![]() GBF (Gesellschaft für Biotechnologische Forschung), Department of Molecular Structure, Braunschweig, Germany. Kalisz, H.M., Hecht, H.-J., Schomburg, D., Schmid, R.D. Background: the nature of alpha-D-mannose - natural aldohexose sugar, C-2 glucose epimer, whose intended use is for preventing urinary tract infections - in the interaction with E. Effects of Carbohydrate Depletion on the Structure, Stability and Activity of Glucose Oxidase from Aspergillus Niger.The structure and properties of glucose will be considered in greater detail than those of the other monosaccharides, not only because of its. The carbohydrate moiety attached to Asn89 at the tip of this lid forms a link between the subunits of the dimer. Glucose is by far the most abundant monosaccharide it occurs free in fruits, plants, honey, in the blood of animals, and combined in many glycosides, disaccharides, and polysaccharides. Part of the entrance to the active site pocket is at the interface to the second subunit of the dimeric enzyme and is formed by a 20-residue lid, which in addition covers parts of the FAD-binding site. One side of this pocket is formed by a six-stranded antiparallel beta-sheet with the flavin ring system of FAD located at the bottom of the pocket on the opposite side. The substrate-binding domain is formed from non-continuous segments of sequence and is characterized by a deep pocket. The FAD-binding domain is topologically very similar to other FAD-binding proteins. During the redox reaction the cofactor remains tightly bound to Agl3 and participates in the reaction in a concentration-dependent manner. The refined model includes 580 amino acid residues, the FAD cofactor, six N-acetylglucosamine residues, three mannose residues and 152 solvent molecules. In the absence of a sulfur donor, UDP-d-glucose is converted via UDP-4-keto-d-glucose to UDP-d-glucose-5,6-ene, the structure of which was determined by 1H and 13C-NMR spectroscopy. The final crystallographic R-value is 18.1% for reflections between 10.0 and 2.3 A resolution. The crystal structure of the partially deglycosylated enzyme from Aspergillus niger has been determined by isomorphous replacement and refined to 2.3 A resolution. Glucose oxidase (beta-D-glucose: oxygen 1-oxidoreductase, EC 1.1.3.4) is an FAD-dependent enzyme that catalyzes the oxidation of beta-D-glucose by molecular oxygen. Diversity, Equity, Inclusion, and Access. ![]() ![]() ![]() Citation, Usage, Privacy Policies, Logo.Biologically Interesting Molecule Reference Dictionary (BIRD). ![]()
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