about
Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triadAutoproteolytic Activation of ThnT Results in Structural Reorganization Necessary for Substrate Binding and CatalysisExploring the role of conformational heterogeneity in cis-autoproteolytic activation of ThnT.Consecutive radical S-adenosylmethionine methylations form the ethyl side chain in thienamycin biosynthesisTryptophan Synthase Uses an Atypical Mechanism To Achieve Substrate Specificity.Catalytic iron-carbene intermediate revealed in a cytochrome carbene transferaseDirected Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational EnsembleEngineered Biosynthesis of β-Alkyl Tryptophan AnaloguesFacile in Vitro Biocatalytic Production of Diverse TryptaminesStructure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactionsModular control of l-tryptophan isotopic substitution via an efficient biosynthetic cascade
P50
Q26781998-555B5E0D-3094-4B55-A225-C398859C655DQ27681206-8273E492-DA9B-474B-9286-D5AEE327BA07Q27684351-C5462490-470B-4399-AA2F-EBD0FE8E883BQ35990000-D061886B-A939-4562-B429-3B077FE5B5CDQ39115544-9FA0A5E8-A048-415D-A508-A5285AF4FE1CQ56889728-0EB97A25-D025-45E4-97F5-65F7CDAD94F7Q56890015-25B10F68-6476-494C-A2C6-7AB0E0945599Q59762064-C60BFE76-56D9-48CD-BCDD-F1A187973CD1Q92320303-86D3BFBB-0BD0-48EB-946C-BC793407F040Q92913386-DEA81F4D-9628-4125-847C-B8CA3332A504Q95839835-A1FD1CB7-80C2-4646-B337-E6A4F0B5521C
P50
description
researcher ORCID ID = 0000-0002-9635-4844
@en
wetenschapper
@nl
name
Andrew R Buller
@ast
Andrew R Buller
@en
Andrew R Buller
@es
Andrew R Buller
@nl
type
label
Andrew R Buller
@ast
Andrew R Buller
@en
Andrew R Buller
@es
Andrew R Buller
@nl
prefLabel
Andrew R Buller
@ast
Andrew R Buller
@en
Andrew R Buller
@es
Andrew R Buller
@nl
P31
P496
0000-0002-9635-4844