TAILIEUCHUNG - báo cáo khoa hoc : Catalytically active filaments – pyruvate decarboxylase from Neurospora crassa. pH-controlled oligomer structure and catalytic function

Pyruvate decarboxylase is a key enzyme in organisms whose energy metab-olism is based on alcoholic fermentation. The enzyme catalyses the nonoxi-dative decarboxylation of 2-oxo acids in the presence of the cofactors thiamine diphosphate and magnesium ions. | IFEBS Journal Catalytically active filaments - pyruvate decarboxylase from Neurospora crassa. pH-controlled oligomer structure and catalytic function o ftf o nip Hl ittl 1 liilisn Ciol-iifi1 o ftff ft f I ft I 1 Ỷ ft I fl l-liJi icp2 Noi Lp I ilio3 Q n i n ka1 Steianie nutti JUliaiie Iieuig Steiien KUttei I GCIU naUoc naUke Lille iviiuHaci spiiika and Stephan Konig1 1 Division of Enzymology Institute of Biochemistry Biotechnology Martin-Luther-University Halle-Wittenberg Halle Saale Germany 2 Microscopy Unit Biocenter of the Martin-Luther-University Halle-Wittenberg Halle Saale Germany 3 Division of Technical Biochemistry Institute of Biochemistry Biotechnology Martin-Luther-University Halle-Wittenberg Halle Saale Germany Keywords analyticalultracentrifugation kinetics smallangle X-ray solution scattering stoppedflow transmission electron microscopy Correspondence S. Konig Abteilung Enzymologie Institut fur Biochemie Biotechnologie Martin-Luther-Universitat Halle-Wittenberg Kurt-Mothes-Str. 3 06120 Halle Saale Germany Fax 49 345 55 24829 Tel 49 345 55 27014 E-mail . Present addresses Division of Molecular Plant Physiology and Biophysics Botany I Julius-von-Sachs-Insti-tute of BiologicalSciences Julius-Maximil-ian-University Wurzburg Wurzburg Germany fKern Laboratory Howard Hughes Medical Institute and Department of Biochemistry Brandeis University Waltham MA USA Pyruvate decarboxylase is a key enzyme in organisms whose energy metabolism is based on alcoholic fermentation. The enzyme catalyses the nonoxidative decarboxylation of 2-oxo acids in the presence of the cofactors thiamine diphosphate and magnesium ions. Pyruvate decarboxylase species from yeasts and plant seeds studied to date are allosterically activated by their substrate pyruvate. However detailed kinetic studies on the enzyme from Neurospora crassa demonstrate for the first time the lack of substrate activation for a yeast pyruvate decarboxylase species. The .

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