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	Probing the role of the hyper-reactive histidine residue of arginase
	Colleluori, D. M. ; Reczkowski, R. S. ; Emig, F. A. ; Cama, E. ; Cox, J. D. ; Scolnick, L. R. ; Compher, K. ; Jude, K. ; Han, S. F. ; Viola, R. E. ; Christianson, D. W. ; Ash, D. E. ; Han SF(韩守法)
	2005
关键词	arginase chemical modification chemical modulation mutagenesis diethyl pyrocarbonate bimetallic hydrolases
英文摘要	Rat liver arginase (arginase 1) is potently inactivated by diethyl pyrocarbonate, with a second-order rate constant of 113 M(-1)s(-1) for the inactivation process at pit 7.0, 25 degrees C. Partial protection front inactivation is provided by the product of the reaction, L-ornithine, while nearly complete protection is afforded by the inhibitor pair, t-ornithine and borate. The role of H141 has been probed by mutagenesis, chemical modulation, and X-ray diffraction. The hyper-reactivity of H141 towards diethyl pyrocarbonate can be explained by its proximity to E277. A proton shuttling role for H141 is Supported by its conformational mobility observed among the known arginase structures. H141 is proposed to serve as an acid/base catalyst, deprotonating the metal-bridging water molecule to generate the metal-bridging hydroxide nucleophile, and by protonating the amino group of the product to facilitate its departure. (c) 2005 Elsevier Inc. All rights reserved.
语种	英语
内容类型	期刊论文
源URL	[http://dspace.xmu.edu.cn/handle/2288/64293]
专题	化学化工－已发表论文
推荐引用方式 GB/T 7714	Colleluori, D. M.,Reczkowski, R. S.,Emig, F. A.,et al. Probing the role of the hyper-reactive histidine residue of arginase[J],2005.
APA	Colleluori, D. M..,Reczkowski, R. S..,Emig, F. A..,Cama, E..,Cox, J. D..,...&韩守法.(2005).Probing the role of the hyper-reactive histidine residue of arginase..
MLA	Colleluori, D. M.,et al."Probing the role of the hyper-reactive histidine residue of arginase".(2005).

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