Characterization of a novel cytochrome P450 from Amycolatopsis sp. CGMCC1149 for hydroxylation of lovastatin. (7th July 2014)

• Record Type: Journal Article
• Authors: Zong, Hong; Zhuge, Bin; Lu, Xinyao; Huo, Xiaoyu; Fang, Huiying; Song, Jian; Sun, Jin
• Is Part Of: Biotechnology and applied biochemistry. Volume 62:Number 1(2015:Jan./Feb.)
• Page Start: 9
• Page End: 16
• Publication Date: 2014-07-07
• Subjects: Biotechnology -- Periodicals; Biochemical engineering -- Periodicals; Biochemistry -- Periodicals; Biochemistry -- Periodicals; Genetic Techniques -- Periodicals; Microbiological Techniques -- Periodicals; 660.6
• DOI: 10.1002/bab.1247
• Languages: English
• ISSNs: 0885-4513

Abstract

<abstract abstract-type="main"> <title>Abstract</title> <p>Wuxistatin, a novel and potent statin, is converted from lovastatin by <italic>Amycolatopsis</italic> sp. CGMCC1149. In the bioconversion, lovastatin is firstly hydroxylated to 3‐hydroxymethyl lovastatin (product I) by a hydroxylase. In the current study, a novel hydroxylase gene <italic>p450lov</italic> was isolated from <italic>Amycolatopsis</italic> sp. CGMCC1149 by degenerate PCR and self‐formed adaptor PCR and expressed in <italic>Escherichia coli</italic>. The gene encodes a 403‐amino‐acid protein with a molecular weight of 44.8 kDa and was designated as a new member of cytochrome P450 (CYP) 105 family, CYP105A44. Meanwhile, a lovastatin catalytic <italic>in vitro</italic> system was established, and an optimal hydroxylation reaction system contained 30 µM lovastatin, 600 µM NADH, 120 µM ferredoxin, 0.04 U ferredoxin−nicotinamide adenine dinucleotide phosphate reductase, and 100 µM CYP105A44 in a final volume of 200 µL Tris HCl buffer (50 mM, pH 7.4). These would be helpful for further studies on the hydroxylation of statins.</p> </abstract>