How an enzyme surmounts the activation energy barrier.
作者信息
Schowen Richard L
机构信息
Higuchi Biosciences Center, Simons Laboratories, 2095 Constant Avenue, University of Kansas, Lawrence, KS 66047, USA.
出版信息
Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):11931-2. doi: 10.1073/pnas.2235806100. Epub 2003 Oct 6.
Abstract
摘要
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How an enzyme surmounts the activation energy barrier.酶如何克服活化能障碍。
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Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis.静电过渡态稳定而非反应物去稳定化提供了高效分支酸变位酶催化的化学基础。
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本文引用的文献
1
The near attack conformation approach to the study of the chorismate to prephenate reaction.用于研究分支酸向预苯酸反应的近攻击构象方法。
Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):12015-20. doi: 10.1073/pnas.1534873100. Epub 2003 Oct 1.
2
Apparent NAC effect in chorismate mutase reflects electrostatic transition state stabilization.在分支酸变位酶中明显的NAC效应反映了静电过渡态稳定化。
J Am Chem Soc. 2003 Aug 27;125(34):10228-37. doi: 10.1021/ja0356481.
3
Understanding the role of active-site residues in chorismate mutase catalysis from molecular-dynamics simulations.通过分子动力学模拟理解活性位点残基在分支酸变位酶催化中的作用。
Angew Chem Int Ed Engl. 2003 Apr 4;42(13):1508-11. doi: 10.1002/anie.200219878.
4
Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor.通过带正电荷的氢键供体对分支酸变位酶过渡态的选择性稳定作用。
J Am Chem Soc. 2003 Mar 19;125(11):3206-7. doi: 10.1021/ja0341992.
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Biopolymers. 2003 Mar;68(3):350-8. doi: 10.1002/bip.10266.
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Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics.环境耦合氢隧穿。将催化与动力学联系起来。
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