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2
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本文引用的文献

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Transamination in Escherichia coli.大肠杆菌中的转氨作用。
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Analysis of an avtA::Mu d1(Ap lac) mutant: metabolic role of transaminase C.avtA::Mu d1（Ap lac）突变体分析：转氨酶C的代谢作用
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Inactivation of the dadB Salmonella typhimurium alanine racemase by D and L isomers of beta-substituted alanines: kinetics, stoichiometry, active site peptide sequencing, and reaction mechanism.β-取代丙氨酸的D型和L型异构体对鼠伤寒沙门氏菌dadB丙氨酸消旋酶的失活作用：动力学、化学计量学、活性位点肽段测序及反应机制
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In vivo DNA cloning and adjacent gene fusing with a mini-Mu-lac bacteriophage containing a plasmid replicon.利用含有质粒复制子的微型Mu - lac噬菌体进行体内DNA克隆及相邻基因融合。
Proc Natl Acad Sci U S A. 1984 Mar;81(5):1480-3. doi: 10.1073/pnas.81.5.1480.
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Role of alanine-valine transaminase in Salmonella typhimurium and analysis of an avtA::Tn5 mutant.丙氨酸-缬氨酸转氨酶在鼠伤寒沙门氏菌中的作用及avtA::Tn5突变体分析
J Bacteriol. 1983 Sep;155(3):1009-14. doi: 10.1128/jb.155.3.1009-1014.1983.
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Inhibition of growth of Salmonella typhimurium and of threonine deaminase and transaminase B by beta-chloroalanine.β-氯丙氨酸对鼠伤寒沙门氏菌生长以及苏氨酸脱氨酶和转氨酶B的抑制作用。
J Bacteriol. 1971 Feb;105(2):519-22. doi: 10.1128/jb.105.2.519-522.1971.
7
Interaction of L-aspartate beta-decarboxylase with beta-chloro-L-alanine. Beta-elimination reaction and active-site labeling.L-天冬氨酸β-脱羧酶与β-氯-L-丙氨酸的相互作用。β-消除反应与活性位点标记。
Biochemistry. 1969 Dec;8(12):5016-21. doi: 10.1021/bi00840a051.
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Regulation of transaminase C synthesis in Escherichia coli: conditional leucine auxotrophy.大肠杆菌中转氨酶C合成的调控：条件性亮氨酸营养缺陷型
J Bacteriol. 1974 Nov;120(2):715-23. doi: 10.1128/jb.120.2.715-723.1974.
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Inhibition studies of the enantiomers of beta chloroalanine on purified alanine racemase from B. subtilis.
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Identification of a mutation affecting an alanine-alpha-ketoisovalerate transaminase activity in Escherichia coli K-12.
Mol Gen Genet. 1979 Oct 2;176(1):147-9. doi: 10.1007/BF00334306.

β-氯-L-丙氨酸对大肠杆菌丙氨酸-缬氨酸转氨酶的抑制作用。

beta-Chloro-L-alanine inhibition of the Escherichia coli alanine-valine transaminase.

作者信息

Whalen W A, Wang M D, Berg C M

出版信息

J Bacteriol. 1985 Dec;164(3):1350-2. doi: 10.1128/jb.164.3.1350-1352.1985.

DOI:10.1128/jb.164.3.1350-1352.1985
PMID:3934143
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC219336/
Abstract

beta-Chloro-L-alanine, an amino acid analog which inhibits a number of enzymes, reversibly inhibited the Escherichia coli K-12 alanine-valine transaminase, transaminase C. This inhibition, along with the inhibition of transaminase B, accounted for the isoleucine-plus-valine requirement of E. coli in the presence of beta-chloro-L-alanine.

摘要

β-氯-L-丙氨酸是一种能抑制多种酶的氨基酸类似物，它可逆地抑制大肠杆菌K-12丙氨酸-缬氨酸转氨酶（转氨酶C）。这种抑制作用，连同对转氨酶B的抑制作用，解释了在存在β-氯-L-丙氨酸的情况下大肠杆菌对异亮氨酸加缬氨酸的需求。