Literature DB >> 6151397

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

C L Burns, D E Main, D J Buckthal, G A Hamilton.   

Abstract

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.

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Year:  1984        PMID: 6151397     DOI: 10.1016/0006-291x(84)91388-3

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Formation of the L-cysteine-glyoxylate adduct is the mechanism by which L-cysteine decreases oxalate production from glycollate in rat hepatocytes.

Authors:  P W Baker; R Bais; A M Rofe
Journal:  Biochem J       Date:  1994-09-15       Impact factor: 3.857

2.  D-aspartate regulates melanocortin formation and function: behavioral alterations in D-aspartate oxidase-deficient mice.

Authors:  Alex S Huang; Anne Beigneux; Zachary M Weil; Paul M Kim; Mark E Molliver; Seth Blackshaw; Randy J Nelson; Stephen G Young; Solomon H Snyder
Journal:  J Neurosci       Date:  2006-03-08       Impact factor: 6.167

  2 in total

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