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A kinetic study of hydrophobic interactions at the S1 and S2 sites of papain.

作者信息

Brubacher L J, Zaher M R

出版信息

Can J Biochem. 1979 Aug;57(8):1064-72. doi: 10.1139/o79-135.

DOI:10.1139/o79-135
PMID:44219
Abstract
摘要

相似文献

1
A kinetic study of hydrophobic interactions at the S1 and S2 sites of papain.木瓜蛋白酶S1和S2位点疏水相互作用的动力学研究。
Can J Biochem. 1979 Aug;57(8):1064-72. doi: 10.1139/o79-135.
2
Dependence of the P2-S2 stereochemical selectivity of papain on the nature of the catalytic-site chemistry. Quantification of selectivity in the catalysed hydrolysis of the enantiomeric N-acetylphenylalanylglycine 4-nitroanilides.木瓜蛋白酶的P2-S2立体化学选择性对催化位点化学性质的依赖性。对映体N-乙酰苯丙氨酰甘氨酸4-硝基苯胺催化水解中选择性的定量分析。
Biochem J. 1990 Mar 15;266(3):653-60. doi: 10.1042/bj2660653.
3
Identification of signalling and non-signalling binding contributions to enzyme reactivity. Alternative combinations of binding interactions provide for change in transition-state geometry in reactions of papain.确定信号和非信号结合对酶反应性的贡献。结合相互作用的不同组合导致木瓜蛋白酶反应中过渡态几何结构的变化。
Biochem J. 1989 Mar 15;258(3):755-64. doi: 10.1042/bj2580755.
4
A re-appraisal of the structural basis of stereochemical recognition in papain. Insensitivity of binding-site-catalytic-site signalling to P2-chirality in a time-dependent inhibition.木瓜蛋白酶中立体化学识别结构基础的重新评估。在时间依赖性抑制中,结合位点 - 催化位点信号对P2手性不敏感。
Biochem J. 1990 Mar 15;266(3):645-51. doi: 10.1042/bj2660645.
5
Comparison of the kinetics of the papain-catalyzed hydrolysis of glycine- and alanine-based esters and thiono esters.木瓜蛋白酶催化甘氨酸和丙氨酸基酯及硫代酯水解动力学的比较。
Biochemistry. 1988 Jan 12;27(1):264-8. doi: 10.1021/bi00401a040.
6
Consequences of molecular recognition in the S1-S2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P1-P2 amide bond into a two-protonic-state reactivity probe.木瓜蛋白酶S1 - S2亚位点间区域分子识别对催化位点化学的影响。通过将P1 - P2酰胺键引入双质子态反应性探针,pH依赖性特征的变化及反向溶剂动力学同位素效应的产生。
Biochem J. 1988 Mar 15;250(3):761-72. doi: 10.1042/bj2500761.
7
Hydrolysis of alkyl ester and amide substrates by papain.木瓜蛋白酶对烷基酯和酰胺底物的水解作用。
Acta Biochim Biophys Acad Sci Hung. 1977;12(4):329-33.
8
The specificity of the S1' subsite of papain.木瓜蛋白酶S1'亚位点的特异性。
Biochem J. 1974 Aug;141(2):495-501. doi: 10.1042/bj1410495.
9
PAPAIN-CATALYSED HYDROLYSIS OF SOME HIPPURIC ESTERS. A NEW MECHANISM FOR PAPAIN-CATALYSED HYDROLYSIS.木瓜蛋白酶催化某些马尿酸酯的水解。木瓜蛋白酶催化水解的新机制。
Biochem J. 1965 Jul;96(1):199-204. doi: 10.1042/bj0960199.
10
Differences in the chemical and catalytic characteristics of two crystallographically 'identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment.两个晶体学上“相同”的酶催化位点在化学和催化特性上的差异。通过结合pH依赖性底物催化动力学以及针对催化位点硫醇基团及其紧邻微环境的反应性探针研究,对猕猴桃蛋白酶和木瓜蛋白酶进行表征。
Biochem J. 1987 Oct 1;247(1):181-93. doi: 10.1042/bj2470181.

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1
New Glutamine-Containing Substrates for the Assay of Cysteine Peptidases From the C1 Papain Family.用于检测C1木瓜蛋白酶家族半胱氨酸肽酶的新型含谷氨酰胺底物
Front Mol Biosci. 2020 Oct 22;7:578758. doi: 10.3389/fmolb.2020.578758. eCollection 2020.