S-adenosylmethionine synthesis: molecular mechanisms and clinical implications
JM Mato, L Alvarez, P Ortiz, MA Pajares - Pharmacology & therapeutics, 1997 - Elsevier
JM Mato, L Alvarez, P Ortiz, MA Pajares
Pharmacology & therapeutics, 1997•ElsevierMethionine adenosyltransferase (MAT) is an ubiquitous enzyme that catalyzes the synthesis
of S-adenosylmethionine from methionine and ATP. In mammals, there are two genes
coding for MAT, one expressed exclusively in the liver and a second enzyme present in all
tissues. Molecular studies indicate that liver MAT exists in two forms: as a homodimer and as
a homotetramer of the same oligomeric subunit. The liver-specific isoenzymes are inhibited
in human liver cirrhosis, and this is the cause of the abnormal metabolism of methionine in …
of S-adenosylmethionine from methionine and ATP. In mammals, there are two genes
coding for MAT, one expressed exclusively in the liver and a second enzyme present in all
tissues. Molecular studies indicate that liver MAT exists in two forms: as a homodimer and as
a homotetramer of the same oligomeric subunit. The liver-specific isoenzymes are inhibited
in human liver cirrhosis, and this is the cause of the abnormal metabolism of methionine in …
Methionine adenosyltransferase (MAT) is an ubiquitous enzyme that catalyzes the synthesis of S-adenosylmethionine from methionine and ATP. In mammals, there are two genes coding for MAT, one expressed exclusively in the liver and a second enzyme present in all tissues. Molecular studies indicate that liver MAT exists in two forms: as a homodimer and as a homotetramer of the same oligomeric subunit. The liver-specific isoenzymes are inhibited in human liver cirrhosis, and this is the cause of the abnormal metabolism of methionine in these subjects.
Elsevier