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). |
个性服务 |
查看访问统计 |
相关权益政策 |
暂无数据 |
收藏/分享 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论