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半胱氨酸与大肠杆菌的生长抑制:以苏氨酸脱氨酶作为靶酶

Cysteine and growth inhibition of Escherichia coli: threonine deaminase as the target enzyme.

作者信息

Harris C L

出版信息

J Bacteriol. 1981 Feb;145(2):1031-5. doi: 10.1128/jb.145.2.1031-1035.1981.

DOI:10.1128/jb.145.2.1031-1035.1981
PMID:7007336
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC217214/
Abstract

Cysteine has been shown to inhibit growth in Escherichia coli strains C6 and HfrH 72, but not M108A. Growth inhibition was overcome by inclusion of isoleucine, leucine, and valine in the medium. Isoleucine biosynthesis was apparently affected, since addition of this amino acid alone could alter the inhibitory effects of cysteine. Homocysteine, mercaptoethylamine, and mercaptoethanol inhibited growth to varying degrees in some strains, these effects also being prevented by addition of branched-chain amino acids. Cysteine, mercaptoethylamine, and homocysteine were inhibitors of threonine deaminase but not transaminase B, two enzymes of the ilvEDA operon. Cysteine inhibition of threonine deaminase was reversed by threonine, although the pattern of inhibition was mixed. These results suggest a relationship between the growth-inhibitory effects of cysteine and other sulfur compounds and the inhibition of isoleucine synthesis at the level of threonine deaminase.

摘要

已证明半胱氨酸可抑制大肠杆菌菌株C6和HfrH 72的生长,但对M108A菌株无抑制作用。在培养基中添加异亮氨酸、亮氨酸和缬氨酸可克服生长抑制。异亮氨酸的生物合成显然受到影响,因为单独添加这种氨基酸可改变半胱氨酸的抑制作用。同型半胱氨酸、巯基乙胺和巯基乙醇在某些菌株中不同程度地抑制生长,添加支链氨基酸也可防止这些作用。半胱氨酸、巯基乙胺和同型半胱氨酸是苏氨酸脱氨酶的抑制剂,但不是ilvEDA操纵子的两种酶——转氨酶B的抑制剂。苏氨酸可逆转半胱氨酸对苏氨酸脱氨酶的抑制作用,尽管抑制模式是混合的。这些结果表明,半胱氨酸和其他硫化合物的生长抑制作用与苏氨酸脱氨酶水平上异亮氨酸合成的抑制之间存在关联。

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本文引用的文献

1
Growth Requirements of Virus-Resistant Mutants of Escherichia Coli Strain "B".大肠杆菌菌株“B”的抗病毒突变体的生长需求
Proc Natl Acad Sci U S A. 1946 May;32(5):120-8. doi: 10.1073/pnas.32.5.120.
2
Isoleucine and valine metabolism in Escherichia coli. XI. Valine inhibition of the growth of Escherichia coli strain K-12.大肠杆菌中异亮氨酸和缬氨酸的代谢。XI. 缬氨酸对大肠杆菌K-12菌株生长的抑制作用。
J Bacteriol. 1962 Mar;83(3):624-30. doi: 10.1128/jb.83.3.624-630.1962.
3
Isoleucine and valine metabolism in Escherichia coli. VIII. The formation of acetolactate.大肠杆菌中异亮氨酸和缬氨酸的代谢。VIII. 乙酰乳酸的形成。
J Biol Chem. 1958 Nov;233(5):1156-60.
4
Interrelationships between amino-acids in the growth of coliform organisms.大肠菌生长过程中氨基酸之间的相互关系。
J Gen Microbiol. 1953 Aug;9(1):37-43. doi: 10.1099/00221287-9-1-37.
5
A requirement for beta-mercaptopyruvate in the in vitro thiolation of transfer ribonucleic acid.体外转移核糖核酸硫醇化过程中对β-巯基丙酮酸的需求。
Biochemistry. 1967 Mar;6(3):855-60. doi: 10.1021/bi00855a028.
6
Transport of sugars and amino acids in bacteria. IV. Regulation of valine transport activity by valine and cysteine.细菌中糖和氨基酸的转运。IV. 缬氨酸和半胱氨酸对缬氨酸转运活性的调节
J Biochem. 1971 Aug;70(2):215-24. doi: 10.1093/oxfordjournals.jbchem.a129633.
7
Sulfur-deficient transfer ribonucleic acid in a cysteine-requiring, "relaxed" mutant of Escherichia coli.大肠杆菌一种需要半胱氨酸的“松弛型”突变体中的缺硫转移核糖核酸
J Bacteriol. 1969 Dec;100(3):1322-7. doi: 10.1128/jb.100.3.1322-1327.1969.
8
Threonine deaminases.苏氨酸脱氨酶
Adv Enzymol Relat Areas Mol Biol. 1973;37:349-95. doi: 10.1002/9780470122822.ch6.
9
An assay for transaminase B enzyme activity in Escherichia coli K-12.大肠杆菌K-12中谷丙转氨酶B酶活性的测定
Anal Biochem. 1973 Jan;51(1):67-79. doi: 10.1016/0003-2697(73)90453-3.
10
Isoleucine and valine metabolism in Escherichia coli. 18. Induction of acetohydroxy acid isomeroreductase.大肠杆菌中异亮氨酸和缬氨酸的代谢。18. 乙酰羟酸异构还原酶的诱导。
J Bacteriol. 1972 Oct;112(1):131-41. doi: 10.1128/jb.112.1.131-141.1972.