Microsomal cytochrome P450 2C5: comparison to microbial P450s and unique features.

doi:10.1016/s0162-0134(00)00102-1

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Article

Microsomal cytochrome P450 2C5: comparison to microbial P450s and unique features.

Journal of inorganic biochemistry - 31 Aug 2000

Williams P A, Cosme J, Sridhar V, Johnson E F, McRee D E

Abstract excerpt

Although microsomal P450s represent the majority of P450s, only microbial P450s have been amenable to crystal structure solution. We have recently solved the first crystal structure of a microsomal P450, 2C5, a progesterone hydroxylase from rabbit. We discuss the features of the protein in common with existing structures of microbial P450s and limitations of homology modeling mammalian P450s based on the...

Topics

Animals
Binding Sites
Crystallography, X-Ray
Cytochrome P-450 Enzyme System
Cytochrome P450 Family 2
Microsomes
Mixed Function Oxygenases
Models, Molecular
Mutation
NADPH-Ferrihemoprotein Reductase
Progesterone
Protein Binding
Protein Structure, Secondary
Rabbits
Steroid 21-Hydroxylase
Substrate Specificity

Source

Open in PubMed

Identifiers

PMID: 11051563
DOI: 10.1016/s0162-0134(00)00102-1

Provenance

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