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Facilitated proton transfer in enzyme catalysis. It may have a crucial role in determining the efficiency and specificity of enzymes.

作者信息

Wang J H

出版信息

Science. 1968 Jul 26;161(3839):328-34. doi: 10.1126/science.161.3839.328.

DOI:10.1126/science.161.3839.328
PMID:4298414
Abstract
摘要

相似文献

1
Facilitated proton transfer in enzyme catalysis. It may have a crucial role in determining the efficiency and specificity of enzymes.酶催化中的质子传递促进作用。它可能在决定酶的效率和特异性方面发挥关键作用。
Science. 1968 Jul 26;161(3839):328-34. doi: 10.1126/science.161.3839.328.
2
Directional character of proton transfer in enzyme catalysis.酶催化中质子转移的方向性特征。
Proc Natl Acad Sci U S A. 1970 Jul;66(3):874-81. doi: 10.1073/pnas.66.3.874.
3
Proton transfer to residues of basic pK(a) during catalysis by carbonic anhydrase.碳酸酐酶催化过程中质子向具有碱性pK(a)的残基转移。
Biochim Biophys Acta. 1999 Sep 14;1434(1):1-5. doi: 10.1016/s0167-4838(99)00170-3.
4
Intramolecular proton transfer from multiple sites in catalysis by murine carbonic anhydrase V.小鼠碳酸酐酶V催化过程中多个位点的分子内质子转移。
Biochemistry. 1998 May 19;37(20):7649-55. doi: 10.1021/bi9729209.
5
Microenvironmental effects on enzyme catalysis. A kinetic study of polyanionic and polycationic derivatives of chymotrypsin.微环境对酶催化的影响。胰凝乳蛋白酶的聚阴离子和聚阳离子衍生物的动力学研究。
Biochemistry. 1972 Oct 24;11(22):4072-84. doi: 10.1021/bi00772a009.
6
Carbon dioxide hydration activity of carbonic anhydrase: paradoxical consequences of the unusually rapid catalysis.碳酸酐酶的二氧化碳水合活性:异常快速催化的矛盾后果。
Proc Natl Acad Sci U S A. 1973 Jul;70(7):1986-9. doi: 10.1073/pnas.70.7.1986.
7
Participation of an acidic group in the chymotrypsin catalysis.一个酸性基团在胰凝乳蛋白酶催化过程中的参与。
J Biochem. 1969 May;65(5):809-19. doi: 10.1093/oxfordjournals.jbchem.a129081.
8
Preparation and properties of carrier-bound enzymes.载体结合酶的制备及其性质
Eur J Biochem. 1972 Jan 31;25(1):129-35. doi: 10.1111/j.1432-1033.1972.tb01676.x.
9
Marcus rate theory applied to enzymatic proton transfer.应用于酶促质子转移的马库斯速率理论。
Biochim Biophys Acta. 2000 May 12;1458(1):88-103. doi: 10.1016/s0005-2728(00)00061-x.
10
Transients and relaxation kinetics of enzyme reactions.酶反应的瞬态和弛豫动力学
Annu Rev Biochem. 1971;40:315-44. doi: 10.1146/annurev.bi.40.070171.001531.

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Mechanism-Based Inactivation of Ribonuclease A.基于机制的核糖核酸酶A失活
J Org Chem. 1995 Oct;60(21):6930-6936. doi: 10.1021/jo00126a051.
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A model for the mechanism of chloride activation of oxygen evolution in photosystem II.光合作用系统 II 中氯激活氧气产生的机制模型。
Photosynth Res. 1987 Sep;13(3):199-223. doi: 10.1007/BF00029400.
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Ribonuclease a: revealing structure-function relationships with semisynthesis.核糖核酸酶A:通过半合成揭示结构-功能关系
J Am Chem Soc. 1995 Aug;117(31):8057-60. doi: 10.1021/ja00136a001.
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Pentavalent Organo-Vanadates as Transition State Analogues for Phosphoryl Transfer Reactions.五价有机钒酸盐作为磷酰基转移反应的过渡态类似物
J Am Chem Soc. 2000 Oct 18;122(41):9911-9916. doi: 10.1021/ja0021058.
6
The correlation of RNase A enzymatic activity with the changes in the distance between Nepsilon2-His12 and N delta1-His119 upon addition of stabilizing and destabilizing salts.添加稳定盐和去稳定盐后,核糖核酸酶A的酶活性与Nε2-组氨酸12和Nδ1-组氨酸119之间距离变化的相关性。
Protein J. 2006 Feb;25(2):117-25. doi: 10.1007/s10930-006-0003-7.
7
Influence of Leaving-Group Electronic Effect on alpha-Chymotrypsin: Catalytic Constants of Specific Substrates.离去基团电子效应对α-胰凝乳蛋白酶的影响:特定底物的催化常数
Proc Natl Acad Sci U S A. 1973 Feb;70(2):517-20. doi: 10.1073/pnas.70.2.517.
8
Active Site of alpha-Chymotrypsin Activation by Association-Desolvation.通过缔合去溶剂化激活α-糜蛋白酶的活性位点
Proc Natl Acad Sci U S A. 1970 Jun;66(2):249-56. doi: 10.1073/pnas.66.2.249.
9
The nature of general base-general acid catalysis in serine proteases.
Proc Natl Acad Sci U S A. 1969 Dec;64(4):1335-42. doi: 10.1073/pnas.64.4.1335.
10
The mechanism of action of ribonuclease.核糖核酸酶的作用机制。
Proc Natl Acad Sci U S A. 1969 Apr;62(4):1151-8. doi: 10.1073/pnas.62.4.1151.