The role of the GGGX motif in determining the activity and enantioselectivity of pig liver esterase towards tertiary alcohols

Autor:	Robert Kourist, Markus Gall, Marlen Schmidt, Uwe T. Bornscheuer
Rok vydání:	2010
Předmět:	Alanine chemistry.chemical_classification Molecular model Stereochemistry Chemistry Mutant Biochemistry Esterase Catalysis Kinetic resolution Enzyme Selectivity Pig liver Biotechnology
Zdroj:	Biocatalysis and Biotransformation. 28:201-208
ISSN:	1029-2446 1024-2422
Popis:	The GGG(A)X motif has been reported to determine the activity of esterases or lipases towards tertiary alcohols. The γ-isoenzyme of pig liver esterase (γ-PLE, PLE 1) contains a GGGX motif; this motif was systematically mutated to the corresponding AGGX, GAGX, GGAX, AAAX, AAGX, AGAX and GAAX motifs to investigate its influence on the activity and especially enantioselectivity in the kinetic resolution of three acetates of tertiary alcohols. None of the mutants showed higher enantioselectivity than the starting enzyme (E=17), and mutation of the central glycine to alanine completely destroyed activity and selectivity. Hence, only subtle changes of this crucial motif lead to substantial changes in esterase properties. These findings were analyzed and interpreted by computer modeling.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::9657de12c90c465f9ab915dd9becc224 https://doi.org/10.3109/10242421003753803 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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