Molecular cloning and characterization of the primary structure of the alkane hydroxylating cytochrome P-450 from the yeast Candida maltosa

Biochem Biophys Res Commun. 1989 Jun 15;161(2):843-50. doi: 10.1016/0006-291x(89)92677-6.

Abstract

A cDNA library was established starting from poly(A) RNA of n-alkane-grown Candida maltosa cells and cDNA clones were isolated containing the entire coding sequence for the alkane hydroxylating cytochrome P-450. The deduced protein consists of 521 amino acids, contains two putative transmembrane segments in the N-terminal region and has a characteristic heme-binding sequence in the C-terminal part. Sequence alignments with members of 11 reported cytochrome P-450 families revealed a strong homology to an alkane-inducible cytochrome P-450 from Candida tropicalis.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Candida / enzymology
  • Candida / genetics*
  • Cloning, Molecular
  • Cytochrome P-450 Enzyme System / genetics*
  • DNA / genetics
  • Membrane Proteins / genetics
  • Multigene Family

Substances

  • Membrane Proteins
  • DNA
  • Cytochrome P-450 Enzyme System

Associated data

  • GENBANK/M27081