Purification and characterization of cytochrome P450 from an isobutene-forming microorganism, Rhodotorula minuta.
A cytochrome P450 was purified from microsomes of Rhodotorula minuta. The optical spectrum of the purified cytochrome was characteristic of a low-spin ferric heme protein. Isovalerate caused a type I spectral change in it. The amino-terminal sequence of the cytochrome was different from those of other known microsomal cytochrome P450s. These results indicate that the cytochrome, which is tentatively named P450rm, is a novel species of cytochrome P450.
Fukuda
H
H
Department of Applied Microbial Technology, Kumamoto Institute of Technology, Japan.
Fujii
T
T
Daimon
H
H
Iwata
M
M
Ogawa
T
T
Tanase
S
S
Morino
Y
Y
D000475:Alkenes / Q000378:metabolism; D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D012248:Rhodotorula / Q000201:enzymology*; D013057:Spectrum Analysis
D000475:Alkenes; D003577:Cytochrome P-450 Enzyme System; C008176:isobutylene