Recent advances in the study of enzyme promiscuity in the tautomerase superfamily.
about
Evidence for the formation of an enamine species during aldol and Michael-type addition reactions promiscuously catalyzed by 4-oxalocrotonate tautomeraseCatalytic Promiscuity of Transaminases: Preparation of Enantioenriched β-Fluoroamines by Formal Tandem Hydrodefluorination/DeaminationThe Generation and Exploitation of Protein Mutability Landscapes for Enzyme EngineeringPromiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.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.Specificity Effects of Amino Acid Substitutions in Promiscuous Hydrolases: Context-Dependence of Catalytic Residue Contributions to Local Fitness Landscapes in Nearby Sequence Space.A mutational analysis of active site residues in trans-3-chloroacrylic acid dehalogenase.Evolution of a Catalytic Mechanism.An overview of the alpha-, beta- and gamma-carbonic anhydrases from Bacteria: can bacterial carbonic anhydrases shed new light on evolution of bacteria?Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases.Demethionylation of Pro-1 variants of 4-oxalocrotonate tautomerase in Escherichia coli by co-expression with an engineered methionine aminopeptidase.Inter- and intramolecular aldol reactions promiscuously catalyzed by a proline-based tautomerase.D-Aminoacylase-initiated cascade Aldol condensation/Robinson annulation for synthesis of substituted cyclohex-2-enones from simple aldehydes and acetone.Biocatalytic Michael-type additions of acetaldehyde to nitroolefins with the proline-based enzyme 4-oxalocrotonate tautomerase yielding enantioenriched γ-nitroaldehydes.Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology
P2860
Q27698082-F35C3C68-A5FD-4B77-A0A6-9790631A3353Q27703818-EF9F998C-2E4C-4DDA-A621-258A2E0F75ABQ28070023-CA7C8D72-EB18-4F92-BEC7-C9B68D6E38CBQ36019839-CF8F79DE-17AD-48E7-834A-59D261DF2972Q36033515-F0F5B597-2483-407C-BD04-0A5FB20552DEQ36351769-D7A0941D-984F-40D9-A49C-C8D310E13BFDQ36360999-5C90AF7E-86E0-423F-99D0-BC36B71A219FQ37189223-57D25DCE-EFC3-4026-A72F-C175E61176CCQ37237749-F576E076-B5B5-40A7-BCFC-1A17DC4CA161Q38207158-CC6FE948-5AD9-43B3-BBF8-F003A7B150FFQ38287400-C0C067DE-E1F1-434F-ABE8-D65D74340374Q38917445-C653BF38-682F-4F65-B53A-CF9A0CCE7B6CQ41852843-BCD3F61B-ABC0-426F-9DBA-8B66A02DC28FQ48145667-6E28AE42-24DB-44A5-A500-466C47DB1822Q50457142-602F7E5D-025C-498E-9ED9-9531C2FB13BFQ54784192-2F995E18-DBEF-4956-B7F1-CDBDA41A85CDQ59320058-0DDFB5D6-B6E0-4258-BE63-839B3FA9BCBF
P2860
Recent advances in the study of enzyme promiscuity in the tautomerase superfamily.
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Recent advances in the study of enzyme promiscuity in the tautomerase superfamily.
@en
type
label
Recent advances in the study of enzyme promiscuity in the tautomerase superfamily.
@en
prefLabel
Recent advances in the study of enzyme promiscuity in the tautomerase superfamily.
@en
P2093
P2860
P356
P1433
P1476
Recent advances in the study of enzyme promiscuity in the tautomerase superfamily.
@en
P2093
Bert-Jan Baas
Edzard M Geertsema
Ellen Zandvoort
Gerrit J Poelarends
P2860
P304
P356
10.1002/CBIC.201300098
P577
2013-05-03T00:00:00Z