Two-Enzyme Hydrogen-Borrowing Amination of Alcohols Enabled by a Cofactor-Switched Alcohol Dehydrogenase

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A biocatalytic cascade for the amination of unfunctionalised cycloalkanes.A hydrogen fuel cell for rapid, enzyme-catalysed organic synthesis with continuous monitoring.

P2860

Q49940924-1F9C5BE4-B70F-4A5D-89E4-EB8EFFACCDB8 Q50107767-DB2A30F8-DB12-402D-BC38-4DBA14B15DDE

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Two-Enzyme Hydrogen-Borrowing Amination of Alcohols Enabled by a Cofactor-Switched Alcohol Dehydrogenase

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http://www.wikidata.org/entity/Q58048488

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im September 2017 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

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наукова стаття, опублікована у вересні 2017

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Two-Enzyme Hydrogen-Borrowing ...... Switched Alcohol Dehydrogenase

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Two-Enzyme Hydrogen-Borrowing ...... Switched Alcohol Dehydrogenase

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Item

label

Two-Enzyme Hydrogen-Borrowing ...... Switched Alcohol Dehydrogenase

@en

Two-Enzyme Hydrogen-Borrowing ...... Switched Alcohol Dehydrogenase

@nl

prefLabel

Two-Enzyme Hydrogen-Borrowing ...... Switched Alcohol Dehydrogenase

@en

Two-Enzyme Hydrogen-Borrowing ...... Switched Alcohol Dehydrogenase

@nl

P1476

Two-Enzyme Hydrogen-Borrowing ...... Switched Alcohol Dehydrogenase

@en

P2093

Matthew P. Thompson

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

Nicholas J. Turner

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

P2860

Biochemical and structural properties of chimeras constructed by exchange of cofactor-binding domains in alcohol dehydrogenases from thermophilic and mesophilic microorganisms

Understanding nature's strategies for enzyme-catalyzed racemization and epimerization

Conversion of alcohols to enantiopure amines through dual-enzyme hydrogen-borrowing cascades

Cloning, functional expression and biochemical characterization of a stereoselective alcohol dehydrogenase from Pseudomonas fluorescens DSM50106.

A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity.

Redesign of the coenzyme specificity of a dehydrogenase by protein engineering.

Mutation of Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase at Trp-110 affects stereoselectivity of aromatic ketone reduction.

Improving the NADH-cofactor specificity of the highly active AdhZ3 and AdhZ2 from Escherichia coli K-12.

Substitutions at the cofactor phosphate-binding site of a clostridial alcohol dehydrogenase lead to unexpected changes in substrate specificity.

Structure-guided alteration of coenzyme specificity of formate dehydrogenase by saturation mutagenesis to enable efficient utilization of NADP+.

P304

3833-3836

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

P31

scholarly article

P356

10.1002/CCTC.201701092

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

P433

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

P478

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

P577

2017-09-13T00:00:00Z

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

Two-Enzyme Hydrogen-Borrowing Amination of Alcohols Enabled by a Cofactor-Switched Alcohol Dehydrogenase

about

P2860

P2860

Two-Enzyme Hydrogen-Borrowing Amination of Alcohols Enabled by a Cofactor-Switched Alcohol Dehydrogenase

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577