Active Site and Loop 4 Movements within Human Glycolate Oxidase: Implications for Substrate Specificity and Drug Design

Human glycolate oxidase (GO) catalyzes the FMN-dependent oxidation of glycolate to glyoxylate and glyoxylate to oxalate, a key metabolite in kidney stone formation. We report herein the structures of recombinant GO complexed with sulfate, glyoxylate, and an inhibitor, 4-carboxy-5-dodecylsulfanyl-1,2...

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Veröffentlicht in:	Biochemistry (Easton) 2008-02, Vol.47 (8), p.2439-2449
Hauptverfasser:	Murray, Michael S, Holmes, Ross P, Lowther, W. Todd
Format:	Artikel
Sprache:	eng
Schlagworte:	Alcohol Oxidoreductases - antagonists & inhibitors Alcohol Oxidoreductases - chemistry Alcohol Oxidoreductases - genetics Alcohol Oxidoreductases - metabolism Binding Sites - genetics Crystallography, X-Ray Drug Design Enzyme Inhibitors - chemistry Enzyme Inhibitors - metabolism Glyoxylates - chemistry Glyoxylates - metabolism Humans Models, Biological Models, Molecular Movement Mutagenesis, Site-Directed Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins - chemistry Recombinant Proteins - metabolism Substrate Specificity Sulfates - chemistry Sulfates - metabolism
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