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Connecting Unexplored Protein Crystal Structures to Enzymatic Function
Author(s) -
SteffenMunsberg Fabian,
Vickers Clare,
Thontowi Ahmad,
Schätzle Sebastian,
Tumlirsch Tony,
Svedendahl Humble Maria,
Land Henrik,
Berglund Per,
Bornscheuer Uwe T.,
Höhne Matthias
Publication year - 2013
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201200544
Subject(s) - enzyme , substrate (aquarium) , chemistry , biocatalysis , function (biology) , enzyme catalysis , catalysis , protein function , combinatorial chemistry , stereochemistry , organic chemistry , biochemistry , biology , reaction mechanism , ecology , evolutionary biology , gene
Digging in the database: Four synthetically useful transaminases for which no function was known were studied by evaluating a set of eight amino donors and seven acceptors (see figure). The four enzymes differ substantially in their catalytic properties and substrate preferences. We also used the enzymes in the asymmetric synthesis of a range of chiral amines and observed excellent enantioselectivities and conversions.