1qlu
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STRUCTURE OF THE H422A MUTANT VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH ISOEUGENOL
OverviewOverview
By mutating the target residue of covalent flavinylation in, vanillyl-alcohol oxidase, the functional role of the histidyl-FAD bond was, studied. Three His(422) mutants (H422A, H422T, and H422C) were purified, which all contained tightly but noncovalently bound FAD. Steady state, kinetics revealed that the mutants have retained enzyme activity, although, the turnover rates have decreased by 1 order of magnitude. Stopped-flow, analysis showed that the H422A mutant is still able to form a stable, binary complex of reduced enzyme and a quinone methide product, intermediate, a crucial step during vanillyl-alcohol oxidase-mediated, catalysis. The only significant change in the catalytic cycle of the H422A, mutant is a marked decrease in reduction rate. Redox potentials of both, wild type and ... [(full description)]
About this StructureAbout this Structure
1QLU is a [Single protein] structure of sequence from [Penicillium simplicissimum] with FAD and EUG as [ligands]. Active as [[1]], with EC number [1.1.3.7]. Full crystallographic information is available from [OCA].
ReferenceReference
Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase., Fraaije MW, van den Heuvel RH, van Berkel WJ, Mattevi A, J Biol Chem. 1999 Dec 10;274(50):35514-20. PMID:10585424
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