Subunit structure, function and organisation of pyruvate decarboxylases from various organisms.
The nature of the environment of macromolecules influences and determines the state of their overall structure and the extent of binding of specific (cofactors, substrates) or unspecific ligands. How these interactions between enzyme molecules and ligands influence their quaternary structures and, in this way, the realisation of high catalytic activity will be discussed here for the enzyme pyruvate decarboxylase from various organisms: brewer's yeast, brewer's yeast strain, recombinant wild type and site-specific mutants of Saccharomyces cerevisiae, the recombinant wild type of the bacterium Zymomonas mobilis and germinating seeds of the plant Pisum sativum from a structural point of view including both high resolution models from crystal structure analysis and low resolution models from small angle X-ray solution scattering with synchrotron radiation.
König
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Institut für Biochemie, Fachbereich Biochemie/Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, D-06099 Halle/Saale, Germany.
D046911:Macromolecular Substances; D008958:Models, Molecular; D018532:Pisum sativum / Q000201:enzymology*; D011487:Protein Conformation; D011767:Pyruvate Decarboxylase / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D012440:Saccharomyces / Q000201:enzymology*; D017355:Zymomonas / Q000201:enzymology*
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D011767:Pyruvate Decarboxylase