scholarly journals A kaleidoscopic look at vanillyl alcohol oxidase

2018 ◽  
Author(s):  
Gudrun Gygli
Keyword(s):  
Alcohol Oxidase ◽  
Vanillyl Alcohol ◽  
Vanillyl Alcohol Oxidase

scholarly journals Multigram Scale Enzymatic Synthesis of (R)-1-(4′-Hydroxyphenyl)ethanol Using Vanillyl Alcohol Oxidase

2018 ◽  
Vol 360 (12) ◽  
pp. 2370-2376 ◽  
Author(s):  
Tom A. Ewing ◽  
Jasmin Kühn ◽  
Silvia Segarra ◽  
Marta Tortajada ◽  
Ralf Zuhse ◽  
...  
Keyword(s):  
Enzymatic Synthesis ◽  
Alcohol Oxidase ◽  
Vanillyl Alcohol ◽  
Vanillyl Alcohol Oxidase

scholarly journals Kinetic mechanism of vanillyl-alcohol oxidase with short-chain 4-alkylphenols

1998 ◽  
Vol 253 (3) ◽  
pp. 712-719 ◽  
Author(s):  
Marco W. Fraaije ◽  
Robert H. H. van den Heuvel ◽  
Jules C. A. A. Roelofs ◽  
Willem J. H. van Berkel
Keyword(s):  
Alcohol Oxidase ◽  
Kinetic Mechanism ◽  
Short Chain ◽  
Vanillyl Alcohol ◽  
Vanillyl Alcohol Oxidase

scholarly journals Direction of the reactivity of vanillyl-alcohol oxidase with 4-alkylphenols

FEBS Letters ◽  
2000 ◽  
Vol 481 (2) ◽  
pp. 109-112 ◽  
Author(s):  
Robert H.H. van den Heuvel ◽  
Marco W. Fraaije ◽  
Willem J.H. van Berkel
Keyword(s):  
Alcohol Oxidase ◽  
Vanillyl Alcohol ◽  
Vanillyl Alcohol Oxidase

scholarly journals The ins and outs of vanillyl alcohol oxidase: Identification of ligand migration paths

2017 ◽  
Vol 13 (10) ◽  
pp. e1005787 ◽  
Author(s):  
Gudrun Gygli ◽  
Maria Fátima Lucas ◽  
Victor Guallar ◽  
Willem J. H. van Berkel
Keyword(s):  
Alcohol Oxidase ◽  
Vanillyl Alcohol ◽  
Ligand Migration ◽  
Vanillyl Alcohol Oxidase

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

2017 ◽  
Vol 292 (35) ◽  
pp. 14668-14679 ◽  
Author(s):  
Tom A. Ewing ◽  
Quoc-Thai Nguyen ◽  
Robert C. Allan ◽  
Gudrun Gygli ◽  
Elvira Romero ◽  
...  
Keyword(s):  
Alcohol Oxidase ◽  
Vanillyl Alcohol ◽  
Tyrosine Residues ◽  
Vanillyl Alcohol Oxidase

scholarly journals Structural Analysis of Flavinylation in Vanillyl-Alcohol Oxidase

2000 ◽  
Vol 275 (49) ◽  
pp. 38654-38658 ◽  
Author(s):  
Marco W. Fraaije ◽  
Robert H. H. van den Heuvel ◽  
Willem J. H. van Berkel ◽  
Andrea Mattevi
Keyword(s):  
Structural Analysis ◽  
Alcohol Oxidase ◽  
Vanillyl Alcohol ◽  
Vanillyl Alcohol Oxidase

scholarly journals Oxidative Catabolism of (+)-Pinoresinol Is Initiated by an Unusual Flavocytochrome Encoded by Translationally Coupled Genes within a Cluster of (+)-Pinoresinol-Coinduced Genes in Pseudomonas sp. Strain SG-MS2

2020 ◽  
Vol 86 (10) ◽  
Author(s):  
Madhura Shettigar ◽  
Sahil Balotra ◽  
Annette Kasprzak ◽  
Stephen L. Pearce ◽  
Michael J. Lacey ◽  
...  
Keyword(s):  
Alcohol Oxidase ◽  
Bioactive Molecules ◽  
Vanillyl Alcohol ◽  
Cofactor Binding ◽  
Enzyme Family ◽  
The Family ◽  
Potential Applications ◽  
Cognate Gene ◽  
Defense Compound ◽  
Vanillyl Alcohol Oxidase

ABSTRACT Burkholderia sp. strain SG-MS1 and Pseudomonas sp. strain SG-MS2 have previously been found to mineralize (+)-pinoresinol through a common catabolic pathway. Here, we used comparative genomics, proteomics, protein semipurification, and heterologous expression to identify a flavoprotein from the vanillyl alcohol oxidase/p-cresol methyl hydroxylase (VAO/PCMH) enzyme family in SG-MS2 that carries out the initial hydroxylation of (+)-pinoresinol at the benzylic carbon. The cognate gene is translationally coupled with a downstream cytochrome gene, and the cytochrome is required for activity. The flavoprotein has a unique combination of cofactor binding and cytochrome requirements for the VAO/PCMH family. The heterologously expressed enzyme has a Km of 1.17 μM for (+)-pinoresinol. The enzyme is overexpressed in strain SG-MS2 upon exposure to (+)-pinoresinol, along with 45 other proteins, 22 of which were found to be encoded by genes in an approximately 35.1-kb cluster also containing the flavoprotein and cytochrome genes. Homologs of 18 of these 22 genes, plus the flavoprotein and cytochrome genes, were also found in a 38.7-kb cluster in SG-MS1. The amino acid identities of four of the other proteins within the SG-MS2 cluster suggest they catalyze conversion of hydroxylated pinoresinol to protocatechuate and 2-methoxyhydroquinone. Nine other proteins upregulated in SG-MS2 on exposure to (+)-pinoresinol appear to be homologs of proteins known to comprise the protocatechuate and 2-methoxyhydroquinone catabolic pathways, but only three of the cognate genes lie within the cluster containing the flavoprotein and cytochrome genes. IMPORTANCE (+)-Pinoresinol is an important plant defense compound, a major food lignan for humans and some other animals, and the model compound used to study degradation of the β-β′ linkages in lignin. We report a gene cluster, in one strain each of Pseudomonas and Burkholderia, that is involved in the oxidative catabolism of (+)-pinoresinol. The flavoprotein component of the α-hydroxylase which heads the pathway belongs to the 4-phenol oxidizing (4PO) subgroup of the vanillyl alcohol oxidase/p-cresol methyl hydroxylase (VAO/PCMH) enzyme family but constitutes a novel combination of cofactor and electron acceptor properties for the family. It is translationally coupled with a cytochrome gene whose product is also required for activity. The work casts new light on the biology of (+)-pinoresinol and its transformation to other bioactive molecules. Potential applications of the findings include new options for deconstructing lignin into useful chemicals and the generation of new phytoestrogenic enterolactones from lignans.

Vanillyl-alcohol oxidase, a tasteful biocatalyst

2001 ◽  
Vol 11 (4-6) ◽  
pp. 185-188 ◽  
Author(s):  
Robert H.H. van den Heuvel ◽  
Marco W. Fraaije ◽  
Andrea Mattevi ◽  
Colja Laane ◽  
Willem J.H. van Berkel
Keyword(s):  
Alcohol Oxidase ◽  
Vanillyl Alcohol ◽  
Vanillyl Alcohol Oxidase

scholarly journals Structure, function and redesign of vanillyl-alcohol oxidase

2002 ◽  
Vol 1233 ◽  
pp. 13-24 ◽  
Author(s):  
Robert H.H van den Heuvel ◽  
Marco W Fraaije ◽  
Andrea Mattevi ◽  
Willem J.H van Berkel
Keyword(s):  
Structure Function ◽  
Alcohol Oxidase ◽  
Vanillyl Alcohol ◽  
Vanillyl Alcohol Oxidase
Sign in / Sign up

Export Citation Format

Share Document