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- W1027435936 abstract "Tryptophan synthetase (L-serine hydrolyase) is a multimeric enzyme catalyzing the terminal reaction in the biosynthesis of L-tryptophan by microbes arid plants. In general, these enzymes in bacteria and plants appear to dissociate readily and reversibly into smaller subunits, while those of fungi do not. Several factors have made E. coli tryptophan synthetase an enzyme of choice for studies of transcription and translation and the regulation of these processes. The structural genes for α and β chains are adjacent to each other and are well mapped. They comprise the two most distal genes of the multigenic trp operon. All or portions of this operon have been translocated to the chromosome of a series of temperate bacteriophage mutants. DNA from these bacteriophages has been used to quantitate the amount of messenger RNA corresponding to various segments of the operon. The α chain of tryptophan synthetase has been isolated in pure form from Escherichia coli (K-12 and B strains), Salmonella typhimurium, Shigella dysenteriae, Aerobacter aerogenes, and Pseudomonas putida. The molecular weight of the α chain obtained from these sources is approximately 29,000." @default.
- W1027435936 created "2016-06-24" @default.
- W1027435936 creator A5035201213 @default.
- W1027435936 creator A5052993074 @default.
- W1027435936 date "1972-01-01" @default.
- W1027435936 modified "2023-10-03" @default.
- W1027435936 title "1 Tryptophan Synthetase" @default.
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- W1027435936 doi "https://doi.org/10.1016/s1874-6047(08)60445-x" @default.
- W1027435936 hasPublicationYear "1972" @default.
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