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Conversion of a Carboxylesterase into a Triacylglycerol Lipase by a Random Mutation
Author(s) -
ReyesDuarte Dolores,
Polaina Julio,
LópezCortés Nieves,
Alcalde Miguel,
Plou Francisco J.,
Elborough Kieran,
Ballesteros Antonio,
Timmis Kenneth N.,
Golyshin Peter N.,
Ferrer Manuel
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200502461
Subject(s) - carboxylesterase , lipase , chemistry , enzyme , substrate (aquarium) , biochemistry , stereochemistry , biology , ecology
A true convert : The carboxylesterase enzyme R.34 (see picture) can be converted into a triacylglycerol lipase without modification of the shape, size, or hydrophobicity of the substrate binding site. The substitution of Asn33 by Asp results in a salt bridge between the Asp33 and Arg49, which causes a distortion of the enzyme structure that makes the catalytic site more accessible to larger substrates but also more labile.