Occurrence of a Catabolic l-Serine (l-Threonine) Deaminase in Saccharomyces cerevisiae
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چکیده
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.
متن کاملMolecular genetics of serine and threonine catabolism in Saccharomyces cerevisiae.
The catabolic L-serine (L-threonine) deaminase of Saccharomyces cerevisiae allows the yeast to grow on media with L-serine or L-threonine as sole nitrogen source. A mutant, cha1 (catabolism of hydroxyamino acids), lacking this enzyme activity has been isolated. We have cloned the CHA1 gene by complementation of a cha1 mutation. Northern analysis showed that CHA1 mRNA has a size of about 1200 ri...
متن کاملL-serine deaminase of Escherichia coli.
The native l-serine deaminase (l-serine hydrolyase, deaminating, EC 4.2.1.13) of Escherichia coli K-12, which seems to be a very labile protein, is rather stable in concentrated solution. Dilution rapidly inactivates it, but in the presence of a saturating concentration of l-serine the molecule is protected from inactivation. It is a very specific enzyme; l-serine is the sole substrate with a K...
متن کاملSerine and threonine catabolism in Saccharomyces cerevisiae: the CHA1 polypeptide is homologous with other serine and threonine dehydratases.
The catabolic L-serine (L-threonine) dehydratase of Saccharomyces cerevisiae allows the yeast to grow on media with L-serine or L-threonine as sole nitrogen source. Previously we have cloned the CHA1 gene by complementation of a mutant, cha1, lacking the dehydratase activity. Here we present the DNA sequence of a 1,766-bp fragment of the CHA1 region encompassing an open reading frame of 1080 bp...
متن کاملIsolation and Properties of a Homogeneous Preparation of Cystathionine Synthetase-l-serine and L-threonine Dehydratase.
Selim and Greenberg (1, 2) achieved a considerable degree of purification of L-serine dehydratase (L-serine hydro-lyase (deaminating), EC 4.2.1.13) from rat liver and demonstrated that this protein preparation contained the cystathionine-synthesizing activity of the liver (L-serine hydro-lyase (adding L-homocysteine), EC 4.2.1.21). These workers (2) also observed activity of their enzyme prepar...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2005
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1982.tb06570.x