Search results
Results from the WOW.Com Content Network
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 stereospecific, meaning it contains different stereoisomers as reactants and products; this process is either catalyzed by L or D- amino acid oxidase and L-amino acid oxidase is present only in the liver and kidney. [2] Oxidative deamination is an important step in the catabolism of amino acids, generating a more ...
Monoamine oxidases (MAO) (EC 1.4.3.4) are a family of enzymes that catalyze the oxidation of monoamines, employing oxygen to clip off their amine group. [1] [2] They are found bound to the outer membrane of mitochondria in most cell types of the body. The first such enzyme was discovered in 1928 by Mary Bernheim in the liver and was named ...
Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or (serum) glutamic oxaloacetic transaminase (GOT, SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1) that was first described by Arthur Karmen and colleagues in 1954.
In a similar vein, this enzyme performs in a myriad of biological activities including apoptosis-induction, edema-induction, hemorrhaging, and inhibition or induction of platelet aggregation. [3] As suggested by the name of the family, LAAOs are flavoenzymes which function to catalyze the stereospecific oxidative deamination of an L-amino acid. [4]
Oxidative deamination is the first step to breaking down the amino acids so that they can be converted to sugars. The process begins by removing the amino group of the amino acids. The amino group becomes ammonium as it is lost and later undergoes the urea cycle to become urea, in the liver. It is then released into the blood stream, where it ...
FMO3 is the main flavin-containing monooxygenase isoenzyme that is expressed in the liver of adult humans. [ 8 ] [ 9 ] [ 10 ] The human FMO3 enzyme catalyzes several types of reactions, including: the N -oxygenation of primary, secondary, and tertiary amines ; [ 9 ] [ 11 ] the S -oxygenation of nucleophilic sulfur -containing compounds; [ 9 ...
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]