Multivalent regulation of isoleucine-valine transaminase in an Escherichia coli K-12 ilvA deletion strain. 1977

E L Kline, and D N Manross, and M L Warwick

In a strain of Escherichia coli K-12 lacking threonine deaminase, the enzyme converting alpha-ketoisovalerate and alpha-keto-beta-methylvalerate to valine and isoleucine, respectively, was multivalently repressed by valine, isoleucine, and leucine. This activity was due to transaminase B, specified by the ilvE structural gene.

UI MeSH Term Description Entries
D007532 Isoleucine An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels. Alloisoleucine,Isoleucine, L-Isomer,L-Isoleucine,Isoleucine, L Isomer,L-Isomer Isoleucine
D002872 Chromosome Deletion Actual loss of portion of a chromosome. Monosomy, Partial,Partial Monosomy,Deletion, Chromosome,Deletions, Chromosome,Monosomies, Partial,Partial Monosomies
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005796 Genes A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms. Cistron,Gene,Genetic Materials,Cistrons,Genetic Material,Material, Genetic,Materials, Genetic
D000637 Transaminases A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1. Aminotransferase,Aminotransferases,Transaminase
D013913 Threonine Dehydratase A pyridoxal-phosphate protein that catalyzes the deamination of THREONINE to 2-ketobutyrate and AMMONIA. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for ISOLEUCINE biosynthesis, while in the latter it is only involved in the breakdown of threonine to supply energy. This enzyme was formerly listed as EC 4.2.1.16. Threonine Deaminase,Threonine Dehydrase,Threonine Ammonia-Lyase,Ammonia-Lyase, Threonine,Deaminase, Threonine,Dehydrase, Threonine,Dehydratase, Threonine,Threonine Ammonia Lyase
D014633 Valine A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway. L-Valine,L Valine

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