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

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The ins and outs of vanillyl alcohol oxidase: Identification of ligand migration paths.A Xylenol Orange-Based Screening Assay for the Substrate Specificity of Flavin-Dependent para-Phenol Oxidases.

P2860

Q42658318-AEFCB687-170E-4FA1-8D75-9545AEE41AE4 Q49996879-77E0CADF-CB48-4421-92BF-B60A972C1F2A

P2860

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

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http://www.wikidata.org/entity/Q50885148

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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name

Two tyrosine residues, Tyr-108 ...... s in vanillyl-alcohol oxidase.

@en

Two tyrosine residues, Tyr-108 ...... s in vanillyl-alcohol oxidase.

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type

Item

label

Two tyrosine residues, Tyr-108 ...... s in vanillyl-alcohol oxidase.

@en

Two tyrosine residues, Tyr-108 ...... s in vanillyl-alcohol oxidase.

@nl

prefLabel

Two tyrosine residues, Tyr-108 ...... s in vanillyl-alcohol oxidase.

@en

Two tyrosine residues, Tyr-108 ...... s in vanillyl-alcohol oxidase.

@nl

P1476

Two tyrosine residues, Tyr-108 ...... s in vanillyl-alcohol oxidase.

@en

P2093

Claudia Binda

http://www.w3.org/2001/XMLSchema#string

Elvira Romero

http://www.w3.org/2001/XMLSchema#string

Gudrun Gygli

http://www.w3.org/2001/XMLSchema#string

Marco W Fraaije

http://www.w3.org/2001/XMLSchema#string

Robert C Allan

http://www.w3.org/2001/XMLSchema#string

P2860

Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism

Asp-170 is crucial for the redox properties of vanillyl-alcohol oxidase

A ternary complex of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) with acetyl-CoA and vanillin gives insights into substrate specificity and mechanism

p-Coumaric acid decarboxylase from Lactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism

Interception of teicoplanin oxidation intermediates yields new antimicrobial scaffolds

The Crystal Structure and Mechanism of an Unusual Oxidoreductase, GilR, Involved in Gilvocarcin V Biosynthesis

Biocatalytic Properties and Structural Analysis of Eugenol Oxidase from Rhodococcus jostii RHA1: A Versatile Oxidative Biocatalyst

Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity

Coot: model-building tools for molecular graphics

Overview of the CCP4 suite and current developments

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14668-14679

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scholarly article

P356

10.1074/JBC.M117.778449

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English

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292

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Andrea Mattevi

Willem J.H. van Berkel

Quoc-Thai Nguyen

Tom A Ewing

P577

2017-07-17T00:00:00Z

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28717004

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5582857

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

about

P2860

P2860

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

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932