Engineering a Promiscuous Tautomerase into a More Efficient Aldolase for Self-Condensations of Linear Aliphatic Aldehydes.

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Engineering a Promiscuous Tautomerase into a More Efficient Aldolase for Self-Condensations of Linear Aliphatic Aldehydes.

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2017 nî lūn-bûn

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2017年学术文章

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Engineering a Promiscuous Taut ...... of Linear Aliphatic Aldehydes.

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Engineering a Promiscuous Taut ...... of Linear Aliphatic Aldehydes.

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Item

label

Engineering a Promiscuous Taut ...... of Linear Aliphatic Aldehydes.

@ast

Engineering a Promiscuous Taut ...... of Linear Aliphatic Aldehydes.

@en

prefLabel

Engineering a Promiscuous Taut ...... of Linear Aliphatic Aldehydes.

@ast

Engineering a Promiscuous Taut ...... of Linear Aliphatic Aldehydes.

@en

P1476

Engineering a Promiscuous Taut ...... of Linear Aliphatic Aldehydes.

@en

P2093

Edzard M Geertsema

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

Jan-Ytzen van der Meer

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

Mehran Rahimi

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P2860

Promiscuity and electrostatic flexibility in the alkaline phosphatase superfamily

Evidence for the formation of an enamine species during aldol and Michael-type addition reactions promiscuously catalyzed by 4-oxalocrotonate tautomerase

A Promiscuous De Novo Retro-Aldolase Catalyzes Asymmetric Michael Additions via Schiff Base Intermediates

The 4-oxalocrotonate tautomerase family of enzymes: how nature makes new enzymes using a beta-alpha-beta structural motif

Physically associated enzymes produce and metabolize 2-hydroxy-2,4-dienoate, a chemically unstable intermediate formed in catechol metabolism via meta cleavage in Pseudomonas putida

Addressing the numbers problem in directed evolution.

The chemical versatility of the beta-alpha-beta fold: catalytic promiscuity and divergent evolution in the tautomerase superfamily.

Expanding the enzyme universe: accessing non-natural reactions by mechanism-guided directed evolution.

Chemomimetic biocatalysis: exploiting the synthetic potential of cofactor-dependent enzymes to create new catalysts.

Mutations Closer to the Active Site Improve the Promiscuous Aldolase Activity of 4-Oxalocrotonate Tautomerase More Effectively than Distant Mutations.

P304

1435-1441

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P31

scholarly article

P356

10.1002/CBIC.201700121

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P433

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

P478

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

P50

Gerrit J Poelarends

P577

2017-04-20T00:00:00Z

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P698

28426139

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P932

5575498

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