. structural basis for a functional monomer in short chain dehydrogenases/reductases. J Biol Chem. 2001 May 25;276(21):18457-63. Epub 2001 Mar 8. PMID:11279087 doi:10.1074/jbc.M100538200