methionine adenosyltransferase


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me·thi·o·nine a·den·o·syl·trans·fer·ase

an enzyme catalyzing the condensation of l-methionine and ATP, forming S-adenosyl-l-methionine, orthophosphate, and pyrophosphate; a deficiency of the hepatic enzyme will result in hypermethionemia.
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1,2) It is formed in vivo from the reaction of the amino acid methionine and adenosine triphosphate (ATP), catalyzed by the enzyme methionine adenosyltransferase.
In the first two sections, biochemists, gastroenterologists, and other specialists from the US, Israel, and Europe discuss fatty liver vulnerability to hypoxic and inflammatory stress, hepatocellular carcinoma, cellular stress responses in the regulation of drug-induced liver steatosis, the role of the Keapl/Nrf2 pathway, the role of methionine adenosyltransferase genes in liver health and disease, the role and modulation of nitric oxide in the cirrhotic liver, and the role of mitochondria in alcoholic and nonalcoholic fatty liver disease.
Distal motor axonopathy and central nervous system myelin vacuolation caused by cycloleucine, an inhibitor of methionine adenosyltransferase.
Methionine, in turn, is an essential amino acid that, together with ATP, participates in the formation of SAMe, in a reaction catalyzed by methionine adenosyltransferase (MAT).
Between the two isoforms of methionine adenosyltransferase, MAT-I is inhibited and MET-III is activated by its product, AdoMet ([9]; [10]).
Methionine can also be increased in methionine adenosyltransferase I/III deficiency, S-adenosylmethionine hydrolase deficiency, glycine N-methyltransferase deficiency, generalized liver disease, and infants fed a formula rich in methionine.
One enzyme class in particular, the methionine adenosyltransferases (MAT), in 1983 was found to be reduced in the blood cells of depressed patients, yet elevated in patients in the manic phase.