Use of Chimeric Enzymes and Site-Directed Mutagenesis for Identification of Three Key Residues Responsible for Differences in Steroid Hydroxylation between Canine Cytochromes P-450 3A12 and 3A26

Author:

Fraser David J.,He You Qun,Harlow Greg R.,Halpert James R.

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference23 articles.

1. Sequence requirements for cytochrome P450 IIB1 catalytic activity: Alteration of the stereospecificity and regioselectivity of steroid hydroxylation by a simultaneous change of two hydrophobic amino acid residues to phenylalanine.;Aoyama;J Biol Chem,1989

2. Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli.

3. Escherichia coli expression and substrate specificities of canine cytochrome P450 3A12 and rabbit cytochrome P450 3A6.;Born;J Pharmacol Expt Ther,1996

4. cDNA and deduced amino acid sequences of a dog liver cytochrome P-450 of the IIIA gene subfamily.;Ciaccio;Biochim Biophys Acta,1991

5. Analysis of Four Residues within Substrate Recognition Site 4 of Human Cytochrome P450 3A4: Role in Steroid Hydroxylase Activity and α-Naphthoflavone Stimulation

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