cysteinylglycine and thiazolidine-2-carboxylic-acid

cysteinylglycine has been researched along with thiazolidine-2-carboxylic-acid* in 1 studies

Other Studies

1 other study(ies) available for cysteinylglycine and thiazolidine-2-carboxylic-acid

Article	Year
Thiazolidine-2-carboxylate derivatives formed from glyoxylate and L-cysteine or L-cysteinylglycine as possible physiological substrates for D-aspartate oxidase. Biochemical and biophysical research communications, 1984, Dec-28, Volume: 125, Issue:3 Adducts of glyoxylate with L-cysteine or L-cysteinylglycine were found to be excellent substrates at low concentrations for beef kidney D-aspartate oxidase. Evidence is presented that cis-thiazolidine-2,4-dicarboxylate and its glycine amide are the actual substrates, and that both are converted in the enzymic reaction to 4-substituted thiazoline-2-carboxylates. The results imply that these thiazolidine derivatives are the likely physiological reactants for mammalian D-aspartate oxidase. Topics: Amino Acid Oxidoreductases; Animals; Aspartic Acid; Cattle; Cysteine; D-Aspartate Oxidase; Dipeptides; Glutamates; Glutamic Acid; Glyoxylates; Hydrogen-Ion Concentration; Proline; Substrate Specificity; Thiazolidines	1984

Article

Year

Thiazolidine-2-carboxylate derivatives formed from glyoxylate and L-cysteine or L-cysteinylglycine as possible physiological substrates for D-aspartate oxidase.

Biochemical and biophysical research communications, 1984, Dec-28, Volume: 125, Issue:3

Adducts of glyoxylate with L-cysteine or L-cysteinylglycine were found to be excellent substrates at low concentrations for beef kidney D-aspartate oxidase. Evidence is presented that cis-thiazolidine-2,4-dicarboxylate and its glycine amide are the actual substrates, and that both are converted in the enzymic reaction to 4-substituted thiazoline-2-carboxylates. The results imply that these thiazolidine derivatives are the likely physiological reactants for mammalian D-aspartate oxidase.

Topics: Amino Acid Oxidoreductases; Animals; Aspartic Acid; Cattle; Cysteine; D-Aspartate Oxidase; Dipeptides; Glutamates; Glutamic Acid; Glyoxylates; Hydrogen-Ion Concentration; Proline; Substrate Specificity; Thiazolidines

1984