pH dependence of the nitrotyrosine-248 and arsanilazotyrosine-248 carboxypeptidase A catalyzed hydrolysis of O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate.

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作者信息

Suh J, Kaiser E T

出版信息

J Am Chem Soc. 1976 Mar 31;98(7):1940-7. doi: 10.1021/ja00423a048.

DOI:10.1021/ja00423a048

PMID:3540

Abstract

摘要

相似文献

pH dependence of the nitrotyrosine-248 and arsanilazotyrosine-248 carboxypeptidase A catalyzed hydrolysis of O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate.

J Am Chem Soc. 1976 Mar 31;98(7):1940-7. doi: 10.1021/ja00423a048.

pPH dependence and competitive product inhibition of the carboxypeptidase A catalyzed hydrolysis of O-(trans-cinnamoyl)-L-beta-phenyllactate.羧肽酶A催化O-(反式肉桂酰基)-L-β-苯基乳酸水解的pH依赖性及竞争性产物抑制作用

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Spectral titration of active site of carboxypeptidase A.

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Direct chemical evidence for the mixed anhydride intermediate of carboxypeptidase A in ester and peptide hydrolysis.羧肽酶A在酯和肽水解中混合酸酐中间体的直接化学证据。

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Multiple inhibitor binding to arsanilazotyrosine-248 carboxypeptidase A.

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Effects of pH on the structure and function of carboxypeptidase A: crystallographic studies.pH对羧肽酶A结构和功能的影响：晶体学研究

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Mechanism of action of carboxypeptidase A in ester hydrolysis.羧肽酶A在酯水解中的作用机制。

Proc Natl Acad Sci U S A. 1976 Nov;73(11):3882-6. doi: 10.1073/pnas.73.11.3882.

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