Title of article :
Characterization of CYP166B1 and its electron transfer system in Streptomyces peucetius var. caesius ATCC 27952
Author/Authors :
Pramod Shrestha، نويسنده , , Tae-Jin Oh، نويسنده , , Narayan Prasad Niraula، نويسنده , , Kwangkyoung Liou، نويسنده , , Jin Cheol Yoo، نويسنده , , Jae Kyung Sohng، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2010
Pages :
6
From page :
372
To page :
377
Abstract :
Although many ferredoxins and ferredoxin reductases have been reported, many details about the homologous electron transfer system of P450s remain unclear. cyp166B1 gene is clustered with the putative ferredoxin (FDX6) in Streptomyces peucetius var. caesius ATCC 27952. Six ferredoxin reductases along with the putative ferredoxin were individually expressed in Escherichia coli and determined the probable primary pathway for dealkylation of 7-ethoxycoumarin as NADH → FDR4 → FDX6 → CYP166B1. Further, mechanistic studies aimed at identifying the endogenous substrate of CYP166B1 would provide a more clear explanation on the homologous electron transfer system.
Keywords :
Cytochrome P450 , Ferredoxin reductase , Electron transfer system , Streptomyces , Ferredoxin
Journal title :
Enzyme and Microbial Technology
Serial Year :
2010
Journal title :
Enzyme and Microbial Technology
Record number :
1185557
Link To Document :
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