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单体酶效率的决定因素：位点特异性分子对胰蛋白酶的加速作用

Determinant of efficiency of a monomeric enzyme: acceleration by site-specific molecules for trypsin.

作者信息

Tanizawa K, Kanaoka Y

出版信息

Experientia. 1979 Jan 15;35(1):16-7. doi: 10.1007/BF01917847.

DOI:10.1007/BF01917847
PMID:421784
Abstract

The interaction of a specific ligand at substrate binding site was shown to be responsible for the catalytic efficiency of trypsin. The reasoning of 'induced fit' theory was refined by kinetic analysis of characteristic properties of 'inverse' substrates.

摘要

已表明特定配体在底物结合位点的相互作用是胰蛋白酶催化效率的原因。通过对“反向”底物特征性质的动力学分析，完善了“诱导契合”理论的推理。

相似文献

1
Determinant of efficiency of a monomeric enzyme: acceleration by site-specific molecules for trypsin.单体酶效率的决定因素：位点特异性分子对胰蛋白酶的加速作用
Experientia. 1979 Jan 15;35(1):16-7. doi: 10.1007/BF01917847.
2
Oxygen and sulfur esters of "inverse substrates": different responses of amidinophenol and amidinothiophenol in the activation of the rate of tryptic hydrolysis of the inverse esters.“反向底物”的氧酯和硫酯：脒基苯酚和脒基硫酚在反向酯胰蛋白酶水解速率激活中的不同反应
J Biochem. 1985 Jan;97(1):275-80. doi: 10.1093/oxfordjournals.jbchem.a135051.
3
Comparative studies on the structure of active sites. Behavior of "inverse substrates" toward trypsin and related enzymes.活性位点结构的比较研究。“反向底物”对胰蛋白酶及相关酶的作用。
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The kinetics of hydrolysis of some extended N-aminoacyl-l-lysine methyl esters.一些扩展的N-氨基酰基-L-赖氨酸甲酯的水解动力学
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Understanding binding selectivity toward trypsin and factor Xa: the role of aromatic interactions.理解对胰蛋白酶和凝血因子Xa的结合选择性：芳香族相互作用的作用。
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Crystal structure reveals basis for the inhibitor resistance of human brain trypsin.晶体结构揭示了人脑胰蛋白酶抑制剂抗性的基础。
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Enzyme substrate and inhibitor interactions.酶底物与抑制剂的相互作用。
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"Inverse substrates" for trypsin-like enzymes.
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Enantiomeric specificity at the deacylation process of tryptic catalysis.胰蛋白酶催化脱酰基过程中的对映体特异性。
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本文引用的文献

1
Application of a Theory of Enzyme Specificity to Protein Synthesis.酶特异性理论在蛋白质合成中的应用。
Proc Natl Acad Sci U S A. 1958 Feb;44(2):98-104. doi: 10.1073/pnas.44.2.98.
2
ON THE ACTIVATION OF TRYPSIN BY AMINES.
Biochim Biophys Acta. 1964 Jun 1;85:507-9. doi: 10.1016/0926-6569(64)90320-7.
3
THE MECHANISM OF THE SPECIFICITY OF TRYPSIN CATALYSIS. 3. ACTIVATION OF THE CATALYTIC SITE OF TRYPSIN BY ALKYLAMMONIUM IONS IN THE HYDROLYSIS OF ACETYLGLYCINE ETHYL ESTER.胰蛋白酶催化特异性的机制。3. 乙酰甘氨酸乙酯水解中烷基铵离子对胰蛋白酶催化位点的激活作用。
J Biol Chem. 1964 May;239:1395-401.
4
Trypsin substrates derived from benzamidine: application to active site titration and isolation of acyl-enzyme intermediate.源自苯甲脒的胰蛋白酶底物：在活性位点滴定和酰基酶中间体分离中的应用
Biochem Biophys Res Commun. 1968 Sep 6;32(5):893-7. doi: 10.1016/0006-291x(68)90325-2.
5
The interaction of trypsin with neutral substrates and modifiers.胰蛋白酶与中性底物及调节剂的相互作用。
Biochemistry. 1968 Oct;7(10):3616-24. doi: 10.1021/bi00850a039.
6
Proteolytic enzymes. VI. Aromatic amidines as competitive inhibitors of trypsin.
J Biochem. 1971 May;69(5):893-9. doi: 10.1093/oxfordjournals.jbchem.a129540.
7
On the specificity of tryptic catalysis.关于胰蛋白酶催化作用的特异性
Biochem Biophys Res Commun. 1971 Aug 6;44(3):745-51. doi: 10.1016/s0006-291x(71)80146-8.
8
Amines as modifiers of the tryptic hydrolysis of neutral substrates.胺类作为中性底物胰蛋白酶水解的修饰剂。
Biochemistry. 1971 Jun 8;10(12):2284-90. doi: 10.1021/bi00788a016.
9
"Inverse substrates" for trypsin. Efficient enzymatic hydrolysis of certain esters with a cationic center in the leaving group1.
J Am Chem Soc. 1977 Jun 22;99(13):4485-8. doi: 10.1021/ja00455a046.