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Transamination is a chemical reaction that transfers an amino group to a ketoacid to form new amino acids.This pathway is responsible for the deamination of most amino acids. This is one of the major degradation pathways which convert essential amino acids to non-essential amino acids (amino acids that can be synthesized de novo by the organism).
Tissue transaminase activities can be investigated by incubating a homogenate with various amino/keto acid pairs. Transamination is demonstrated if the corresponding new amino acid and keto acid are formed, as revealed by paper chromatography. Reversibility is demonstrated by using the complementary keto/amino acid pair as starting reactants.
The amino acids that are produced by protein catabolism can then be further catabolized in amino acid catabolism. Among the several degradative processes for amino acids are Deamination (removal of an amino group), transamination (transfer of amino group), decarboxylation (removal of carboxyl group), and dehydrogenation (removal of hydrogen ...
Because skeletal muscle is unable to utilize the urea cycle to safely dispose of ammonium ions generated in the breakdown of branch chain amino acids, it must get rid of it in a different way. To do so, the ammonium is combined with free α-ketoglutarate via a transamination reaction in the cell, yielding glutamate and α-keto acid.
Amino acid biosynthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids ...
Deamination is the removal of an amino group from a molecule. [1] Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy.
In biochemistry, dehydrogenase enzymes can catalyze the reductive amination of α-keto acids and ammonia to yield α-amino acids. Reductive amination is predominantly used for the synthesis of the amino acid glutamate starting from α-ketoglutarate, while biochemistry largely relies on transamination to introduce nitrogen in the other amino ...
In enzymology, a D-amino-acid transaminase (EC 2.6.1.21) is an enzyme that catalyzes the chemical reaction: D-alanine + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } pyruvate + D-glutamate Thus, the two substrates of this enzyme are D-alanine and 2-oxoglutarate , whereas its two products are pyruvate and D- glutamate .