Activation of Thiamin Diphosphate and FAD in the Phosphatedependent Pyruvate Oxidase fromLactobacillus plantarum

This publication has 14 references indexed in Scilit:

• How Thiamine Diphosphate Is Activated in Enzymes
  Science, 1997
• The Refined Structures of a Stabilized Mutant and of Wild-type Pyruvate Oxidase from Lactobacillus plantarum
  Journal of Molecular Biology, 1994
• Structure of the Thiamine- and Flavin-Dependent Enzyme Pyruvate Oxidase
  Science, 1993
• Stability and reconstitution of pyruvate oxidase from lactobacillus plantarum: Dissection of the stabilizing effects of coenzyme binding and subunit interaction
  Protein Science, 1992
• Absolute stereochemistry of flavins in enzyme-catalyzed reactions
  Biochemistry, 1986
• Irreversible Inactivation of Pyruvate Decarboxylase in the Presence of Substrate and an Oxidant. An Example of Paracatalytic Enzyme Inactivation
  European Journal of Biochemistry, 1979
• Preparation, characterization, and chemical properties of the flavin coenzyme analogues 5-deazariboflavin, 5-deazariboflavin 5'-phosphate, and 5-deazariboflavin 5'-diphosphate, 5' → 5'-adenosine ester
  Biochemistry, 1976
• A spectrophotometric determination of carbanions with tetranitromethane
  Analytica Chimica Acta, 1970
• Oxidation of Biological Thiols:Glutathione-Indophenol Interactions^*
  Biochemistry, 1964
• The Nature of the Flavin Binding in Microsomal Cytochrome b5 Reductase
  Published by Elsevier ,1961