1n5d

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===CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE===
===CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE===
{{ABSTRACT_PUBMED_11279087}}
{{ABSTRACT_PUBMED_11279087}}
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==Function==
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[[http://www.uniprot.org/uniprot/CBR1_PIG 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).<ref>PMID:1377683</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:011279087</ref><ref group="xtra">PMID:015799708</ref><references group="xtra"/>
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<ref group="xtra">PMID:011279087</ref><ref group="xtra">PMID:015799708</ref><references group="xtra"/><references/>
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Ghosh, D.]]
[[Category: Ghosh, D.]]

Revision as of 08:51, 27 March 2013

Template:STRUCTURE 1n5d

Contents

CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE

Template:ABSTRACT PUBMED 11279087

Function

[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 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.

Reference

  • 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
  • Tanaka M, Bateman R, Rauh D, Vaisberg E, Ramachandani S, Zhang C, Hansen KC, Burlingame AL, Trautman JK, Shokat KM, Adams CL. An unbiased cell morphology-based screen for new, biologically active small molecules. PLoS Biol. 2005 May;3(5):e128. Epub 2005 Apr 5. PMID:15799708 doi:10.1371/journal.pbio.0030128
  1. ↑ Tanaka M, Ohno S, Adachi S, Nakajin S, Shinoda M, Nagahama Y. Pig testicular 20 beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity. cDNA cloning of pig testicular 20 beta-hydroxysteroid dehydrogenase. J Biol Chem. 1992 Jul 5;267(19):13451-5. PMID:1377683

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