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THE CHEMISTRY OF AMINO-ACID DEAMINATION. In alkaline solution, and in presence of carbon compounds, ammonia readily undergoes oxidation, as emphasised by the extensive investigations of Fosse. [1919, 1920, 1921, 1922]. This difficulty of accounting for the production of ammonia by oxidation has already been
Deamination. Deamination means the removal of amino group from -amino acid in the form of ammonia with formation of -keto acid. The liver and kidney are the main sites for deamination. Deamination may be oxidative or non-oxidative. A. Oxidative deamination. It is catalyzed by one of the following enzymes: 1. L-amino
The oxidative deamination of pyridoxamine to yield pyridoxal and "3, and of many a-amino acids to yield the corre- sponding or-keto acids and ammonia, is catalyzed in dilute aqueous solutions by pyridoxal and appropriate metal ions. 5-Desoxypyridoxal and 4-nitrosalicylaldehyde replace pyridoxal effectively,
a process of oxidative deamination. The results of these studies thus support the older views of Neubauer (8) and Knoop (9). It is an interesting fact, however, that although the animal organism, as a whole, is concerned chiefly with the metabolism of the naturally occurring amino acids of the 1 series,' the in- dividual tissues
Oxidative deamination is a form of deamination that generates ?-keto acids and other oxidized products from amine-containing compounds, and occurs largely in the liver and kidney. Oxidative deamination is an important step in the catabolism of amino acids, generating a more metabolizable form of the amino acid, and
cofactor and is allosterically regulated by GTP and ADP. The combined action of the aminotransferases and GD is referred to as transdeamination. A few amino acids bypass the transdeamination pathway and undergo direct oxidative deamination. Glutamate dehydrogenase (Mr 330,000) is a complex allosteric enzyme and
Oxidative deamination (20.2b):. The transamination steps do not result in any NET deamination. GLUTAMATE is oxidatively deaminated by. GLUTAMATE DEHYDROGENASE, yielding NH. 3 and regenerating ?-ketoglutarate (p. 619):
The degradation of amino acids usually begins with deamination. However, transamination or oxidative deamination is not the first reaction in catabolism of eight amino acids: Serine and threonine are deaminated by dehydration, and histidine undergoes deamination by desaturation. (both reactions were mentioned
OXIDATIVE DEAMINATION. It is the liberation of free ammonia from the amino group of amino acids coupled with oxidation. Takes place mostly in liver and kidney. L-Amino acid Oxidase. L-Amino acid ?-Keto acid + NH. 3. FMN. FMNH2. H2O2. ? O2. Catalase. NON-OXIDATIVE DEAMINATION – Some aa can be
OXIDATIVE DEAMINATION OF D-HOMOCYSTEINESULFINIC. ACID. C. De MARCO and A. RINALDI. Department of Biochemistry, University of Cagliari, 09100 Caligari, Italy. Received 2 April 1971. 1. Introduction. Homocysteinesulfinic acid (HCS) has been prepared by Jolles-Bergeret [l] , who also demonstrated that it.

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February 2018