Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 98, Issue 11, Pages 5009-5017Publisher
SPRINGER
DOI: 10.1007/s00253-014-5525-x
Keywords
Cytochrome P450; Redox partner; mRNA expression profile; Streptomyces avermitilis MA4680
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Funding
- WCU (World Class University) program through the National Research Foundation of Korea (NRF) - Ministry of Education, Science and Technology [R322012000102130]
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It was previously proposed that regiospecific hydroxylation of daidzein at 3'-position is mediated by cytochrome P450 hydroxylase (CYP105D7) in the presence of putidaredoxin (CamB) and putidaredoxin reductase (CamA) as electron transfer proteins from Pseudomonas putida. The genome sequence of Streptomyces avermitilis MA4680 revealed 33 P450 (CYPs) with 6 ferredoxin reductases (Fprs) and 9 ferredoxins (Fdxs) as their putative electron transfer partner proteins. To identify right endogenous electron transfer proteins for CYP105D7 activity, in vitro reconstitution, gene disruption, and quantitative reverse transcription polymerase chain reaction (qRT-PCR) mRNA expression profile analysis were examined. The most effective electron transfer proteins for CYP105D7 appear to be FdxH (SAV7470), which is located downstream to CYP105D7 as a cluster, and FprD (SAV5675). Throughout our overall analysis, we proposed that the primary electron transfer pathway for CYP105D7 follows as such NAD(P)H -> FdxH -> FprD -> CYP105D7.
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