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

scientific article

Mutations Closer to the Active Site Improve the Promiscuous Aldolase Activity of 4-Oxalocrotonate Tautomerase More Effectively than Distant Mutations. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/CBIC.201600149
P698PubMed publication ID27238293

P50authorGerrit J PoelarendsQ88902935
P2093author name stringBert-Jan Baas
Mehran Rahimi
Edzard M Geertsema
Harshwardhan Poddar
Jan-Ytzen van der Meer
P2860cites workDiminishing returns and tradeoffs constrain the laboratory optimization of an enzymeQ27683542
Evidence for the formation of an enamine species during aldol and Michael-type addition reactions promiscuously catalyzed by 4-oxalocrotonate tautomeraseQ27698082
The 4-oxalocrotonate tautomerase family of enzymes: how nature makes new enzymes using a beta-alpha-beta structural motifQ28202879
Physically associated enzymes produce and metabolize 2-hydroxy-2,4-dienoate, a chemically unstable intermediate formed in catechol metabolism via meta cleavage in Pseudomonas putidaQ28354983
Expanding the substrate scope of enzymes: combining mutations obtained by CASTingQ33247423
Addressing the numbers problem in directed evolutionQ33345289
Evolutionary potential of (beta/alpha)8-barrels: functional promiscuity produced by single substitutions in the enolase superfamilyQ33967159
Designed divergent evolution of enzyme functionQ33993746
Enzyme promiscuity: a mechanistic and evolutionary perspectiveQ34021669
The chemical versatility of the beta-alpha-beta fold: catalytic promiscuity and divergent evolution in the tautomerase superfamilyQ34095040
Improving enzyme properties: when are closer mutations better?Q36113206
Enzyme promiscuity: evolutionary and mechanistic aspects.Q36580808
Protein engineers turned evolutionistsQ37020095
Recent progress in stereoselective synthesis with aldolasesQ37673484
Mutational effects and the evolution of new protein functions.Q37773157
Novel carbon-carbon bond formations for biocatalysisQ37847523
Recent advances in the study of enzyme promiscuity in the tautomerase superfamilyQ38104684
Recent developments in enzyme promiscuity for carbon-carbon bond-forming reactionsQ38322861
Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective MichaelasesQ38917445
Promiscuous catalysis of asymmetric Michael-type additions of linear aldehydes to β-nitrostyrene by the proline-based enzyme 4-oxalocrotonate tautomeraseQ43778627
Biocatalytic Michael-type additions of acetaldehyde to nitroolefins with the proline-based enzyme 4-oxalocrotonate tautomerase yielding enantioenriched γ-nitroaldehydes.Q54784192
The Catalytic Asymmetric Aldol Reaction.Q55033822
Chemical and enzymic ketonization of 2-hydroxymuconate, a conjugated enolQ56815356
Directed evolution of enantioselective enzymes: iterative cycles of CASTing for probing protein-sequence spaceQ56899243
P433issue13
P304page(s)1225-1228
P577publication date2016-05-30
P1433published inChemBioChemQ634395
P1476titleMutations Closer to the Active Site Improve the Promiscuous Aldolase Activity of 4-Oxalocrotonate Tautomerase More Effectively than Distant Mutations
P478volume17

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cites work (P2860)
Q64057759Biocatalytic Asymmetric Michael Additions of Nitromethane to α,β-Unsaturated Aldehydes via Enzyme-bound Iminium Ion Intermediates
Q90238189Enantiocomplementary Epoxidation Reactions Catalyzed by an Engineered Cofactor-Independent Non-Natural Peroxygenase
Q89966600Enantioselective Aldol Addition of Acetaldehyde to Aromatic Aldehydes Catalyzed by Proline-Based Carboligases
Q36351769Engineering a Promiscuous Tautomerase into a More Efficient Aldolase for Self-Condensations of Linear Aliphatic Aldehydes
Q89738262Selective Colorimetric "Turn-On" Probe for Efficient Engineering of Iminium Biocatalysis