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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.
Oxidative deamination is a form of deamination that generates α-keto acids and other oxidized products from amine-containing compounds, and occurs primarily in the liver. [1] Oxidative deamination is stereospecific, meaning it contains different stereoisomers as reactants and products; this process is either catalyzed by L or D- amino acid ...
The net chemical change is the addition of a water group and removal of an ammonia group, which corresponds to a +1 (0.98402) Da mass increase. Although deamidation occurs on glutamine, glycosylated asparagine and other amides, these are negligible under typical proteolysis conditions. [1]
Catabolism, therefore, provides the chemical energy necessary for the maintenance and growth of cells. Examples of catabolic processes include glycolysis , the citric acid cycle , the breakdown of muscle protein in order to use amino acids as substrates for gluconeogenesis , the breakdown of fat in adipose tissue to fatty acids , and oxidative ...
Norepinephrine degradation. Monoamine oxidase is shown left in the blue box. [11]Monoamine oxidases catalyze the oxidative deamination of monoamines. In the first part of the reaction, cofactor FAD oxidizes the substrate yielding the corresponding imine which converts the cofactor into its reduced form FADH2.
In organic chemistry, keto acids or ketoacids (also called oxo acids or oxoacids) are organic compounds that contain a carboxylic acid group (−COOH) and a ketone group (>C=O). [1] In several cases, the keto group is hydrated. The alpha-keto acids are especially important in biology as they are involved in the Krebs citric acid cycle and in ...
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).
SDH catalyzes the deamination of L-serine to yield pyruvate, with the release of ammonia. [1] This enzyme has one substrate, L-serine, and two products, pyruvate and NH 3, and uses one cofactor, pyridoxal phosphate (PLP). The enzyme's main role is in gluconeogenesis in the liver's cytoplasm. [citation needed]