Imidazolylacetolphosphate: l-Glutamate Aminotransferase
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چکیده
منابع مشابه
Production of D-Glutamate from L-Glutamate with Glutamate Racemase and L-Glutamate Oxidase.
We studied production of D-glutamate from L-glutamate using a bioreactor consisting of two columns of sequentially connected immobilized glutamate racemase (EC 5.1.1.3, from Bacillus subtilis IFO 3336) and L-glutamate oxidase (EC 1.4.3.11, from Streptomyces sp. X119-6): L-glutamate was racemized by the glutamate racemase column, and then L-glutamate was oxidized by the L-glutamate oxidase colum...
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delta-Aminolevulinic acid (ALA), the first committed precursor of porphyrin biosynthesis, is formed in Escherichia coli by the C5 pathway in a three-step, tRNA-dependent transformation from glutamate. The first two enzymes of this pathway, glutamyl-tRNA synthetase and Glu-tRNA reductase, are known in E. coli (J. Lapointe and D. Söll, J. Biol. Chem. 247:4966-4974, 1972; D. Jahn, U. Michelsen, an...
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Aminotransferases and glutamate dehydrogenase are two main types of enzymes involved in the initial steps of amino acid catabolism, which plays a key role in the cheese flavor development. In the present work, glutamate dehydrogenase and aminotransferase activities were screened in twenty one strains of lactic acid bacteria of dairy interest, either cheese-isolated or commercial starters, inclu...
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In the title compound, CH(6)N(3) (+)·C(5)H(8)NO(4) (-), there are two independent cations and two independent anions in the asymmetric unit. In the crystal structure, cations and anions are linked by inter-molecular N-H⋯O hydrogen bonds into a three-dimensional network.
متن کاملProteolytic release of a histidinol dehydrogenase fragment from the double enzyme histidinol dehydrogenase-imidazolylacetol-phosphate: L-glutamate aminotransferase.
A double enzyme of Salmonella typhimuriwn, containing histidinol dehydrogenase and imidazolylacetolphosphate:~glutamate aminotransferase, was mildly proteolyzed in an attempt to release these activities from covalent linkage. This treatment releases an active histidinol dehydrogenase fragment larger than normal histidinol dehydrogenase, while completely destroying aminotransferase activity. The...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1967
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96160-0