An engineered chorismate mutase with allosteric regulation (Q44485770)

3 December 2017

title

An engineered chorismate mutase with allosteric regulation (English)

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3 December 2017

Sheng Zhang

1

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3 December 2017

David B Wilson

series ordinal

2

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3 December 2017

Bruce Ganem

series ordinal

3

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3 December 2017

language of work or name

English

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publication date

1 July 2003

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Bioorganic & Medicinal Chemistry

3 December 2017

published in

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3 December 2017

volume

11

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3 December 2017

issue

14

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3 December 2017

page(s)

3109-3114

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Chorismate Mutase-Prephenate Dehydratase fromEscherichia coli

3 December 2017

cites work

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Regulation of Phenylalanine Biosynthesis. Studies on the Mechanism of Phenylalanine Binding and Feedback Inhibition in theEscherichia coliP-Protein†

1 reference

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7 January 2021

The self-association of chorismate mutase/prephenate dehydratase from Escherichia coli K12

1 reference

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7 January 2021

Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 2. Evidence for identical subunits catalysing the two activities

1 reference

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7 January 2021

Chorismate mutase:prephenate dehydratase from Acinetobacter calcoaceticus. Purification, properties and immunological cross-reactivity

1 reference

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7 January 2021

Loss of allosteric control but retention of the bifunctional catalytic competence of a fusion protein formed by excision of 260 base pairs from the 3' terminus of pheA from Erwinia herbicola

1 reference

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7 January 2021

Location of the active site of allosteric chorismate mutase from Saccharomyces cerevisiae, and comments on the catalytic and regulatory mechanisms

1 reference

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7 January 2021

Site-directed mutagenesis of monofunctional chorismate mutase engineered from the E. coli P-protein.

1 reference

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7 January 2021

Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase

1 reference

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7 January 2021

Engineering aspartate transcarbamylase

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7 January 2021

One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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7 January 2021

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

1 reference

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7 January 2021

10.1016/S0968-0896(03)00242-6

Identifiers

DOI

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3 December 2017

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