tailieunhanh - Báo cáo khoa học: New insights into structure–function relationships of oxalyl CoA decarboxylase fromEscherichia coli

The geneyfdUfrom Escherichia coliencodes a putative oxalyl coenzyme A decarboxylase, a thiamine diphosphate-dependent enzyme that is potentially involved in the degradation of oxalate. The enzyme has been purified to homogeneity. The kinetic constants for conversion of the substrate oxalyl coenzyme A by the enzyme in the absence and presence of the inhibitor coenzyme A | New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli Tobias Werther1 Agnes Zimmer1 1 Georg Wille2 Ralph Golbik1 Manfred S. Weiss3 and Stephan Konig1 1 Department of Enzymology Institute of Biochemistry Biotechnology Faculty for BiologicalSciences Martin Luther University Halle-Wittenberg Halle Germany 2 Institute of Biophysics Johann Wolfgang Goethe University Frankfurt am Main Germany 3 Macromolecular Crystallography BESSY-MX Electron Storage Ring BESSY II Helmholtz Zentrum Berlin fur Materialien und Energie Albert Einstein StraBe 15 Berlin Germany Keywords ADP activation crystal structure oxalate degradation thiamine diphosphate X-ray scattering Correspondence S. Konig Institute of Biochemistry Biotechnology Martin Luther University Halle-Wittenberg Kurt Mothes StraBe 3 06120 Halle Saale Germany Fax 49 345 5527014 Tel 49 345 5524829 E-mail . Website http . enzymologie Present address Humboldt University Berlin Institute of Biology Research Group StructuralBiology Biochemistry Germany Research Group Macromolecular Interactions Division of StructuralBiology Helmholtz Centre for Infections Research Braunschweig Germany Database Structuraldata for holo-EcODC ThDP-EcODC in the absence of additional ligands and in complex with either ADP or acetyl CoA have been submitted to the Protein Data Bank under the accession numbers 2q27 2q28 and 2q29 respectively. Received 28 January 2010 revised 26 March 2010 accepted 8 April 2010 doi The gene yfdU from Escherichia coll encodes a putative oxalyl coenzyme A decarboxylase a thiamine diphosphate-dependent enzyme that is potentially involved in the degradation of oxalate. The enzyme has been purified to homogeneity. The kinetic constants for conversion of the substrate oxalyl coenzyme A by the enzyme in the absence and presence of the inhibitor coenzyme A as well as in the absence and