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生物物理学. 评论“极端电场在酮固醇异构酶活性部位推动催化反应”。

BIOPHYSICS. Comment on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".

机构信息

Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.

Department of Chemistry and Biochemistry, California State University Long Beach, Long Beach, CA 90840, USA.

出版信息

Science. 2015 Aug 28;349(6251):936. doi: 10.1126/science.aab1584. Epub 2015 Aug 27.

DOI:10.1126/science.aab1584
PMID:26315426
Abstract

Fried et al. (Reports, 19 December 2014, p. 1510) demonstrated a strong correlation between reaction rate and the carbonyl stretching frequency of a product analog bound to ketosteroid isomerase oxyanion hole mutants and concluded that the active-site electric field provides 70% of catalysis. Alternative comparisons suggest a smaller contribution, relative to the corresponding solution reaction, and highlight the importance of atomic-level descriptions.

摘要

弗里德等人(1914 年 12 月 19 日,第 1510 页报道)证明了反应速率与结合到酮甾体异构酶氧阴离子穴突变体的产物类似物的羰基伸缩频率之间存在很强的相关性,并得出结论,活性位点电场提供了 70%的催化作用。其他比较表明,与相应的溶液反应相比,电场的贡献相对较小,这凸显了原子水平描述的重要性。

相似文献

1
BIOPHYSICS. Comment on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".生物物理学. 评论“极端电场在酮固醇异构酶活性部位推动催化反应”。
Science. 2015 Aug 28;349(6251):936. doi: 10.1126/science.aab1584. Epub 2015 Aug 27.
2
BIOPHYSICS. Comment on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".生物物理学。对“极端电场助力酮甾类异构酶活性位点的催化作用”的评论。
Science. 2015 Aug 28;349(6251):936. doi: 10.1126/science.aab0095. Epub 2015 Aug 27.
3
BIOPHYSICS. Response to Comments on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".生物物理学。对《极端电场助力酮甾类异构酶活性位点催化作用》评论的回应
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4
Extreme electric fields power catalysis in the active site of ketosteroid isomerase.极强电场助力酮甾体异构酶活性位点的催化作用。
Science. 2014 Dec 19;346(6216):1510-4. doi: 10.1126/science.1259802.
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A Critical Test of the Electrostatic Contribution to Catalysis with Noncanonical Amino Acids in Ketosteroid Isomerase.非典型氨基酸在酮固醇异构酶中对催化的静电贡献的关键检验。
J Am Chem Soc. 2016 Sep 14;138(36):11890-5. doi: 10.1021/jacs.6b06843. Epub 2016 Sep 1.
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Proton affinity of the oxyanion hole in the active site of ketosteroid isomerase.酮甾体异构酶活性部位中氧阴离子穴的质子亲和力。
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Using unnatural amino acids to probe the energetics of oxyanion hole hydrogen bonds in the ketosteroid isomerase active site.利用非天然氨基酸探究酮甾体异构酶活性位点中氧负离子空穴氢键的能量学。
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Ketosteroid isomerase provides further support for the idea that enzymes work by electrostatic preorganization.酮甾体异构酶为酶通过静电预组织起作用的观点提供了进一步的支持。
Proc Natl Acad Sci U S A. 2010 Mar 2;107(9):4075-80. doi: 10.1073/pnas.0914579107. Epub 2010 Feb 11.
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QM/MM modelling of ketosteroid isomerase reactivity indicates that active site closure is integral to catalysis.QM/MM 建模研究酮甾体异构酶反应性表明活性位点的封闭是催化的必要条件。
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10
Evaluating the catalytic contribution from the oxyanion hole in ketosteroid isomerase.评估酮甾体异构酶中氧阴离子穴的催化贡献。
J Am Chem Soc. 2011 Dec 21;133(50):20052-5. doi: 10.1021/ja208050t. Epub 2011 Nov 22.

引用本文的文献

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A Preorganized Electric Field Leads to Minimal Geometrical Reorientation in the Catalytic Reaction of Ketosteroid Isomerase.预组织电场导致酮甾体异构酶催化反应中最小的几何重排。
J Am Chem Soc. 2020 Jun 3;142(22):9993-9998. doi: 10.1021/jacs.0c00383. Epub 2020 May 19.
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Regulation and Plasticity of Catalysis in Enzymes: Insights from Analysis of Mechanochemical Coupling in Myosin.酶催化的调控与可塑性:来自肌球蛋白机械化学偶联分析的见解
Biochemistry. 2017 Mar 14;56(10):1482-1497. doi: 10.1021/acs.biochem.7b00016. Epub 2017 Mar 1.
3
BIOPHYSICS. Response to Comments on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".
生物物理学。对《极端电场助力酮甾类异构酶活性位点催化作用》评论的回应
Science. 2015 Aug 28;349(6251):936. doi: 10.1126/science.aab1627. Epub 2015 Aug 27.