2xfh

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[[Image:2xfh.png|left|200px]]
 
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{{STRUCTURE_2xfh| PDB=2xfh | SCENE= }}
{{STRUCTURE_2xfh| PDB=2xfh | SCENE= }}
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===STRUCTURE OF CYTOCHROME P450 ERYK COCRYSTALLIZED WITH INHIBITOR CLOTRIMAZOLE.===
===STRUCTURE OF CYTOCHROME P450 ERYK COCRYSTALLIZED WITH INHIBITOR CLOTRIMAZOLE.===
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{{ABSTRACT_PUBMED_20845962}}
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==Function==
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[[http://www.uniprot.org/uniprot/CPXQ_SACEN CPXQ_SACEN]] Responsible for the C-12 hydroxylation of the macrolactone ring of erythromycin. Thus, EryK catalyzes the hydroxylation of erythromycin D (ErD) at the C-12 position to produce erythromycin C (ErC). Erythromycin B (ErB) is not a substrate for this enzyme.<ref>PMID:8416893</ref> <ref>PMID:7849045</ref>
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{{ABSTRACT_PUBMED_20845962}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:020845962</ref><references group="xtra"/>
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<ref group="xtra">PMID:020845962</ref><references group="xtra"/><references/>
[[Category: Saccharopolyspora erythraea]]
[[Category: Saccharopolyspora erythraea]]
[[Category: Gianni, S.]]
[[Category: Gianni, S.]]

Revision as of 20:52, 17 April 2013

Template:STRUCTURE 2xfh

Contents

STRUCTURE OF CYTOCHROME P450 ERYK COCRYSTALLIZED WITH INHIBITOR CLOTRIMAZOLE.

Template:ABSTRACT PUBMED 20845962

Function

[CPXQ_SACEN] Responsible for the C-12 hydroxylation of the macrolactone ring of erythromycin. Thus, EryK catalyzes the hydroxylation of erythromycin D (ErD) at the C-12 position to produce erythromycin C (ErC). Erythromycin B (ErB) is not a substrate for this enzyme.[1] [2]

About this Structure

2xfh is a 1 chain structure with sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.

Reference

  • Montemiglio LC, Gianni S, Vallone B, Savino C. Azole drugs trap cytochrome P450 EryK in alternative conformational states. Biochemistry. 2010 Sep 16. PMID:20845962 doi:10.1021/bi101062v
  1. ↑ Stassi D, Donadio S, Staver MJ, Katz L. Identification of a Saccharopolyspora erythraea gene required for the final hydroxylation step in erythromycin biosynthesis. J Bacteriol. 1993 Jan;175(1):182-9. PMID:8416893
  2. ↑ Lambalot RH, Cane DE, Aparicio JJ, Katz L. Overproduction and characterization of the erythromycin C-12 hydroxylase, EryK. Biochemistry. 1995 Feb 14;34(6):1858-66. PMID:7849045

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