Understanding molecular recognition of promiscuity of thermophilic methionine adenosyltransferase sMAT fromSulfolobus solfataricus
نویسندگان
چکیده
منابع مشابه
Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency.
Methionine adenosyltransferase (MAT) is a key enzyme in transmethylation, transsulfuration, and the biosynthesis of polyamines. Genetic deficiency of alpha/beta-MAT causes isolated persistent hypermethioninemia and, in some cases, unusual breath odor or neural demyelination. However, the molecular mechanism(s) underlying this deficiency has not been clearly defined. In this study, we characteri...
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Insights into the three-dimensional (3D) structure of the enzyme, Methionine S-adenosyltransferase (MAT). can throw light on its role in humans and help in evolving se lectivity attributes of inhibitors targeted at bacterial MAT. We report here a 30model of human MAT, using the X-ray structure of MAT from the rat as a template, by comparative protein modeling principles. The resulting model has...
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Hepatocellular carcinoma (HCC) is the most common primary malignant tumor of the liver. Detection of HCC can be difficult, as most of the patients who develop this tumor have no symptoms other than those related to their longstanding liver disease. There is an urgent need to understand the molecular mechanisms that are responsible for the development of this disease so that appropriate therapie...
متن کاملHighly conserved Methionine Adenosyltransferase (MAT) isoenzymes
It has been shown that changes of intracellular levels of S-adenosylmethionine (SAM) are related to the well beings of cells and organisms. The fluctuation of SAM level is cause by imbalance between SAM synthesis and metabolic pathways (methylation, transsulfuration and aminiopropylation) or degradation. S-adenosylmethionine biosynthesis is strictly and solely dependent on the activity of Methi...
متن کاملInteraction of liver methionine adenosyltransferase with hydroxyl radical.
Liver methionine adenosyltransferase (MAT) plays a critical role in the metabolism of methionine converting this amino acid, in the presence of ATP, into S-adenosylmethionine. Here we report that hydrogen peroxide (H2O2), via generation of hydroxyl radical, inactivates liver MAT by reversibly and covalently oxidizing an enzyme site. In vitro studies using pure liver recombinant enzyme and mutan...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2014
ISSN: 1742-464X
DOI: 10.1111/febs.12784