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1
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
Proc Natl Acad Sci U S A. 1984 Dec;81(24):7767-71. doi: 10.1073/pnas.81.24.7767.
2
Environment and conformation dependent sensitivity of the arsanilazotyrosine-248 carboxypeptidase A chromophore.对氨基苯胂酸酪氨酸-248羧肽酶A发色团的环境和构象依赖性敏感性。
Biochemistry. 1975 Feb 25;14(4):649-60. doi: 10.1021/bi00675a001.
3
Enzymatic activities of carobxypeptidase A's in solution and in crystals.角豆羧肽酶A在溶液和晶体中的酶活性。
Proc Natl Acad Sci U S A. 1973 Dec;70(12):3797-801. doi: 10.1073/pnas.70.12.3797.
4
Similarities between the conformation of arsanilazotyrosine 248 of carboxypeptidase A in the crystalline state and in solution.结晶态和溶液态的羧肽酶A中对氨基苯砷酸酪氨酸248的构象之间的相似性。
Proc Natl Acad Sci U S A. 1972 Oct;69(10):2850-4. doi: 10.1073/pnas.69.10.2850.
5
Crystallographic studies on apocarboxypeptidase A and the complex with glycyl-L-tyrosine.脱辅基羧肽酶A及其与甘氨酰-L-酪氨酸复合物的晶体学研究。
Proc Natl Acad Sci U S A. 1983 Dec;80(23):7151-4. doi: 10.1073/pnas.80.23.7151.
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Three high-resolution crystal structures of cadmium-substituted carboxypeptidase A provide insight into the enzymatic function.镉取代的羧肽酶A的三种高分辨率晶体结构为酶的功能提供了深入见解。
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Structure and dynamics of the metal site of cadmium-substituted carboxypeptidase A in solution and crystalline states and under steady-state peptide hydrolysis.镉取代羧肽酶A的金属位点在溶液态、晶态及稳态肽水解条件下的结构与动力学
Biochemistry. 1997 Sep 23;36(38):11514-24. doi: 10.1021/bi970936t.
8
Crystal structure of the complex of carboxypeptidase A with a strongly bound phosphonate in a new crystalline form: comparison with structures of other complexes.羧肽酶A与一种紧密结合的膦酸盐以新晶型形成的复合物的晶体结构：与其他复合物结构的比较。
Biochemistry. 1990 Jun 12;29(23):5546-55. doi: 10.1021/bi00475a019.
9
Conformations of arsanilazotyrosine-248 carboxypeptidase A alpha, beta, gamma, comparison of crystals and solution.对氨基苯胂酸酪氨酸-248羧肽酶Aα、β、γ的构象：晶体与溶液的比较
Proc Natl Acad Sci U S A. 1973 Jul;70(7):2006-10. doi: 10.1073/pnas.70.7.2006.
10
Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248.处于新晶体环境中的天然羧肽酶A显示出重要的酪氨酸248的不同构象。
Biochemistry. 1998 Nov 24;37(47):16555-64. doi: 10.1021/bi981678i.

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1
Mutational analysis of aspartoacylase: implications for Canavan disease.天冬氨酸酰基转移酶的突变分析：对卡纳万病的意义。
Brain Res. 2007 May 7;1148:1-14. doi: 10.1016/j.brainres.2007.02.069. Epub 2007 Mar 3.
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Carboxylate binding modes in zinc proteins: a theoretical study.锌蛋白中的羧酸盐结合模式：理论研究。
Biophys J. 1999 Nov;77(5):2777-87. doi: 10.1016/S0006-3495(99)77110-9.
3
Complex between carboxypeptidase A and a hydrated ketomethylene substrate analogue.羧肽酶A与水合酮亚甲基底物类似物之间的复合物。
Proc Natl Acad Sci U S A. 1988 Feb;85(3):684-8. doi: 10.1073/pnas.85.3.684.

本文引用的文献

1
Metallocarboxypeptidases: stability constants and enzymatic characteristics.金属羧肽酶：稳定常数与酶学特性
J Biol Chem. 1961 Aug;236:2244-9.
2
On the interpretation of the pH variation of the maximum initial velocity of an enzyme-catalyzed reaction.关于酶催化反应最大初始速度的pH变化的解释
Biochim Biophys Acta. 1954 Mar;13(3):347-53. doi: 10.1016/0006-3002(54)90340-6.
3
The effect of pH on the affinities of enzymes for substrates and inhibitors.pH 对酶与底物及抑制剂亲和力的影响。
Biochem J. 1953 Aug;55(1):161-70. doi: 10.1042/bj0550161.
4
The pH dependence of peptide hydrolysis by nitrocarboxypeptidase A.硝基羧肽酶A催化肽水解的pH依赖性
Arch Biochem Biophys. 1980 Sep;203(2):542-52. doi: 10.1016/0003-9861(80)90211-8.
5
Resonance Raman spectroscopy of arsanilazocarboxypeptidase A: conformational equilibria in solution and crystal phases.对氨基苯胂酸羧肽酶A的共振拉曼光谱：溶液和晶相中构象平衡
Biochemistry. 1980 Feb 19;19(4):759-66. doi: 10.1021/bi00545a023.
6
Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A resolution.
J Mol Biol. 1982 Sep 25;160(3):475-98. doi: 10.1016/0022-2836(82)90309-6.
7
Binding of ligands to the active site of carboxypeptidase A.配体与羧肽酶A活性位点的结合。
Proc Natl Acad Sci U S A. 1981 Sep;78(9):5455-9. doi: 10.1073/pnas.78.9.5455.
8
Carboxypeptidase A mechanisms.羧肽酶A的作用机制。
Proc Natl Acad Sci U S A. 1980 Jul;77(7):3875-8. doi: 10.1073/pnas.77.7.3875.
9
Structure of an actively exchanging complex between carboxypeptidase A and a substrate analogue.羧肽酶A与底物类似物之间的活性交换复合物的结构。
Proc Natl Acad Sci U S A. 1980 Jun;77(6):3288-91. doi: 10.1073/pnas.77.6.3288.
10
Refined crystal structure of carboxypeptidase A at 1.54 A resolution.分辨率为1.54埃的羧肽酶A的精细晶体结构。
J Mol Biol. 1983 Aug 5;168(2):367-87. doi: 10.1016/s0022-2836(83)80024-2.

pH对羧肽酶A结构和功能的影响：晶体学研究

Effects of pH on the structure and function of carboxypeptidase A: crystallographic studies.

作者信息

Shoham G, Rees D C, Lipscomb W N

出版信息

Proc Natl Acad Sci U S A. 1984 Dec;81(24):7767-71. doi: 10.1073/pnas.81.24.7767.

DOI:10.1073/pnas.81.24.7767
PMID:6595659
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC392233/
Abstract

High-resolution crystal structures are described for carboxypeptidase A (EC 3.4.17.1) in crystals grown at pH 8.5, 9.0, and 9.5 and compared with the structure at pH 7.5. The comparison shows that in the pH range of 7.5-9.5 the enzyme structure is practically unchanged, and, most importantly, that the flexible side chain of Tyr-248 remains exclusively in the "up" position, away from the Zn atom, throughout the pH range. There is no evidence for binding of Tyr-248 to Zn at any of these pH values. We conclude that the interaction of Tyr-248 with Zn is not an essential part of the mechanism of carboxypeptidase A and that its occurrence is an artifact of chemical modification of Tyr-248. It is also suggested that Tyr-248 is not uniquely associated with the observed high pK of the enzymatic hydrolysis.

摘要

描述了在pH 8.5、9.0和9.5条件下生长的晶体中羧肽酶A（EC 3.4.17.1）的高分辨率晶体结构，并与pH 7.5时的结构进行了比较。比较结果表明，在7.5 - 9.5的pH范围内，酶的结构基本不变，最重要的是，在整个pH范围内，Tyr - 248的柔性侧链始终仅处于“向上”位置，远离锌原子。没有证据表明在这些pH值中的任何一个下Tyr - 248与锌结合。我们得出结论，Tyr - 248与锌的相互作用不是羧肽酶A作用机制的必要部分，其出现是Tyr - 248化学修饰的假象。还表明Tyr - 248与观察到的酶促水解的高pK值并非唯一相关。