منابع مشابه
Ox liver glutamate dehydrogenase
1. The effect of pyridoxal 5'-phosphate on the activity of ox liver glutamate dehydrogenase towards different amino acid substrates was investigated. 2. Both alanine and glutamate activities decreased steadily in the presence of pyridoxal 5'phosphate. 3. The alanine/glutamate activity ratio increased as a function of inactivation by pyridoxal 5'-phosphate, indicating that glutamate activity is ...
متن کاملRegulation of Bovine Glutamate Dehydrogenase
The activity of bovine liver glutamate dehydrogenase is affected in several ways depending on substrate concentrations and pH. At pH 6.5 and below, both oxidative deamination and reductive amination reactions are inhibited by ADP. At pH 7.0 and above both activatory and inhibitory effects can be observed depending on substrate concentrations. The effects are explicable in terms of a model with ...
متن کاملProduction 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...
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...
متن کاملThe Molecular Weight of the Polypeptide Chains of L-glutamate Dehydrogenase.
L-Glutamate dehyd.rogenase, originally reported as having a molecular weight of about l,OOO,OOO (I), is known to be readily dissociated into subunits of smaller size (l-3). The size of the ultimate subunits, the individual polypeptide chains, has, however, not been definitely established. Jirgensons (4) reported finding about 20 moles of NHz-terminal acid per lo6 g of enzyme, suggesting a molec...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1965
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)97635-0