Chorismate mutase/prephenate dehydratase from Escherichia coli K12. Effects of chemical modification on the enzymic activities and allosteric inhibition. - Suppr | 超能文献

Chorismate mutase/prephenate dehydratase from Escherichia coli K12. Effects of chemical modification on the enzymic activities and allosteric inhibition.

作者信息

Gething M J, Davidson B E

出版信息

Eur J Biochem. 1977 Aug 15;78(1):111-7. doi: 10.1111/j.1432-1033.1977.tb11719.x.

DOI:10.1111/j.1432-1033.1977.tb11719.x

Abstract

摘要

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Chorismate mutase/prephenate dehydratase from Escherichia coli K12. Effects of chemical modification on the enzymic activities and allosteric inhibition.

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The reactivity of the sulphydryl groups of chorismate mutase/prephenate dehydratase--a bifunctional enzyme of phenylalanine biosynthesis in Escherichia coli K12.

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Chorismate mutase/prephenate dehydratase from Escherichia coli K12. Modification with 5,5'-dithio-bis(2-nitrobenzoic acid).来自大肠杆菌K12的分支酸变位酶/预苯酸脱水酶。用5,5'-二硫代双（2-硝基苯甲酸）进行修饰。

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Chorismate mutase/prephenate dehydratase from Escherichia coli K12. Binding studies with the allosteric effector phenylalanine.

Eur J Biochem. 1978 May;86(1):165-74. doi: 10.1111/j.1432-1033.1978.tb12296.x.

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Kinetic studies on the mechanism of chorismate mutase/prephenate dehydratase from Escherichia coli K12.大肠杆菌K12分支酸变位酶/预苯酸脱水酶作用机制的动力学研究

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Chorismate mutase-prephenate dehydratase from Escherichia coli: active sites of a bifunctional enzyme.来自大肠杆菌的分支酸变位酶-预苯酸脱水酶：一种双功能酶的活性位点

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The self-association of chorismate mutase/prephenate dehydratase from Escherichia coli K12.来自大肠杆菌K12的分支酸变位酶/预苯酸脱水酶的自我缔合。

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Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 1. The effect of NaCl and its use in a new purification involving affinity chromatography on sepharosyl-phenylalanine.来自大肠杆菌K12的分支酸变位酶/预苯酸脱水酶。1. NaCl的作用及其在涉及琼脂糖基-苯丙氨酸亲和色谱的新纯化方法中的应用。

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Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins.来自大肠杆菌的分支酸变位酶-预苯酸脱水酶。利用基因工程蛋白对催化结构域和调节结构域的研究。

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Chorismate mutase/prephenate dehydrogenase: protection of the active site(s) against inactivation by iodoacetamide [proceedings].

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