A single amino acid substitution converts cytochrome P450(14DM) to an inactive form, cytochrome P450SG1: complete primary structures deduced from cloned DNAS

Biochem Biophys Res Commun. 1988 Aug 30;155(1):317-23. doi: 10.1016/s0006-291x(88)81087-8.


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.

MeSH terms

  • 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


  • CYP51A1 protein, human
  • Fungal Proteins
  • DNA
  • Cytochrome P-450 Enzyme System
  • Oxidoreductases
  • Sterol 14-Demethylase

Associated data

  • GENBANK/M21483
  • GENBANK/M21484