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

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

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

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Mutations Closer to the Active Site Improve the Promiscuous Aldolase Activity of 4-Oxalocrotonate Tautomerase More Effectively than Distant Mutations.Engineering a Promiscuous Tautomerase into a More Efficient Aldolase for Self-Condensations of Linear Aliphatic Aldehydes.Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases.Stereochemical Control of Enzymatic Carbon-Carbon Bond-Forming Michael-Type Additions by "Substrate Engineering".Inter- and intramolecular aldol reactions promiscuously catalyzed by a proline-based tautomerase.

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

http://www.wikidata.org/entity/Q27698082

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name

Evidence for the formation of ...... y 4-oxalocrotonate tautomerase

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Evidence for the formation of ...... y 4-oxalocrotonate tautomerase

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Evidence for the formation of ...... y 4-oxalocrotonate tautomerase

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Evidence for the formation of ...... y 4-oxalocrotonate tautomerase

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Evidence for the formation of ...... y 4-oxalocrotonate tautomerase

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Evidence for the formation of ...... y 4-oxalocrotonate tautomerase

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Evidence for the formation of ...... y 4-oxalocrotonate tautomerase

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Evidence for the formation of ...... y 4-oxalocrotonate tautomerase

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Evidence for the formation of ...... y 4-oxalocrotonate tautomerase

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Evidence for the formation of ...... y 4-oxalocrotonate tautomerase

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Edzard M Geertsema

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Harshwardhan Poddar

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Mehran Rahimi

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P2860

Crystal structure of 4-oxalocrotonate tautomerase inactivated by 2-oxo-3-pentynoate at 2.4 A resolution: analysis and implications for the mechanism of inactivation and catalysis

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

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

Crystal structures of proline-derived enamines.

Chiral amines as organocatalysts for asymmetric conjugate addition to nitroolefins and vinyl sulfones via enamine activation.

Recent advances in the study of enzyme promiscuity in the tautomerase superfamily.

Promiscuous catalysis of asymmetric Michael-type additions of linear aldehydes to β-nitrostyrene by the proline-based enzyme 4-oxalocrotonate tautomerase.

Mutants of 4-oxalocrotonate tautomerase catalyze the decarboxylation of oxaloacetate through an imine mechanism.

Diphenylprolinol silyl ether as catalyst of an asymmetric, catalytic, and direct Michael reaction of nitroalkanes with alpha,beta-unsaturated aldehydes.

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738-741

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scholarly article

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10.1002/CBIC.201402687

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5

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16

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Andy-Mark Thunnissen

Gerrit J Poelarends

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2015-03-23T00:00:00Z

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25728471

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