A kinetic and structural comparison of chorismate mutase/prephenate dehydratase from mutant strains of Escherichia coli K12 defective in the PheA gene-Reference-Cited by-同舟云学术

A kinetic and structural comparison of chorismate mutase/prephenate dehydratase from mutant strains of Escherichia coli K12 defective in the PheA gene

Published:1981-10 Issue:1 Volume:211 Page:66-75
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Baldwin Graham S.,Davidson Barrie E.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference37 articles.

1. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase

2. Chorismate Mutase-Prephenate Dehydratase from Escherichia coli K-12

3. Chorismate Mutase/Prephenate Dehydratase from Escherichia coli K12. Modification with 5,5'-Dithio-bis(2-nitrobenzoic acid)

4. Chorismate Mutase/Prephenate Dehydratase from Escherichia coli K12. Effects of Chemical Modification on the Enzymic Activities and Allosteric Inhibition

5. Chorismate mutase-prephenate dehydratase from Escherichia coli: active sites of a bifunctional enzyme

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