@article{b7e06eb24c544cc88839e2a7dab0e6e6,
title = "The role of the GGGX motif in determining the activity and enantioselectivity of pig liver esterase towards tertiary alcohols",
abstract = "The GGG(A) X motif has been reported to determine the activity of esterases or lipases towards tertiary alcohols. The gamma-isoenzyme of pig liver esterase (gamma-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.",
keywords = "alcohol bacillus-subtilis biocatalysis cloning enantioselectivity functional expression GGG(A) X motif identification kinetic resolution molecular modeling mutants pichia-pastoris pig liver esterase space tertiary versatile",
author = "M Gall and R Kourist and M Schmidt and Bornscheuer, {U T}",
note = "ISI Document Delivery No.: 628EZ Times Cited: 1 Cited Reference Count: 36 Gall, Markus Kourist, Robert Schmidt, Marlen Bornscheuer, Uwe T. European Network on Directed Evolution of Functional Proteins (ENEFP) ; European Social Funds ; VentureCup M-V [UG09005] The authors gratefully acknowledge Dr. Dominique Bottcher and Sebastian Bartsch (Institute of Biochemistry, Department of Biotechnology and Enzyme Catalysis, Greifswald) for inspiring scientific discussions. M. G. thanks the European Network on Directed Evolution of Functional Proteins (ENEFP) for financial support. R. K. thanks the European Social Funds and the VentureCup M-V (UG09005). Taylor & francis ltd Abingdon",
year = "2010",
doi = "10.3109/10242421003753803",
language = "English",
volume = "28",
pages = "201--208",
journal = "Biocatalysis and Biotransformation",
issn = "1024-2422",
publisher = "Taylor & Francis Group",
}