Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase
Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase
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DOI：
10.1016/j.febslet.2010.12.035
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发表时间：
2011-02-04
期刊：
影响因子：
3.5
通讯作者：
Peters, John W.
中科院分区：
文献类型：
--
作者：
Pandey, Arti S.;Mulder, David W.;Peters, John W.
2-酮丙基辅酶M氧化还原酶/羧化酶（2-KPCC）的结构已在观察到CO2的状态下确定，提供了对羧化机制的见解。在酶的底物包封状态下，CO2结合在狭窄的疏水底物进入通道的底部。通道的底部由从疏水环境到亲水环境的过渡界定，其中CO2位于攻击底物的酮丙基的碳负离子的位置，以最终产生乙酰乙酸。这种结合模式有效地区分H2O和防止酮丙基离去基团的质子化。结构总结：2-KPCC结合2-KPCC通过X射线晶体学（查看相互作用）（C）2011欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
The structure of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) has been determined in a state in which CO2 is observed providing insights into the mechanism of carboxylation. In the substrate encapsulated state of the enzyme, CO2 is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO2 is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H2O and prevents protonation of the ketopropyl leaving group.Structured summary:2-KPCC binds to 2-KPCC by x-ray crystallography (View interaction) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.