SERINE AND THREONINE DEAMINASES OF ESCHERICHIA COLI: ACTIVATORS FOR A CELL-FREE ENZYME
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چکیده
منابع مشابه
Serine and threonine desaminaes of Escherichia coli; activators for a cell-free enzyme.
Serine has been reported by many workers to be deaminated by a variety of bacterial cells and tissues, but this process was first studied in detail by Gale and Stephenson in 1938 (1). These workers followed the serine deaminase of Escherichia coli by measuring the release of ammonia by resting cell suspensions. The reaction proceeded anaerobically, thereby distinguishing it from the oxidative d...
متن کاملInduced formation of serine and threonine deaminases by Escherichia coli.
The ability of Escherichia coli to deaminate Dand L-serine (Gale and Stephenson, 1938) and Dand L-threonine (Chargaff and Sprinson, 1943) has been known for some time, and properties of the partly purified enzymes have been determined (Wood and Gunsalus, 1949; Metzler and Snell, 1952). These enzymes catalyze welldefined, easily measured reactions. Upon discovering that the enzymes are inducible...
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Non-enzymatic deamination of serine and cysteine is catalyzed by pyridoxal and certain metal salts at 100” (2). This finding suggested that pyridoxal phosphate might be involved in the enzymatic deamination of these amino acids. Vitamin B, has already been implicated in the desulfhydration of cysteine by rat liver (3) and of cysteine and homocysteine by bacteria (4). Several similarities of cys...
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Studies concerning the identity of the serine and threonine deaminases have been carried out in several laboratories. Wood and Gunsalus (1949) employing a partially purified system extracted from Escherichia coli suggested that both serine and threonine are deaminated by the same enzyme. Similarly, studies with Neurospora indicate that these amino acids are deaminated by one enzyme (Yanofsky, 1...
متن کاملThreonine synthesis from aspartate in Escherichia coli cell-free extracts: pathway dynamics.
We have developed an experimental model of the whole threonine pathway that allows us to study the production of threonine from aspartate under different conditions. The model consisted of a desalted crude extract of Escherichia coli to which we added the substrates and necessary cofactors of the pathway: aspartate, ATP and NADPH. In this experimental model we measured not only the production o...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1949
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)56638-2