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	THE ROLE OF THR268 IN OXYGEN ACTIVATION OF CYTOCHROME P450(BM-3)
	Yeom, H. ; Sligar, S. G. ; Li, H. Y. ; Poulos, T. L. ; Fulco, A. J. ; Li HY(李海燕)
	1995
关键词	FATTY-ACID MONOOXYGENATION NITRIC-OXIDE SYNTHASE PUTATIVE DISTAL SITE 2 FUNCTIONAL DOMAINS BACILLUS-MEGATERIUM CRYSTAL-STRUCTURE ACTIVE-SITE AMINO-ACID IDENTIFICATION HYDROXYLATION
英文摘要	Cytochrome P450(BM-3), a catalytically self-sufficient monooxygenase from Bacillus megaterium, catalyzes the omega-n (n = 1-3) hydroxylation of fatty acids in the presence of O-2 and NADPH. Like most other P450s, cytochrome P450(BM-3) contains a threonine residue (Thr268) in the distal I helix thought to be important for O-2 binding and activation. Thr268 has been converted to alanine and the enzymatic properties and heme domain crystal structure determined. Using sodium laurate as the substrate, the mutant exhibited slower rates of O-2 and NADPH consumption. In addition, electron transfer is uncoupled from substrate hydroxylation as evidenced by the greater production of water and peroxide in the mutant compared to the wild-type enzyme. The crystal structure of the mutant reveals that the only changes in structure are confined to the site of mutation. These data indicate an important role for Thr268 in O-2 binding and activation in the metabolism of sodium laurate by cytochrome P450(BM-3).
语种	英语
内容类型	期刊论文
源URL	[http://dspace.xmu.edu.cn/handle/2288/62183]
专题	化学化工－已发表论文
推荐引用方式 GB/T 7714	Yeom, H.,Sligar, S. G.,Li, H. Y.,et al. THE ROLE OF THR268 IN OXYGEN ACTIVATION OF CYTOCHROME P450(BM-3)[J],1995.
APA	Yeom, H.,Sligar, S. G.,Li, H. Y.,Poulos, T. L.,Fulco, A. J.,&李海燕.(1995).THE ROLE OF THR268 IN OXYGEN ACTIVATION OF CYTOCHROME P450(BM-3)..
MLA	Yeom, H.,et al."THE ROLE OF THR268 IN OXYGEN ACTIVATION OF CYTOCHROME P450(BM-3)".(1995).

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