Synergistic effects of mutations in cytochrome P450cam designed to mimic CYP101D1.

doi:10.1021/bi400676d

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Article

Synergistic effects of mutations in cytochrome P450cam designed to mimic CYP101D1.

Biochemistry - 13 Aug 2013

Batabyal Dipanwita, Li Huiying, Poulos Thomas L

Abstract excerpt

A close orthologue to cytochrome P450cam (CYP101A1) that catalyzes the same hydroxylation of camphor to 5-exo-hydroxycamphor is CYP101D1. There are potentially important differences in and around the active site that could contribute to subtle functional differences. Adjacent to the heme iron ligand, Cys357, is Leu358 in P450cam, whereas this residue is Ala in CYP101D1. Leu358 plays a role in binding of the...

Topics

Bacterial Proteins
Binding Sites
Camphor
Camphor 5-Monooxygenase
Crystallography, X-Ray
Electron Transport
Hydroxylation
Kinetics
Ligands
Models, Molecular
Mutation
Oxidation-Reduction
Protein Conformation

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Identifiers

PMID: 23865948
DOI: 10.1021/bi400676d
PMCID: PMC3790332

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