• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

利用质子磁共振波谱对大肠杆菌天冬氨酸转氨酶使氨基酸发生特定α-氘代反应进行的动力学研究。

Kinetic studies with the use of proton-magnetic-resonance spectroscopy of the specific alpha-deuteration of amino acids by Escherichia coli aspartate aminotransferase.

作者信息

Gout E, Chesne S, Beguin C G, Pelmont J

出版信息

Biochem J. 1978 Jun 1;171(3):719-23. doi: 10.1042/bj1710719.

DOI:10.1042/bj1710719
PMID:352342
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1184019/
Abstract

Escherichia coli aspartate aminotransferase was exposed to aspartate or phenylalanine without oxo acid in buffered 2H2O. The alpha-hydrogen of the amino acids underwent first-order exchange with respect to both substrate and enzyme. P.m.r. spectroscopy gave consistent reaction-rate constants. The deuterium-exchange rate was only moderately increased by addition of oxo acids and was of the same order as the transamination rate. No beta-deuteration was observed. The C(alpha)-H-bond-breaking step is discussed as a part of the entire transamination mechanism.

摘要

在缓冲的重水(2H₂O)中,将大肠杆菌天冬氨酸转氨酶暴露于无酮酸的天冬氨酸或苯丙氨酸中。氨基酸的α-氢与底物和酶均发生一级交换。核磁共振光谱给出了一致的反应速率常数。加入酮酸后,氘交换速率仅适度增加,且与转氨速率处于同一量级。未观察到β-氘化现象。讨论了C(α)-H键断裂步骤作为整个转氨机制的一部分。

相似文献

1
Kinetic studies with the use of proton-magnetic-resonance spectroscopy of the specific alpha-deuteration of amino acids by Escherichia coli aspartate aminotransferase.利用质子磁共振波谱对大肠杆菌天冬氨酸转氨酶使氨基酸发生特定α-氘代反应进行的动力学研究。
Biochem J. 1978 Jun 1;171(3):719-23. doi: 10.1042/bj1710719.
2
[Transamination of L-aspartate and L-phenylalanine in Escherichia coli K 12].[大肠杆菌K12中L-天冬氨酸和L-苯丙氨酸的转氨作用]
Biochimie. 1975;57(9):1029-34. doi: 10.1016/s0300-9084(75)80358-0.
3
The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km.大肠杆菌天冬氨酸转氨酶中酪氨酸-225突变为苯丙氨酸,导致分光光度法和动力学pKa值发生碱性转变,同时kcat和Km值降低。
Biochemistry. 1991 Jan 8;30(1):305-12. doi: 10.1021/bi00215a041.
4
Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.通过同源建模和定点诱变将大肠杆菌天冬氨酸转氨酶的底物特异性重新设计为大肠杆菌酪氨酸转氨酶的底物特异性。
Protein Sci. 1995 Sep;4(9):1750-7. doi: 10.1002/pro.5560040910.
5
The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis.大肠杆菌天冬氨酸转氨酶催化的反应有多个部分速率决定步骤,而Y225F突变体催化的反应则以酮亚胺水解为主。
Biochemistry. 1996 Apr 23;35(16):5280-91. doi: 10.1021/bi952138d.
6
The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases.利用天然和非天然氨基酸底物来界定大肠杆菌天冬氨酸转氨酶和酪氨酸转氨酶的底物特异性差异。
Protein Sci. 1995 Sep;4(9):1743-9. doi: 10.1002/pro.5560040909.
7
Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change.通过将天冬氨酸转氨酶222位的天冬氨酸替换为丙氨酸来表征大肠杆菌中天冬氨酸转氨酶诱导的明显负协同性。存在极其缓慢的构象变化的证据。
Protein Eng. 1994 Mar;7(3):413-24. doi: 10.1093/protein/7.3.413.
8
Nonidentity of the aspartate and the aromatic aminotransferase components of transaminase A in Escherichia coli.大肠杆菌中转氨酶A中天冬氨酸和芳香族氨基转移酶成分的非同一性。
J Bacteriol. 1972 Oct;112(1):365-71. doi: 10.1128/jb.112.1.365-371.1972.
9
Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity.
Biochemistry. 1990 Jun 12;29(23):5469-76. doi: 10.1021/bi00475a010.
10
Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases.缺乏天冬氨酸和芳香族氨基酸转氨酶的大肠杆菌突变体。
J Bacteriol. 1977 Apr;130(1):429-40. doi: 10.1128/jb.130.1.429-440.1977.

本文引用的文献

1
Mechanism of transaminase action.转氨酶作用机制。
Biochem J. 1961 Jan;78(1):116-9. doi: 10.1042/bj0780116.
2
Mechanisms in enzymatic transamination; effect of alpha-ketoglutarate concentration on the rate of exchange of the hydrogen of aspartate.酶促转氨作用的机制;α-酮戊二酸浓度对天冬氨酸氢交换速率的影响。
J Biol Chem. 1956 Apr;219(2):833-43.
3
Nuclear magnetic resonance spectroscopy of amino acids, peptides, and proteins.氨基酸、肽和蛋白质的核磁共振光谱学
Adv Protein Chem. 1970;24:447-545. doi: 10.1016/s0065-3233(08)60246-6.
4
[Glutamate-oxaloacetate transaminase of Escherichia coli: II. Properties].
Biochimie. 1974;56(5):631-9. doi: 10.1016/s0300-9084(74)80033-7.
5
[Glutamate-oxaloacetate transaminase from Escherichia coli. I. Purification and specificity].[来自大肠杆菌的谷氨酸草酰乙酸转氨酶。I. 纯化与特异性]
Biochimie. 1973;55(3):237-44. doi: 10.1016/s0300-9084(73)80121-x.
6
Proton magnetic resonance studies of glutamate-alanine transaminase-catalyzed deuterium exchange. Evidence for proton conservation during prototropic transfer from the alpha carbon of L-alanine to the C4-position of pyridoxal 5'-phosphate.谷氨酸-丙氨酸转氨酶催化的氘交换的质子磁共振研究。L-丙氨酸α-碳上的质子向磷酸吡哆醛5'-磷酸C4位质子转移过程中质子守恒的证据。
J Biol Chem. 1976 Feb 25;251(4):1088-96.
7
Hydrogen exchane at the beta-carbon of amino acids during transamination.转氨基作用过程中氨基酸β-碳上的氢交换。
Eur J Biochem. 1975 Nov 15;59(2):395-403. doi: 10.1111/j.1432-1033.1975.tb02467.x.
8
Letter: Conformational analysis of amino acids and peptides using specific isotope substitution. II. Conformation of serine, tyrosine, phenylalanine, aspartic acid, asparagine, and aspartic acid beta-methyl ester in various ionization states.信函:使用特定同位素取代对氨基酸和肽进行构象分析。II. 丝氨酸、酪氨酸、苯丙氨酸、天冬氨酸、天冬酰胺及天冬氨酸β-甲酯在不同电离状态下的构象
J Am Chem Soc. 1975 Sep 17;97(19):5630-1. doi: 10.1021/ja00852a077.
9
Twin pigeon embryos.双鸽胚胎。
Poult Sci. 1976 Sep;55(5):1976-7. doi: 10.3382/ps.0551976.
10
Nuclear magnetic resonance studies of D2O-substrate exchange reactions catalyzed by glutamic pyruvic and glutamic oxaloacetic transaminases.谷氨酸丙酮酸转氨酶和谷氨酸草酰乙酸转氨酶催化的D2O-底物交换反应的核磁共振研究。
Biochemistry. 1976 Dec 14;15(25):5671-8. doi: 10.1021/bi00670a037.