CYP102A1 Protein, Priestia megaterium (P. pastoris, His)

The CYP102A1 protein acts as a fatty acid monooxygenase, catalyzing the hydroxylation of fatty acids at various positions. The protein also exhibits NADPH-dependent reductase activity, promoting electron transfer within its domain. CYP102A1 Protein, Priestia megaterium (P. pastoris, His) is the recombinant CYP102A1 protein, expressed by P. pastoris , with C-6*His labeled tag. The total length of CYP102A1 Protein, Priestia megaterium (P. pastoris, His) is 471 a.a., with molecular weight of 55.2 kDa.

CYP102A1, known as a fatty acid monooxygenase, exhibits versatile enzymatic activities contributing to its role in diverse metabolic processes. This protein catalyzes the hydroxylation of fatty acids at various omega positions, including omega-1, omega-2, and omega-3, with a particular preference for medium and long-chain fatty acids such as lauric, myristic, and palmitic acids. Additionally, CYP102A1 can metabolize some primary fatty acid metabolites into secondary and tertiary products. Notably, it displays a marginal activity towards short-chain fatty acids. Its ability to hydroxylate highly branched fatty acids is crucial for regulating membrane fluidity. Beyond its monooxygenase function, CYP102A1 demonstrates a NADPH-dependent reductase activity in the C-terminal domain, facilitating electron transfer to the heme iron of the cytochrome P450 N-terminal domain. An intriguing aspect of its functionality involves the inactivation of quorum sensing signals produced by competing bacteria. CYP102A1 efficiently oxidizes acyl homoserine lactones (AHLs), key molecules in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs), thus contributing to the modulation of bacterial communication.

Others

P. pastoris

C-6*His

P14779 (T2-R472)

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TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGIPSPSTEQSAKKVR

55.2 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.