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Papers In Press, published online ahead of print September 9, 2005
J. Biol. Chem, 10.1074/jbc.M506078200
Submitted on June 3, 2005
Revised on September 7, 2005
Accepted on September 9, 2005
-N1-histidyl FAD
Department of Life Science, National Yang-Ming University, Taipei 11221
Corresponding Author: shliaw{at}ym.edu.tw
Glucooligosaccharide oxidase from Acremonium strictum has been screened for potential applications in oligosaccharide acid production and alternative carbohydrate detection, because it catalyzes the oxidation of glucose, maltose, lactose, cellobiose and cello- and malto-oligosaccharides. We report the crystal structures of the enzyme and of its complex with an inhibitor, 5-amino-5-deoxy-cellobiono-1,5-lactam at 1.55-Å and 1.98-Å resolution, respectively. Unexpectedly, the protein structure demonstrates the first known double attachment flavinylation, 6-S-cysteinyl, 8
-N1-histidyl FAD. The FAD cofactor is cross-linked to the enzyme via the C6 atom and the 8 -methyl group of the isoalloxazine ring with Cys130 and His70, respectively. This sugar oxidase possesses an open carbohydrate-binding groove, allowing the accommodation of higher oligosaccharides. The complex structure suggests that this enzyme may prefer a 
-D-glucosyl residue at the reducing end with the conserved Tyr429 acting as a general base to abstract the OH1 proton in concert with the H1 hydride transfer to the flavin N5. Finally, a detailed comparison illustrates the structural conservation as well as the divergence between this protein and its related flavoenzymes.
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