Results 251 to 260 of about 213,170 (299)
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Metabolism of Sulfur-Containing Amino Acids

Annual Review of Nutrition, 1986
Met metabolism occurs primarily by activation of Met to AdoMet and further metabolism of AdoMet by either the transmethylation-transsulfuration pathway or the polyamine biosynthetic pathway. The catabolism of the methyl group and sulfur atom of Met ultimately appears to be dependent upon the transmethylation-transsulfuration pathway because the MTA ...
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Disorders of Sulfur Amino Acid Metabolism

2000
Several inherited defects are known in the conversion of the sulfur-containing amino acid methionine to cys teine and the ultimate oxidation of cysteine to inorganic sulfate (Fig. 21.1). Cystathionine β-synthase (CBS) deficiency is the most important.
ANDRIA, GENEROSO, fowler B, Sebastio G.
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Sulfur Amino Acid Metabolism in Hepatobiliary Disorders

Scandinavian Journal of Gastroenterology, 1992
Sulfur amino acid metabolism was studied in patients with mild to severe forms of liver dysfunction and compared with that of healthy controls. Patients with mild liver dysfunction (for example, Gilbert's syndrome) had a normal sulfur amino acid metabolism.
J, Mårtensson   +5 more
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Sulfur Amino Acids

1970
Several sulfur amino acids and sulfur compounds are found in mammalian tissues. While some find their origin in the diet, other sulfur amino acids are formed in vivo from methionine in the tissues. Thus it is known that methionine is converted into homocysteine, cystathionine, cysteine, hypotaurine, and taurine.
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BIOCHEMISTRY OF SULFUR-CONTAINING AMINO ACIDS

Annual Review of Biochemistry, 1983
The literature on sulfur amino acid metabolism is too vast for a short chapter to cover in great depth. I attempt here a brief overview with references to many specialized review articles. This review emphasizes aspects of sulfur amino acid metabolism elucidated in the last ten years, in particular aspects not generally covered in biochemistry texts, e.
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The reactions of the sulfur-containing amino acids with phosphoric and sulfuric acids

Archives of Biochemistry and Biophysics, 1951
Abstract Both cystine and cysteine react very differently toward 6.0 M phosphoric and sulfuric acids. With phosphoric acid, extensive decomposi tion occurs; with sulfuric acid, very little. Cystine, in phosphoric acid at 100 °C. produces hydrogen sulfide, free sulfur, cysteic acid, ammonia, alanine, serine, and pyruvic acid.
J C, ANDREWS, R B, BRUCE
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Microbial sulfur amino acids: An overview

1987
Publisher Summary This chapter presents an overview microbial sulfur amino acids. Various microorganisms assimilate inorganic sulfur to synthesize sulfur amino acids. Hydrogen sulfide, the final product of bacterial sulfate reduction, reacts microbially with serine and homoserine to form cysteine and homocysteine, respectively. Cysteine, homocysteine,
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Methods for measuring sulfur amino acid metabolism

Current Opinion in Clinical Nutrition and Metabolic Care, 2002
The importance of sulfur amino acid metabolism has become increasingly apparent in recent years. Methionine and cysteine are precursors of glutathione, which plays an important role in intracellular antioxidant/free radical defenses. Homocysteine is a non-protein-bound sulfur amino acid strongly implicated in the pathogenesis of several diseases.
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The Oxidation of Sulfur-Containing Amino Acids by L-Amino Acid Oxidases

1982
L-amino acid oxidase (LAO) from various sources is known to act on most of natural and unnatural amino acids of the L configuration (1). Among the sulfur containing amino acids, apart methionine which is known since long time as one of the best substrates for this enzyme, cystine (2), homocystine (3) and thialysine (4) have also been found more ...
D, Cavallini   +6 more
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Disorders of Sulfur Amino Acids

2003
The sulfur amino acids are methionine, homocysteine, cystathionine, cyst(e)ine, and taurine. Defects in several of the enzymatic steps of their metabolism are known; some, but not all, result in human disease. The remethylation of homocysteine to methionine is closely dependent on folate and cobalamin cofactors, and relevant defects of their metabolism
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