Asymmetric Ketone Reduction by Imine Reductases.

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A Retrosynthesis Approach for Biocatalysis in Organic Synthesis.Recent advances in imine reductase-catalyzed reactions.Extended Catalytic Scope of a Well-Known Enzyme: Asymmetric Reduction of Iminium Substrates by Glucose Dehydrogenase.

P2860

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P2860

Asymmetric Ketone Reduction by Imine Reductases.

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http://www.wikidata.org/entity/Q51289611

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh-hant

name

Asymmetric Ketone Reduction by Imine Reductases.

@en

Asymmetric Ketone Reduction by Imine Reductases.

@nl

type

Item

label

Asymmetric Ketone Reduction by Imine Reductases.

@en

Asymmetric Ketone Reduction by Imine Reductases.

@nl

prefLabel

Asymmetric Ketone Reduction by Imine Reductases.

@en

Asymmetric Ketone Reduction by Imine Reductases.

@nl

P1476

Asymmetric Ketone Reduction by Imine Reductases.

@en

P2093

Leann Quertinmont

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

Maike Lenz

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

Stefan Lutz

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

P2860

Structural assembly of the active site in an aldo-keto reductase by NADPH cofactor

Structure and activity of NADPH-dependent reductase Q1EQE0 from Streptomyces kanamyceticus, which catalyses the R-selective reduction of an imine substrate

An Ancient Fingerprint Indicates the Common Ancestry of Rossmann-Fold Enzymes Utilizing Different Ribose-Based Cofactors

STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF CIRCULAR PERMUTATION ON THE ACTIVE SITE OF OLD YELLOW ENZYME

RApid Parallel Protein EvaluatoR (RAPPER), from gene to enzyme function in one day.

Mutagenesis of 3 alpha-hydroxysteroid dehydrogenase reveals a "push-pull" mechanism for proton transfer in aldo-keto reductases.

An (R)-Imine Reductase Biocatalyst for the Asymmetric Reduction of Cyclic Imines

Steric vs. electronic effects in the Lactobacillus brevis ADH-catalyzed bioreduction of ketones.

Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity.

Synthesis of enantiopure fluorohydrins using alcohol dehydrogenases at high substrate concentrations.

P304

253-256

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P31

scholarly article

P356

10.1002/CBIC.201600647

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

P433

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

P478

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

P50

Bettina M. Nestl

Jan Meisner

Johannes Kästner

P577

2016-12-02T00:00:00Z

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

P698

27911981

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

Asymmetric Ketone Reduction by Imine Reductases.

about

P2860

P2860

Asymmetric Ketone Reduction by Imine Reductases.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698