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A Practical and Fast Method To Predict the Thermodynamic Preference of ω‐Transaminase‐Based Transformations
Author(s) -
Meier Robert J.,
Gundersen Maria T.,
Woodley John M.,
Schürmann Martin
Publication year - 2015
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.201500347
Subject(s) - transaminase , in silico , simple (philosophy) , base (topology) , molecule , chemistry , computational chemistry , computer science , biological system , combinatorial chemistry , biochemical engineering , mathematics , organic chemistry , engineering , enzyme , biochemistry , biology , mathematical analysis , philosophy , epistemology , gene
Abstract A simple, easy‐to‐use, and fast approach method is proposed and validated that can predict whether a transaminase reaction is thermodynamically unfavourable. This allowed us to deselect, in the present case, at least 50% of the reactions because they were thermodynamically unfavourable as confirmed by experiment. Once a larger data base is established, in silico screening of several new reactions (new target molecules) can easily be performed each day.