title: Characterization of diverse natural variants of CYP102A1 found within a species of Bacillus megaterium.
abstract: An extreme diversity of substrates and catalytic reactions of cytochrome P450 (P450) enzymes is considered to be the consequence of evolutionary adaptation driven by different metabolic or environmental demands. Here we report the presence of numerous natural variants of P450 BM3 (CYP102A1) within a species of Bacillus megaterium. Extensive amino acid substitutions (up to 5% of the total 1049 amino acid residues) were identified from the variants. Phylogenetic analyses suggest that this P450 gene evolve more rapidly than the rRNA gene locus. It was found that key catalytic residues in the substrate channel and active site are retained. Although there were no apparent variations in hydroxylation activity towards myristic acid (C14) and palmitic acid (C16), the hydroxylation rates of lauric acid (C12) by the variants varied in the range of >25-fold. Interestingly, catalytic activities of the variants are promiscuous towards non-natural substrates including human P450 substrates. It can be suggested that CYP102A1 variants can acquire new catalytic activities through site-specific mutations distal to the active site.
authors: School of Biological Sciences and Technology, Chonnam National University, Gwangju 500-757, Republic of Korea. chyun@jnu.ac.kr.
authors: Ji-Yeon
authors: JY
authors: Kang
authors: So-Young
authors: SY
authors: Kim
authors: Dooil
authors: D
authors: Kim
authors: Dong-Hyun
authors: DH
authors: Kim
authors: Sun-Mi
authors: SM
authors: Shin
authors: Sun-Ha
authors: SH
authors: Park
authors: Keon-Hee
authors: KH
authors: Kim
authors: Heung-Chae
authors: HC
authors: Jung
authors: Jae-Gu
authors: JG
authors: Pan
authors: Young Hee
authors: YH
authors: Joung
authors: Youn-Tae
authors: YT
authors: Chi
authors: Ho Zoon
authors: HZ
authors: Chae
authors: Taeho
authors: T
authors: Ahn
authors: Chul-Ho
authors: CH
authors: Yun