Some Comparative Kinetic Data on the Enzyme Imidazoleacetol Phosphate:l-Glutamate Aminotransferase Derived from Mutant Strains of Salmonella typhimurium
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. The Genetic Control of the Enzymes of Histidine Biosynthesis in Salmonella typhimurium
2. Imidazolylacetolphosphate: l-Glutamate Aminotransferase
3. Imidazolylacetolphosphate: l-Glutamate Aminotransferase
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1. Biosynthesis of Histidine;EcoSal Plus;2009-02-13
2. Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5′-phosphate and l-histidinol phosphate;Journal of Molecular Biology;2001-08
3. L-Histidinol phosphate aminotransferase from Salmonella typhimurium. Kinetic behavior and sequence at the pyridoxal-P binding site;Biochimie;1989-04
4. Intracellular Roles of Microbial Aminotransferases: Overlap Enzymes Across Different Biochemical Pathways;CRC Critical Reviews in Microbiology;1981-01
5. Properties of the imidazolylacetolphosphate aminotransferase produced in a mutant demonstrating no apparent genetic involvement of the structural gene;Journal of Bacteriology;1975-07
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