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Trends in Biochemical Sciences|March 1, 2000
Flavoenzymes: diverse catalysts with recurrent featuresM W Fraaije, A MatteviFEBS Letters|January 27, 1997
Mercuration of vanillyl-alcohol oxidase from Penicillium simplicissimum generates inactive dimersM W Fraaije, A Mattevi, W J van BerkelProteins|April 1, 1997
Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimumA Mattevi, M W Fraaije, A Coda, et al.The Journal of Biological Chemistry|December 10, 1999
Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidaseM W Fraaije, R H van den Heuvel, W J van Berkel, et al.The Journal of Biological Chemistry|May 16, 2000
Asp-170 is crucial for the redox properties of vanillyl-alcohol oxidaseR H van den Heuvel, M W Fraaije, A Mattevi, et al.The Journal of Biological Chemistry|September 14, 2000
Structural analysis of flavinylation in vanillyl-alcohol oxidaseM W Fraaije, R H van Den Heuvel, W J van Berkel, et al.Structure (London, England : 1993)|July 15, 1997
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificityA Mattevi, M W Fraaije, A Mozzarelli, et al.Proceedings of the National Academy of Sciences of the United States of America|August 2, 2000
Inversion of stereospecificity of vanillyl-alcohol oxidaseR H van Den Heuvel, M W Fraaije, M Ferrer, et al.The Journal of Biological Chemistry|July 18, 1997
Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase. Evidence for formation of a p-quinone methide intermediateM W Fraaije, W J van BerkelPageof 7