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1
Confirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme.通过使用特定的氮-15标记酶来确认丝氨酸蛋白酶低场质子共振的归属。
Proc Natl Acad Sci U S A. 1985 Dec;82(23):7948-51. doi: 10.1073/pnas.82.23.7948.
2
Nitrogen-15 NMR spectroscopy of the catalytic-triad histidine of a serine protease in peptide boronic acid inhibitor complexes.肽硼酸抑制剂复合物中丝氨酸蛋白酶催化三联体组氨酸的氮-15核磁共振光谱。
Biochemistry. 1988 Oct 4;27(20):7689-97. doi: 10.1021/bi00420a018.
3
Carbon nuclear magnetic resonance studies of the histidine residue in alpha-lytic protease. Implications for the catalytic mechanism of serine proteases.α-裂解蛋白酶中组氨酸残基的碳核磁共振研究。对丝氨酸蛋白酶催化机制的启示。
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4
Catalytic mechanism of serine proteases: reexamination of the pH dependence of the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic protease.丝氨酸蛋白酶的催化机制：对α-裂解蛋白酶催化三联体中组氨酸1J13C2-H耦合常数pH依赖性的重新审视。
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High-resolution nitrogen-15 nuclear magnetic resonance studies of alpha-lytic protease in solid state. Direct comparison of enzyme structure in solution and in the solid state.固态α-裂解蛋白酶的高分辨率氮-15核磁共振研究。溶液和固态中酶结构的直接比较。
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8
15N NMR spectroscopy of hydrogen-bonding interactions in the active site of serine proteases: evidence for a moving histidine mechanism.丝氨酸蛋白酶活性位点中氢键相互作用的15N核磁共振光谱：移动组氨酸机制的证据
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Science. 1994 Jun 24;264(5167):1927-30. doi: 10.1126/science.7661899.

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本文引用的文献

1
Proton nuclear magnetic resonance evidence for the absence of a stable hydrogen bond between the active site aspartate and histidine residues of native subtilisins and for its presence in thiolsubtilisins.
Biochemistry. 1981 Oct 27;20(22):6366-70. doi: 10.1021/bi00525a013.
2
Nitrogen-15-labeled yeast tRNAPhe: double and two-dimensional heteronuclear NMR of guanosine and uracil ring NH groups.氮-15标记的酵母苯丙氨酸转运核糖核酸：鸟苷和尿嘧啶环NH基团的二维和双维异核核磁共振
Biochemistry. 1984 Sep 11;23(19):4395-400. doi: 10.1021/bi00314a024.
3
High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. II. Polarization of histidine 57 by substrate analogues and competitive inhibitors.胰凝乳蛋白酶活性位点的高分辨率核磁共振研究。II. 底物类似物和竞争性抑制剂对组氨酸57的极化作用
J Mol Biol. 1974 Jul 5;86(3):541-58. doi: 10.1016/0022-2836(74)90179-x.
4
High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. I. The hydrogen bonded protons of the "charge relay" system.胰凝乳蛋白酶活性位点的高分辨率核磁共振研究。I. “电荷中继”系统的氢键质子。
J Mol Biol. 1974 Jul 5;86(3):519-40. doi: 10.1016/0022-2836(74)90178-8.
5
High resolution nuclear magnetic resonance study of the histidine--aspartate hydrogen bond in chymotrypsin and chymotrypsinogen.胰凝乳蛋白酶和胰凝乳蛋白酶原中组氨酸-天冬氨酸氢键的高分辨率核磁共振研究。
J Mol Biol. 1972 Nov 14;71(2):507-11. doi: 10.1016/0022-2836(72)90366-x.
6
Carbon nuclear magnetic resonance studies of the histidine residue in alpha-lytic protease. Implications for the catalytic mechanism of serine proteases.α-裂解蛋白酶中组氨酸残基的碳核磁共振研究。对丝氨酸蛋白酶催化机制的启示。
Biochemistry. 1973 Nov 6;12(23):4732-43. doi: 10.1021/bi00747a028.
7
Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transfer.丝氨酸蛋白酶的作用机制：四面体中间体与协同质子转移
Biochemistry. 1976 Dec 14;15(25):5581-8. doi: 10.1021/bi00670a024.
8
A detailed structural comparison between the charge relay system in chymotrypsinogen and in alpha-chymotrypsin.
Biochemistry. 1976 Oct 5;15(20):4481-5. doi: 10.1021/bi00665a023.
9
Hydrogen bonds in serine proteinases and their complexes with protein proteinase inhibitors. Proton nuclear magnetic resonance studies.
Biochemistry. 1978 Oct 31;17(22):4648-56. doi: 10.1021/bi00615a010.
10
Zymogen activation in serine proteinases. Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and chymotrypsin Aalpha.丝氨酸蛋白酶中的酶原激活。牛胰凝乳蛋白酶原A和α-胰凝乳蛋白酶的两个组氨酸的质子磁共振pH滴定研究。
Biochemistry. 1978 Oct 31;17(22):4627-40. doi: 10.1021/bi00615a008.

通过使用特定的氮-15标记酶来确认丝氨酸蛋白酶低场质子共振的归属。

Confirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme.

作者信息

Bachovchin W W

出版信息

Proc Natl Acad Sci U S A. 1985 Dec;82(23):7948-51. doi: 10.1073/pnas.82.23.7948.

DOI:10.1073/pnas.82.23.7948
PMID:3934665
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC390887/
Abstract

Proton NMR spectra of serine proteases in 1H2O solutions typically show a single resonance at very low magnetic field--i.e., 14-18 ppm from dimethylsilylapentanesulfonate. This resonance has been assigned to the proton hydrogen bonded between aspartic acid-102 and histidine-57 (chymotrypsin numbering system) of the "charge-relay system" or catalytic triad of serine proteases [Robillard, G. & Shulman, R. G. (1972) J. Mol. Biol. 71, 507-511]. Since then, there have been a number of reports that have cast doubt on its correctness. In the present work we have tested this assignment using alpha-lytic protease (EC 3.4.21.12, Myxobacter alpha-lytic proteinase), a bacterial serine protease homologous to elastase, which is specifically labeled with nitrogen-15 at N delta 1 of its single histidine residue. The low-field region of the proton spectra of this labeled enzyme shows a single resonance having the properties reported [Robillard, G. & Shulman, R. G. (1974) J. Mol. Biol. 86, 519-540], which, in addition, exhibits spin-spin splitting to the nitrogen-15 label. The observation of this 15N delta 1-H coupling makes the assignment of this resonance to the charge-relay proton unequivocal.

摘要

丝氨酸蛋白酶在(^{1}H_{2}O)溶液中的质子核磁共振谱通常在非常低的磁场下显示出单一共振峰——即相对于二甲基硅烷基戊烷磺酸盐为(14 - 18) ppm。该共振峰已被指定为丝氨酸蛋白酶“电荷中继系统”或催化三联体中天门冬氨酸 - 102和组氨酸 - 57（胰凝乳蛋白酶编号系统）之间氢键结合的质子[罗比拉德，G. 和舒尔曼，R. G.（1972年）《分子生物学杂志》71卷，507 - 511页]。从那时起，有许多报告对其正确性提出了质疑。在本研究中，我们使用α - 裂解蛋白酶（EC 3.4.21.12，粘细菌α - 裂解蛋白酶）对这一指定进行了测试，α - 裂解蛋白酶是一种与弹性蛋白酶同源的细菌丝氨酸蛋白酶，其单个组氨酸残基的(Nδ1)被氮 - 15特异性标记。这种标记酶的质子谱低场区域显示出一个具有所报道性质的单一共振峰[罗比拉德，G. 和舒尔曼，R. G.（1974年）《分子生物学杂志》86卷，519 - 540页]，此外，该共振峰对氮 - 15标记表现出自旋 - 自旋分裂。这种(^{15}Nδ1 - H)耦合的观察结果使得将该共振峰指定为电荷中继质子变得明确无疑。