Escherichia coli K-12 mutant with alternate requirements for vitamin B6 or branched-chain amino acids and lacking transaminase C activity.
نویسنده
چکیده
An Escherichia coli K-12 auxotrophic derivative that grows if supplemented with pyridoxine, isoleucine, leucine, or alanine is described.
منابع مشابه
Regulation of transaminase C synthesis in Escherichia coli: conditional leucine auxotrophy.
The regulation of synthesis of the valine-alanine-alpha-aminobutyrate transaminase (transaminase C) was studied in Escherichia coli mutants lacking the branched-chain amino acid transaminase (transaminase B). An investigation was made of two strains, CU2 and CU2002, each carrying the same transaminase B lesion but exhibiting different growth responses on a medium supplemented with branched-chai...
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The major component of leucine uptake in Escherichia coli K-12 is a common system for l-leucine, l-isoleucine, and l-valine (LIV-I) with a Michaelis constant (K(m)) value of 0.2 muM (LIV-I system). The LIV-binding protein appears to be associated with this system. It now appears that the LIV-I transport system and LIV-binding protein also serve for the entry of l-alanine, l-threonine, and possi...
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The herbicide sulfometuron methyl is a potent inhibitor of the branched-chain amino acid biosynthetic enzyme acetolactate synthase (ALS) isolated from bacteria, fungi, and plants. However, it did not prevent growth of wild-type Salmonella typhimurium LT2 or Escherichia coli K-12. These species each contain two acetolactate synthase isozymes. Growth of S. typhimurium and E. coli mutants lacking ...
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Three experiments were carried out on a total of 78 female rats to examine the effect of an excess intake of leucine, with and without additions of vitamin B6 and/or niacin, on the excretion of tryptophan and niacin metabolites, and on branched-chain amino acid transaminase activity in some organs and on serum amino acid levels. An excess in take of leucine (10% leucine) retarded the growth of ...
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The growth recovery of Escherichia coli K-12 and Salmonella enterica serovar Typhimurium DeltarelA mutants were compared after nutritional downshifts requiring derepression of the branched-chain amino acid pathways. Because wild-type E. coli K-12 and S. enterica serovar Typhimurium LT2 strains are defective in the expression of the genes encoding the branch point acetohydroxy acid synthetase II...
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ورودعنوان ژورنال:
- Journal of bacteriology
دوره 130 1 شماره
صفحات -
تاریخ انتشار 1977