Biodegradative l -Threonine Deaminase of Salmonella typhimurium

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منابع مشابه

Biodegradative L-threonine deaminase of Salmonella typhimurium.

The threonine deaminase formed under anaerobic conditions by Salmonella typhimurium is induced by l-serine and l-threonine, is catabolite repressible, requires cyclic adenosine 3',5'-monophosphate for its synthesis and adenylic acid for optimal activity, and is immunologically different from biosynthetic threonine deaminase.

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Threonine Deaminase from Salmonella typhimurium

Purified threonine deaminase of Salmonella typhimurium was found to be monodisperse and to have a molecular weight of 194,000. The protein, in 6 M guanidine HCI and 0.1 M P-mercaptoethanol, dissociates into polypeptide chains of molecular weight 48,500. Tryptic peptide analysis implies that the four component chains of the native enzyme are of identical amino acid sequence. L-Isoleucine and L-v...

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Multivalent induction of biodegradative threonine deaminase.

To determine the inducer(s) of the biodegradative threonine deaminase in Escherichia coli, the effects of various amino acids on the synthesis of this enzyme were investigated. The complex medium used hitherto for the enzyme induction can be completely replaced by a synthetic medium composed of 18 natural amino acids. In this synthetic medium, the omission of each of the seven amino acids threo...

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Threonine deaminase from Salmonella typhimurium. II. The subunit structure.

Purified threonine deaminase of Salmonella typhimurium was found to be monodisperse and to have a molecular weight of 194,000. The protein, in 6 M guanidine HCI and 0.1 M P-mercaptoethanol, dissociates into polypeptide chains of molecular weight 48,500. Tryptic peptide analysis implies that the four component chains of the native enzyme are of identical amino acid sequence. L-Isoleucine and L-v...

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Formation of biodegradative threonine deaminase in Escherichia coli.

Studies were carried out on the formation of biodegradative L-threonine deaminase (EC 4.2.1.16) in resting cells of Escherichia coli. The results obtained are as follows: (1) The enzyme level was increased by adding L-threonine together with yeast extract to the cell suspension. (2) In the course of the enzyme formation, the addition of chloramphenicol or glucose to the medium resulted in insta...

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1974

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.120.1.559-561.1974