spacer CRYSTAL STRUCTURE OF THE SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE IN COMPLEX WITH PQQ
Primary citation
Title Structure and mechanism of soluble quinoprotein glucose dehydrogenase.
Authors Oubrie, A.search; Rozeboom, H.J.search; Kalk, K.H.search; Olsthoorn, A.J.search; Duine, J.A.search; Dijkstra, B.W.search
Journal EMBO J.search vol:18, pag:5187-5194 (1999), Identifiers: PubMed ID (10508152)search DOI (10.1093/emboj/18.19.5187)
Abstract Soluble glucose dehydrogenase (s-GDH; EC 1.1.99.17) is a classical quinoprotein which requires the cofactor pyrroloquinoline quinone (PQQ) to oxidize glucose to gluconolactone. The reaction mechanism of PQQ-dependent enzymes has remained controversial due to the absence of comprehensive structural data. We have determined the X-ray structure of s-GDH with the cofactor at 2.2 A resolution, and of a complex with reduced PQQ and glucose at 1.9 A resolution. These structures reveal the active site of s-GDH, and show for the first time how a functionally bound substrate interacts with the cofactor in a PQQ-dependent enzyme. Twenty years after the discovery of PQQ, our results finally provide conclusive evidence for a reaction mechanism comprising general base-catalyzed hydride transfer, rather than the generally accepted covalent addition-elimination mechanism. Thus, PQQ-dependent enzymes use a mechanism similar to that of nicotinamide- and flavin-dependent oxidoreductases.
MeSH terms Binding Sitessearch, Calciumsearch, Crystallographysearch, X-Raysearch, Glucosesearch, Glucose Dehydrogenasessearch, Modelssearch, Molecularsearch, Oxidation-Reductionsearch, Protein Conformationsearch, Recombinant Proteinssearch, Solubilitysearch
Other entries described in this publication 1cq1
Secondary citations
Title The 1.7 Angstrom crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal sequence repeat
Authors Oubrie, A.search; Rozeboom, H.J.search; Kalk, K.H.search; Duine, J.A.search; Dijkstra, B.W.search
Journal J.MOL.BIOL.search vol:289, pag:319-333 (1999) DOI (10.1006/jmbi.1999.2766)
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