Directed evolution of a thermostable l-aminoacylase biocatalyst

Journal of Biotechnology

Volumn 155, Issue 4, 2011, Pages 396-405

  Parker, Brenda M ^a   Taylor, Ian N ^b   Woodley, John M ^c   Ward, John M ^a   Dalby, Paul A ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b Chirotech Technology Ltd   (United Kingdom)

^c TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

Author keywords

Amino acids; Biocatalysis; Directed evolution; L Aminoacylase; Saturation mutagenesis

Indexed keywords

ACTIVE SITE; AMIDE HYDROLYSIS; BIOCATALYSIS; CHIRAL INTERMEDIATES; CLOSED FORM; CONFORMATIONAL TRANSITIONS; DIRECTED EVOLUTION; ENANTIOSELECTIVE; EXTREME ENVIRONMENT; L-AMINO ACIDS; L-AMINOACYLASE; PROCESS CONDITION; RACEMIC MIXTURES; SATURATION MUTAGENESIS; STRUCTURAL HOMOLOGY; WILD TYPES; ZINC-BINDING DOMAINS;

AMIDES; AMINO ACIDS; ENZYME ACTIVITY;

SUBSTRATES;

ENZYME VARIANT; LEVO AMINOACYLASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING KINETICS; BIOCATALYSIS; CHEMICAL MUTAGENESIS; CHIRALITY; DIMERIZATION; ENANTIOSELECTIVITY; ENZYME ACTIVITY; HYDROLYSIS; PRIORITY JOURNAL; RACEMIC MIXTURE; TEMPERATURE SENSITIVITY; THERMOCOCCUS LITORALIS;

AMIDES; AMIDOHYDROLASES; BINDING SITES; DIRECTED MOLECULAR EVOLUTION; ENZYME STABILITY; EVOLUTION, MOLECULAR; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PHENYLALANINE; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; THERMOCOCCUS; VALINE;

THERMOCOCCUS LITORALIS;

EID: 80052421687     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.07.029     Document Type: Article

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