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Thiazolidine-2-carboxylate derivatives formed from glyoxylate and L-cysteine or L-cysteinylglycine as possible physiological substrates for D-aspartate oxidase
Authors:C L Burns  D E Main  D J Buckthal  G A Hamilton
Affiliation:1. Istituto di Chimica Biologica, Universitàdi Bari, 70126 Bari, Italy;2. Centro di Studio sui Mitocondri e Metabolismo Energetico, Universitàdi Bari, 70126 Bari, Italy
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.
Keywords:HEPES  4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid  RBM  rat brain mitochondria  RHM  rat heart mitochondria  RKM  rat kidney mitochondria  RLM  rat liver mitochondria  αGP  L-glycerol-3-phosphate  DHAP  dihydroxyacetonphosphate  MDH  malate dehydrogenase  AAT  aspartate aminotransferase  ASP  aspartate  FUM  fumarate  MAL  malate  OAA  oxaloacetate  PEP  phosphoenolpyruvate  Pi  inorganic phosphate  PYR  pyruvate
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