Roles of two surface residues near the access channel in the substrate recognition by cytochrome P450cam.

doi:10.1016/j.bpc.2008.02.016

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Article

Roles of two surface residues near the access channel in the substrate recognition by cytochrome P450cam.

Biophysical chemistry - 1 Jun 2008

Behera Rabindra Kumar, Mazumdar Shyamalava

Abstract excerpt

Detailed stopped-flow kinetics of binding of 1R-camphor to cytochrome P450cam has been studied at different temperatures for the wild type as well as for two site specific mutants T192E and S190D of the enzyme, where the surface exposed Threonine and Serine residues were mutated by acidic amino acids. The near-UV and visible circular dichroism spectra as well as the intrinsic fluorescence spectra of the WT and...

Topics

Binding Sites
Camphor 5-Monooxygenase
Kinetics
Models, Biological
Molecular Structure
Mutation
Protein Binding
Serine
Spectrum Analysis
Substrate Specificity
Thermodynamics
Threonine

Source

Open in PubMed

Identifiers

PMID: 18395959
DOI: 10.1016/j.bpc.2008.02.016

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