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          Institute: MPI für medizinische Forschung     Collection: Jahrbuch 2012     Display Documents



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ID: 638078.0, MPI für medizinische Forschung / Jahrbuch 2012
Enzyme−Substrate Complementarity Governs Access to a Cationic Reaction Manifold in the P450 BM3−Catalysed Oxidation of Cyclopropyl Fatty Acids
Translation of Title:Enzyme−Substrate Complementarity Governs Access to a Cationic Reaction Manifold in the P450 BM3−Catalysed Oxidation of Cyclopropyl Fatty Acids
Authors:Cryle, Max; Hayes, Patricia Y.; De Voss, James J.
Language:English
Date of Publication (YYYY-MM-DD):2012-12-07
Title of Journal:Chemistry ˆ’ A European Journal
Journal Abbrev.:Chemistry − A European Journal
Volume:18
Issue / Number:50
Start Page:15994
End Page:15999
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:The products of cytochrome P450BM3−catalysed oxidation of cyclopropyl−containing dodecanoic acids are consistent with the presence of a cationic reaction intermediate, which results in efficient dehydrogenation of the rearranged probes by the enzyme. These results highlight the importance of enzyme−substrate complementarity, with a cationic intermediate occurring only when the probes used begin to diverge from ideal substrates for this enzyme. This also aids in reconciling literature reports supporting the presence of cationic intermediates with certain cytochrome P450 enzyme/substrate pairs
Free Keywords:carbocation;
CYP102A1;
cytochromes;
enzyme catalysis;
oxidation
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Heme and Flavin Enzymes
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Cytochrome P450
Identifiers:LOCALID:7881
URI:http%3A%2F%2Fonlinelibrary.wiley.com%2Fdoi%2F10.10...
URI:http%3A%2F%2Fonlinelibrary.wiley.com%2Fdoi%2F10.10...
URI:http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpubmed%2F23109...
DOI:10.1002%2Fchem.201203035
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