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Characterization of Two Self-Sufficient Monooxygenases, CYP102A15 and CYP102A170, as Long-Chain Fatty Acid Hydroxylases

Authors
Rimal, HemrajLee, Woo-HaengKim, Ki-HwaPark, HyunOh, Tae-Jin
Issue Date
May-2020
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Keywords
Bacillus sp.; cytochrome P450; fatty acid hydroxylation; Paenibacillus sp.; self-sufficient monooxygenase
Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.30, no.5, pp.777 - 784
Indexed
SCIE
SCOPUS
KCI
Journal Title
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume
30
Number
5
Start Page
777
End Page
784
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/56169
DOI
10.4014/jmb.1911.11048
ISSN
1017-7825
Abstract
Self-sufficient P450s, due to their fused nature, are the most effective tools for electron transfer to activate C-H bonds. They catalyze the oxygenation of fatty acids at different omega positions. Here, two new, self-sufficient cytochrome P450s, named 'CYP102A15 and CYP102A170,' from polar Bacillus sp. PAMC 25034 and Paenibacillus sp. PAMC 22724, respectively, were cloned and expressed in E. coli. The genes are homologues of CYP102A1 from Bacillus megaterium. They catalyzed the hydroxylation of both saturated and unsaturated fatty acids ranging in length from C-12-C-20, with a moderately diverse profile compared to other members of the CYP102A subfamily. CYP102A15 exhibited the highest activity toward linoleic acid with K-m 15.3 mu M, and CYP102A170 showed higher activity toward myristic acid with K-m 17.4 mu M. CYP10A170 also hydroxylated the Eicosapentaenoic acid at omega-1 position only. Various kinetic parameters of both monooxygenases were also determined.
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