Linked Life Data

17047872

Source:http://linkedlifedata.com/resource/pubmed/id/17047872

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2006-10-18
pubmed:abstractText
The fundamental nature of reactivity in cytochrome P450 enzymes is currently controversial. Modelling of bacterial P450cam has suggested an important role for the haem propionates in the catalysis, though this finding has been questioned. Understanding the mechanisms of this enzyme family is important both in terms of basic biochemistry and potentially in the prediction of drug metabolism. We have modelled the hydroxylation of camphor by P450cam, using combined quantum mechanics/molecular mechanics (QM/MM) methods. A set of reaction pathways in the enzyme was determined. We were able to pinpoint the source of the discrepancies in the previous results. We show that when a correct ionization state is assigned to Asp297, no spin density appears on the haem propionates and the protein structure in this region remains preserved. These results indicate that the haem propionates are not involved in catalysis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1477-0520
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3931-7
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Mechanisms of reaction in cytochrome P450: Hydroxylation of camphor in P450cam.
pubmed:affiliation
Centre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol, UK BS8 1TS.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't