Results 251 to 260 of about 60,211 (294)

Potential inhibitors of S-adenosylmethionine-dependent methyltransferases. 6. Structural modifications of S-adenosylmethionine

Journal of Medicinal Chemistry, 1976
Structural analogues of S-adenosyl-L-methionine (SAM), with modifications in the amino acid, sugar, or base portions of the molecule, have been synthesized and evaluated as either inhibitors and/or substrates for the enzymes catechol O-methyltransferase, phenylethanolamine N-methyltransferase, histamine N-methyltransferase, and hydroxyindole O ...
R T, Borchardt, Y, Shiong, J A, Huber, A F, Wycpalek   +3 more
openaire   +2 more sources

On Lowering S-Adenosylmethionine

1978
L-Dopa produces a marked lowering of brain S-adenosylmethionine (8), but nicotinamide, although also a methyl group acceptor, does not (3). It would be interesting to have a theoretical explanation for this difference in activity, especially if it would help in the selection of new agents which might have S-adenosylmethionine lowering activity.
openaire   +2 more sources

SAMe: S-Adenosylmethionine

American Journal of Health-System Pharmacy, 2000
J C, Echols, U, Naidoo, C, Salzman
  +6 more sources

Assay for S-adenosylmethionine: Methionine methyltransferase

Analytical Biochemistry, 1973
Abstract A quantitative assay for S-adenosylmethionine: methionine methyltransferase in phosphate buffer extracts has been developed. This enzyme catalyzes the biosynthesis of S-methylmethionine from methionine and S-adenosylmethionine. The radioactively labeled product, S-methylmethionine, is first separated from the radioactively labeled substrate,
B D, Allamong, L, Abrahamson
openaire   +2 more sources

S-adenosylmethionine decarboxylase from human placenta

International Journal of Biochemistry, 1977
Abstract 1. 1. S-adenosylmethionine decarboxylase from human placenta has been purified more than 1200-fold by use of Chromatographic techniques. 2. 2. The molecular weight was determined as approx 53,000 by gel nitration. 3. 3. The enzyme preparations were quite unstable in the absence of reducing agents; the crude enzyme was rapidly ...
PORTA, RAFFAELE, C. Esposito, G. Della Pietra   +2 more
openaire   +3 more sources

Inhibition of angiogenesis by S-adenosylmethionine

Biochemical and Biophysical Research Communications, 2011
Metastasis is a leading cause of mortality and morbidity in cancer. One of the steps in metastasis process is the formation of new blood vessels. Aberrant DNA methylation patterns are common in cancer cells. In recent studies, S-adenosylmethionine (SAM), which is a DNA methylating agent, has been found to have inhibitory effects on some carcinoma cells
Mehmet, Sahin, Emel, Sahin, Saadet, Gümüşlü, Abdullah, Erdoğan, Meral, Gültekin   +4 more
openaire   +2 more sources

The synthesis of S-adenosylmethionine by mutants with defects in S-adenosylmethionine synthetase

Molecular and General Genetics MGG, 1976
Some metK mutants of Salmonella typhimurium with constitutive methionine biosynthesis have no detectable S-adenosylmethionine (SAM) synthetase, the enzyme which converts methionine to SAM, the postulated corepressor of the methionine pathway. However, these mutants are not auxotrophic for SAM, an essential compound for many reactions.
openaire   +2 more sources

Quantitation of S-adenosylmethionine decarboxylase protein

Biochemistry, 1985
A method for the specific labeling of the active site of S-adenosylmethionine decarboxylase was developed. The method consisted of incubating cell extracts with 3H-decarboxylated S-adenosylmethionine and sodium cyanoborohydride in the presence of a spermidine synthase inhibitor.
A, Shirahata, K L, Christman, A E, Pegg
openaire   +2 more sources

S-adenosylmethionine: nothing goes to waste

Trends in Biochemical Sciences, 2004
S-adenosylmethionine (SAM or AdoMet) is a biological sulfonium compound known as the major biological methyl donor in reactions catalyzed by methyltransferases. SAM is also used as a source of methylene groups (in the synthesis of cyclopropyl fatty acids), amino groups (in the synthesis of 7,8-diaminoperlagonic acid, a precursor of biotin), ribosyl ...
Marc, Fontecave, Mohamed, Atta, Etienne, Mulliez   +2 more
openaire   +2 more sources

Regulation of mammalian S-Adenosylmethionine decarboxylase

Advances in Enzyme Regulation, 1988
S-Adenosylmethionine decarboxylase is a key enzyme in the biosynthesis of polyamines that is the rate limiting step in the formation of spermidine and spermine. The activity of S-adenosylmethionine decarboxylase is known to be regulated negatively by these polyamines and positively by their precursor, putrescine.
A E, Pegg, T, Kameji, A, Shirahata, B, Stanley, R, Madhubala, A, Pajunen   +5 more
openaire   +2 more sources