1e8g: Difference between revisions
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Revision as of 16:03, 30 October 2007
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STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL
OverviewOverview
Vanillyl-alcohol oxidase (VAO) is member of a newly recognized, flavoprotein family of structurally related oxidoreductases. The enzyme, contains a covalently linked FAD cofactor. To study the mechanism of, flavinylation we have created a design point mutation (His-61 --> Thr). In, the mutant enzyme the covalent His-C8alpha-flavin linkage is not formed, while the enzyme is still able to bind FAD and perform catalysis. The H61T, mutant displays a similar affinity for FAD and ADP (K(d) = 1.8 and 2.1, microm, respectively) but does not interact with FMN. H61T is about, 10-fold less active with 4-(methoxymethyl)phenol) (k(cat) = 0.24 s(-)(1), K(m) = 40 microm) than the wild-type enzyme. The crystal structures of, both the holo and apo form of H61T are highly similar to the structure of, ... [(full description)]
About this StructureAbout this Structure
1E8G is a [Single protein] structure of sequence from [Penicillium simplicissimum] with FAD and FCR as [ligands]. Active as [Vanillyl-alcohol oxidase], with EC number [1.1.3.38]. Structure known Active Sites: AC1, AC2, AC3 and AC4. Full crystallographic information is available from [OCA].
ReferenceReference
Structural analysis of flavinylation in vanillyl-alcohol oxidase., Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A, J Biol Chem. 2000 Dec 8;275(49):38654-8. PMID:10984479
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