Molecular cloning and characterization of the primary structure of the alkane hydroxylating cytochrome P-450 from the yeast Candida maltosa.
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.
Schunck
W H
WH
Central Institute of Molecular Biology, Academy of Sciences of the GDR, Berlin-Buch.
Kärgel
E
E
Gross
B
B
Wiedmann
B
B
Mauersberger
S
S
Köpke
K
K
Kiessling
U
U
Strauss
M
M
Gaestel
M
M
Müller
H G
HG
D000595:Amino Acid Sequence; D001483:Base Sequence; D002175:Candida / Q000201:enzymology / Q000235:genetics*; D003001:Cloning, Molecular; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics*; D004247:DNA / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics; D005810:Multigene Family
D008565:Membrane Proteins; D004247:DNA; D003577:Cytochrome P-450 Enzyme System