| Literature DB >> 24768738 |
Dong Liu1, Xiaojie Zhou2, Mei Li3, Shunyi Zhu3, Xinghui Qiu4.
Abstract
A complete cDNA encoding the NADPH-cytochrome P450 reductase (haCPR) and its genomic sequence from the cotton bollworm Helicoverpa armigera were cloned and sequenced. The open reading frame of haCPR codes for a protein of 687 amino acid residues with a calculated molecular mass of 77.4kDa. The haCPR gene spans over 11 kb and its coding region is interrupted by 11 introns. haCPR is ubiquitously expressed in various tissues and at various stages of development. Escherichia coli produced haCPR enzyme exhibited catalytic activity for NADPH-dependent reduction of cytochrome c, following Michaelis-Menten kinetics. The functionality of CPR was further demonstrated by its capacity to support cytochrome P450 (e.g. haCYP9A14 and chicken CYP1A5) mediated O-dealkylation activity of alkoxyresorufins. The flavoprotein-specific inhibitor (diphenyleneiodonium chloride, DPI) showed a potent inhibition to haCPR activity (IC50=1.69 μM). Inhibitory effect of secondary metabolites in the host plants (tannic acid, quercetin and gossypol) on CPR activity (with an IC50 value ranged from 15 to 90 μM) was also observed.Entities:
Keywords: Enzymatic kinetics; Gene structure; Helicoverpa armigera; Inhibition; NADPH–cytochrome P-450 reductase; Spatial and temporal expression
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Year: 2014 PMID： 24768738 DOI： 10.1016/j.gene.2014.04.054
Source DB: PubMed Journal: Gene ISSN： 0378-1119 Impact factor: 3.688