Document Detail


Structure of cytochrome P450 PimD suggests epoxidation of the polyene macrolide pimaricin occurs via a hydroperoxoferric intermediate.
MedLine Citation:
PMID:  20797613     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We present the X-ray structure of PimD, both substrate-free and in complex with 4,5-desepoxypimaricin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. Intervention in this secondary metabolic pathway could advance the development of drugs with improved pharmacologic properties. Epoxidation by P450 typically includes formation of a charge-transfer complex between an oxoferryl pi-cation radical species (Compound I) and the olefin pi-bond as the initial intermediate. Catalytic and structural evidence presented here suggest that epoxidation of 4,5-desepoxypimaricin proceeds via a hydroperoxoferric intermediate (Compound 0). The oxygen atom of Compound 0 distal to the heme iron may insert into the double bond of the substrate to make an epoxide ring. Stereoelectronic features of the putative transition state suggest substrate-assisted proton delivery.
Authors:
Petrea M Kells; Hugues Ouellet; Javier Santos-Aberturas; Jesus F Aparicio; Larissa M Podust
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Chemistry & biology     Volume:  17     ISSN:  1879-1301     ISO Abbreviation:  Chem. Biol.     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-08-27     Completed Date:  2011-01-18     Revised Date:  2013-02-04    
Medline Journal Info:
Nlm Unique ID:  9500160     Medline TA:  Chem Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  841-51     Citation Subset:  IM    
Copyright Information:
Copyright (c) 2010 Elsevier Ltd. All rights reserved.
Affiliation:
Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158, USA.
Data Bank Information
Bank Name/Acc. No.:
PDB/2X9P;  2XBK
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Anti-Bacterial Agents / chemistry*,  metabolism*
Benzene / chemistry,  metabolism
Biocatalysis
Crystallography, X-Ray
Cytochrome P-450 Enzyme System / chemistry*,  metabolism*
Epoxy Compounds / metabolism*
Models, Molecular
Molecular Sequence Data
Natamycin / chemistry*,  metabolism*
Peroxynitrous Acid / metabolism
Protein Conformation
Protons
Stereoisomerism
Substrate Specificity
Grant Support
ID/Acronym/Agency:
R01 GM025515/GM/NIGMS NIH HHS; R01 GM025515-33/GM/NIGMS NIH HHS; R01 GM078553/GM/NIGMS NIH HHS; R01 GM078553-04/GM/NIGMS NIH HHS; R01 GM25515/GM/NIGMS NIH HHS; R01GM078553/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/Epoxy Compounds; 0/Protons; 14691-52-2/Peroxynitrous Acid; 71-43-2/Benzene; 7681-93-8/Natamycin; 9035-51-2/Cytochrome P-450 Enzyme System
Comments/Corrections

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