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

Tiklamalar: 241
ID: 109640
2019
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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 sp. PAMC 25034 and sp. PAMC 22724, respectively, were cloned and expressed in . The genes are homologues of CYP102A1 from . They catalyzed the hydroxylation of both saturated and unsaturated fatty acids ranging in length from C-C, with a moderately diverse profile compared to other members of the CYP102A subfamily. CYP102A15 exhibited the highest activity toward linoleic acid with K 15.3 μM, and CYP102A170 showed higher activity toward myristic acid with Km 17.4 μM. CYP10A170 also hydroxylated the Eicosapentaenoic acid at ω-1 position only. Various kinetic parameters of both monooxygenases were also determined.
Referans Anahtari
rimal2019characterizationjournal Kullanarak makale yazarken otomatik alinti icin bu anahtari kullanin SciMatic Makale Yoneticisi veya Tez Yoneticisi
Yazarlar Rimal, Hemraj;Lee, Woo-Haeng;Kim, Ki-Hwa;Park, Hyun;Oh, Tae-Jin;
Dergi Journal of microbiology and biotechnology
Yil 2019
DOI
10.4014/jmb.1911.11048
URL
Anahtar Kelimeler
cytochrome p450 bacillus sp. paenibacillus sp. fatty acid hydroxylation self-sufficient monooxygenase

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