Subcellular localization of vanillyl-alcohol oxidase inPenicillium simplicissimum
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(97)01605-0/fullpdf
Reference39 articles.
1. Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum. A novel aromatic alcohol oxidase containing covalently bound FAD
2. Substrate Specificity of Flavin-Dependent Vanillyl-Alcohol Oxidase from Penicillium Simplicissimum. Evidence for the Production of 4-Hydroxycinnamyl Alcohols from 4-Allylphenols
3. Enigmatic Gratuitous Induction of the Covalent Flavoprotein Vanillyl-Alcohol Oxidase in Penicillium simplicissimum
4. Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity
5. Biosynthesis and Function of Enzymes with Covalently Bound Flavin
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1. Vanillyl alcohol oxidase from Diplodia corticola: Residues Ala420 and Glu466 allow for efficient catalysis of syringyl derivatives;Journal of Biological Chemistry;2023-07
2. Vanillyl alcohol oxidase;Flavin-Dependent Enzymes: Mechanisms, Structures and Applications;2020
3. On the origin of vanillyl alcohol oxidases;Fungal Genetics and Biology;2018-07
4. A single loop is essential for the octamerization of vanillyl alcohol oxidase;The FEBS Journal;2016-06-13
5. Kinetic Isotope Effects on the Noncovalent Flavin Mutant Protein of Pyranose 2-Oxidase Reveal Insights into the Flavin Reduction Mechanism;Biochemistry;2010-04-09
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