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Purification of cytochrome p 450 alk from n alkane grown cells of candida maltosa and cloning and nucleotide sequencing of the encoding gene


Purification of cytochrome p 450 alk from n alkane grown cells of candida maltosa and cloning and nucleotide sequencing of the encoding gene



Agricultural and Biological Chemistry 53(8): 2217-2226



ISSN/ISBN: 0002-1369

DOI: 10.1271/bbb1961.53.2217

When the cells of an n-alkane-assimilating yeast, Candida maltosa IAM12247, were transferred from a glucose medium to an n-alkane medium, various enzymes are induced in the endoplasmic reticulum and peroxisome. Cytochrome P-450alk, one of these enzymes in the endoplasmic reticulum, was purified after mild solubilization of the membrane, followed by a few steps of chromatography. The enzyme was characterized spectrophotometrically and its N-terminal amino acid sequence (12 residues) was determined. Using oligonucleotide probes prepared to match parts of the N-terminal amino acid sequence and of the partial cDNA sequence of cytochrome P-450alk of C. maltosa EH15, we isolated from a gene library of C. maltosa IAM12247 a clone which had a gene encoding cytochrome P-450alk. By nucleotide sequencing of this gene, the amino acid sequence of this enzyme was deduced. It consisted of 523 amino acids (59,838 daltons), with a non-cleavable signal sequence in the N-terminal region. The structure of this enzyme was compared with some other membranes of the cytochrome P-450 superfamily.

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Accession: 007709869

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