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1e0y

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Revision as of 16:52, 30 March 2008 by OCA (Talk | contribs)
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PDB ID 1e0y

Drag the structure with the mouse to rotate
, resolution 2.75Å
Ligands: ,
Activity: Vanillyl-alcohol oxidase, with EC number 1.1.3.38
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE D170S/T457E DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE


Overview

Vanillyl-alcohol oxidase (VAO) is the prototype of a newly recognized family of structurally related oxidoreductases sharing a conserved FAD-binding domain. The active site of VAO is formed by a cavity where the enzyme is able to catalyze many reactions with phenolic substrates. Among these reactions is the stereospecific hydroxylation of 4-ethylphenol-forming (R)-1-(4'-hydroxyphenyl)ethanol. During this conversion, Asp-170 is probably critical for the hydration of the initially formed p-quinone methide intermediate. By site-directed mutagenesis, the putative active site base has been relocated to the opposite face of the active site cavity. In this way, a change in stereospecificity has been achieved. Like native VAO, the single mutants T457E, D170A, and D170S preferentially converted 4-ethylphenol to the (R)-enantiomer of 1-(4'-hydroxyphenyl)ethanol. The double mutants D170A/T457E and D170S/T457E exhibited an inverted stereospecificity with 4-ethylphenol. Particularly, D170S/T457E was strongly (S)-selective, with an enantiomeric excess of 80%. The crystal structure of D170S/T457E, in complex with trifluoromethylphenol, showed a highly conserved mode of ligand binding and revealed that the distinctive catalytic properties of this mutant are not caused by major structural changes.

About this Structure

1E0Y is a Single protein structure of sequence from Penicillium simplicissimum. Full crystallographic information is available from OCA.

Reference

Inversion of stereospecificity of vanillyl-alcohol oxidase., van Den Heuvel RH, Fraaije MW, Ferrer M, Mattevi A, van Berkel WJ, Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9455-60. PMID:10920192

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