Chemical modification of glucosamine-6-phosphate synthase by diethyl pyrocarbonate: Evidence of histidine requirement for enzymatic activity
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference23 articles.
1. Glucosamine-6-phosphate synthase from Escherichia coli yields two proteins upon limited proteolysis: Identification of the glutamine amidohydrolase and 2R ketose/aldose isomerase-bearing domains based on their biochemical properties
2. Possible involvement of Lys603 from Escherichia coli glucosamine-6-phosphate synthase in the binding of its substrate fructose 6-phosphate
3. Glucosamine-6-phosphate synthase from Escherichia coli: mechanism of the reaction at the fructose 6-phosphate binding site
4. A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases
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