Lack of variation in S-adenosyl L-homocysteine hydrolase(SAHH) phenotype among Japanese.
نویسندگان
چکیده
منابع مشابه
cDNA for S-adenosyl-L-homocysteine hydrolase from Catharanthus roseus.
The majority of the Met synthesized in plants is utilized for methylations performed with S-adenosyl-L-Met. These reactions play a major role in the modification of a large variety of acceptor molecules, such as lipids, polysaccharides, nucleic acids, proteins, and secondary plant products (reviewed by Giovanelli, 1987). The hydrolysis of SAH to adenosine and L-homocysteine by SAH hydrolase is ...
متن کاملInhibition of S-adenosyl-L-homocysteine hydrolase induces immunosuppression.
Lymphocytes depend on transmethylation reactions for efficient activation and function. These reactions are primarily catalyzed by S-adenosylmethionine-dependent methyltransferases, which convert S-adenosylmethionine to S-adenosyl-L-homocysteine. S-adenosyl-L-homocysteine is then hydrolyzed by S-adenosyl-L-homocysteine hydrolase to prevent feedback inhibition of transmethylation reactions. By i...
متن کاملS-Inosyl-L-Homocysteine Hydrolase, a Novel Enzyme Involved in S-Adenosyl-L-Methionine Recycling.
UNLABELLED S-Adenosyl-L-homocysteine, the product of S-adenosyl-L-methionine (SAM) methyltransferases, is known to be a strong feedback inhibitor of these enzymes. A hydrolase specific for S-adenosyl-L-homocysteine produces L-homocysteine, which is remethylated to methionine and can be used to regenerate SAM. Here, we show that the annotated S-adenosyl-L-homocysteine hydrolase in Methanocaldoco...
متن کاملOxidative deamination of S-adenosyl-L-homocysteine by rat kidney L-amino acid oxidase.
Cell-free extracts prepared from rat kidney or liver catalyzed the oxidative deamination of S-adenosyl-Lhomocysteine to S-adenosyl-y-thio-a-ketobutyrate. This reaction was found to be catalyzed by L-amino acid oxidase (L-amino acid:oxygen oxidoreductase (deaminating), EC 1.4.3.2). In the presence of catalase, 0.48 pmole of oxygen was consumed for each micromole of substrate oxidized, and 1 pmol...
متن کاملAre L-adenosine and its derivatives substrates for S-adenosyl-L-homocysteine hydrolase?
Moffatt oxidation of 2',3'-O-isopropylidene-L-adenosine and treatment of the resulting crude 5'-aldehyde with hydroxylamine followed by deprotection gave L-adenosine 5'-carboxaldehyde oximes, whose enantiomers are known to be potent inhibitors of S-adenosyl-L-homocysteine (AdoHcy) hydrolase. The L-adenosine and its 5'-aldehyde oxime derivatives were found to be inactive as inhibitors of AdoHcy ...
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ژورنال
عنوان ژورنال: Journal of the Anthropological Society of Nippon
سال: 1990
ISSN: 0003-5505,1884-765X
DOI: 10.1537/ase1911.98.353