RRC ID 54404
Author Ishida N, Aoyama Y, Hatanaka R, Oyama Y, Imajo S, Ishiguro M, Oshima T, Nakazato H, Noguchi T, Maitra US.
Title A single amino acid substitution converts cytochrome P450(14DM) to an inactive form, cytochrome P450SG1: complete primary structures deduced from cloned DNAS.
Journal Biochem Biophys Res Commun
Abstract Genes for lanosterol 14-demethylase, cytochrome P450(14DM), and a mutated inactive cytochrome P450SG1 were cloned from S. cerevisiae strains D587 and SG1, respectively. A single nucleotide change resulting in substitution of Asp for Gly-310 of cytochrome P450(14DM) was found to have occurred in cytochrome P450SG1. In this protein the 6th ligand to heme iron is a histidine residue instead of a water molecule, which may be the ligand for the active cytochrome P450(14DM). Molecular models of the active sites of the cytochrome P450(14DM) and cytochrome P450SG1 were built by computer modeling on the basis of the known structure of that of cytochrome P450CAM whose crystallographic data are available. The mechanisms which may cause a histidine residue to gain access to the heme iron are discussed.
Volume 155(1)
Pages 317-23
Published 1988-8-30
DOI 10.1016/s0006-291x(88)81087-8
PII S0006-291X(88)81087-8
PMID 3046615
MeSH Amino Acid Sequence Base Sequence Cloning, Molecular* Cytochrome P-450 Enzyme System / genetics* Cytochrome P-450 Enzyme System / isolation & purification DNA / isolation & purification* Fungal Proteins / genetics Fungal Proteins / isolation & purification Genes Genes, Fungal* Humans Infant, Newborn Molecular Sequence Data Mutation* Oxidoreductases / genetics Saccharomyces cerevisiae / genetics Sterol 14-Demethylase
IF 2.705
Times Cited 67
DNA material Yeast mutant CYP51F1m/pBKS- (RDB16757)