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The binding of tyrosine and NAD+ to chorismate mutase/prephenate dehydrogenase from Escherichia coli K12 and the effects of these ligands on the activity and self-association of the enzyme. Analysis in terms of a model.

作者信息

Hudson G S, Howlett G J, Davidson B E

出版信息

J Biol Chem. 1983 Mar 10;258(5):3114-20.

PMID:6338013
Abstract
摘要

相似文献

1
The binding of tyrosine and NAD+ to chorismate mutase/prephenate dehydrogenase from Escherichia coli K12 and the effects of these ligands on the activity and self-association of the enzyme. Analysis in terms of a model.酪氨酸和NAD⁺与来自大肠杆菌K12的分支酸变位酶/预苯酸脱氢酶的结合以及这些配体对该酶活性和自缔合的影响。基于一个模型的分析。
J Biol Chem. 1983 Mar 10;258(5):3114-20.
2
Chorismate mutase-prephenate dehydrogenase from Escherichia coli: cooperative effects and inhibition by L-tyrosine.来自大肠杆菌的分支酸变位酶-预苯酸脱氢酶：协同效应及L-酪氨酸的抑制作用
Arch Biochem Biophys. 1985 Aug 1;240(2):646-54. doi: 10.1016/0003-9861(85)90072-4.
3
Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Kinetic mechanism of the prephenate dehydrogenase reaction.来自大肠杆菌的分支酸变位酶-预苯酸脱氢酶。预苯酸脱氢酶反应的动力学机制。
Biochim Biophys Acta. 1982 Apr 3;702(2):212-9. doi: 10.1016/0167-4838(82)90505-2.
4
Characterization of monofunctional chorismate mutase/prephenate dehydrogenase enzymes obtained via mutagenesis of recombinant plasmids in vitro.通过体外重组质粒诱变获得的单功能分支酸变位酶/预苯酸脱氢酶的特性分析。
Eur J Biochem. 1982 Jun;124(3):513-9. doi: 10.1111/j.1432-1033.1982.tb06623.x.
5
Chorismate mutase-prephenate dehydrogenase from Escherichia coli. 2. Evidence for two different active sites.来自大肠杆菌的分支酸变位酶-预苯酸脱氢酶。2. 存在两个不同活性位点的证据。
Biochemistry. 1990 Nov 6;29(44):10255-61. doi: 10.1021/bi00496a015.
6
The prephenate dehydrogenase component of the bifunctional T-protein in enteric bacteria can utilize L-arogenate.肠道细菌中双功能T蛋白的预苯酸脱氢酶组分能够利用L-阿洛酮糖酸。
FEBS Lett. 1987 May 25;216(1):133-9. doi: 10.1016/0014-5793(87)80771-8.
7
Chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes: evidence that the two reactions occur at one active site.产气气杆菌的分支酸变位酶-预苯酸脱氢酶：两个反应发生在一个活性位点的证据。
Biochemistry. 1979 Jun 26;18(13):2766-75. doi: 10.1021/bi00580a012.
8
Chorismate mutase-prephenate dehydrogenase from Escherichia coli.来自大肠杆菌的分支酸变位酶-预苯酸脱氢酶
Methods Enzymol. 1987;142:440-50. doi: 10.1016/s0076-6879(87)42055-7.
9
Regulation of Chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from alcaligenes eutrophus.真养产碱杆菌分支酸变位酶-预苯酸脱水酶和预苯酸脱氢酶的调控
J Bacteriol. 1976 May;126(2):723-32. doi: 10.1128/jb.126.2.723-732.1976.
10
Chorismate mutase/prephenate dehydrogenase from Escherichia coli K12: purification, characterization, and identification of a reactive cysteine.来自大肠杆菌K12的分支酸变位酶/预苯酸脱氢酶：纯化、特性鉴定及一个活性半胱氨酸的识别
Biochemistry. 1984 Dec 4;23(25):6240-9. doi: 10.1021/bi00320a054.

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Production of aromatic amino acids and their derivatives by Escherichia coli and Corynebacterium glutamicum.大肠杆菌和谷氨酸棒杆菌对芳香族氨基酸及其衍生物的生产。
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共生古菌中芳香族氨基酸生物合成的两种关键酶的表征
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Functional mapping of protein-protein interactions in an enzyme complex by directed evolution.通过定向进化对酶复合物中蛋白质-蛋白质相互作用进行功能图谱绘制。
PLoS One. 2014 Dec 31;9(12):e116234. doi: 10.1371/journal.pone.0116234. eCollection 2014.
5
Metabolic engineering of Escherichia coli for L-tyrosine production by expression of genes coding for the chorismate mutase domain of the native chorismate mutase-prephenate dehydratase and a cyclohexadienyl dehydrogenase from Zymomonas mobilis.通过表达编码天然分支酸变位酶-预苯酸脱水酶的分支酸变位酶结构域的基因以及来自运动发酵单胞菌的环己二烯基脱氢酶，对大肠杆菌进行代谢工程改造以生产L-酪氨酸。
Appl Environ Microbiol. 2008 May;74(10):3284-90. doi: 10.1128/AEM.02456-07. Epub 2008 Mar 14.
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Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus.嗜热细菌水生栖热菌中预苯酸脱氢酶的生化特性
Protein Sci. 2006 Jun;15(6):1417-32. doi: 10.1110/ps.051942206.
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Feedback inhibition of chorismate mutase/prephenate dehydrogenase (TyrA) of Escherichia coli: generation and characterization of tyrosine-insensitive mutants.大肠杆菌分支酸变位酶/预苯酸脱氢酶（TyrA）的反馈抑制：酪氨酸不敏感突变体的产生与特性分析
Appl Environ Microbiol. 2005 Nov;71(11):7224-8. doi: 10.1128/AEM.71.11.7224-7228.2005.