Two tyrosine residues, Tyr-108 and Tyr-503, are responsible for the deprotonation of phenolic substrates in vanillyl-alcohol oxidase-Reference-Cited by-同舟云学术

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Two tyrosine residues, Tyr-108 and Tyr-503, are responsible for the deprotonation of phenolic substrates in vanillyl-alcohol oxidase

Published:2017-09 Issue:35 Volume:292 Page:14668-14679
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ewing Tom A.,Nguyen Quoc-Thai,Allan Robert C.,Gygli Gudrun,Romero Elvira,Binda Claudia,Fraaije Marco W.,Mattevi Andrea,van Berkel Willem J.H.

Funder

Seventh Framework Programme

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference35 articles.

1. Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum: a novel aromatic alcohol oxidase containing covalently bound FAD;de Jong;Eur. J. Biochem,1992

2. Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum: evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols;Fraaije;Eur. J. Biochem,1995

3. Regio- and stereospecific conversion of 4-alkylphenols by the covalent flavoprotein vanillyl-alcohol oxidase;van den Heuvel;J. Bacteriol,1998

4. Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity;Mattevi;Structure,1997

5. A novel oxidoreductase family sharing a conserved FAD-binding domain;Fraaije;Trends Biochem. Sci,1998

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