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Separating Thermodynamics from Kinetics—A New Understanding of the Transketolase Reaction
Author(s) -
Marsden Stefan R.,
Gjonaj Lorina,
Eustace Stephen J.,
Hanefeld Ulf
Publication year - 2017
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.201601649
Subject(s) - transketolase , chemistry , kinetics , active site , substrate (aquarium) , hydrogen bond , computational chemistry , stereochemistry , catalysis , organic chemistry , enzyme , molecule , physics , oceanography , quantum mechanics , geology
Transketolase catalyzes asymmetric C−C bond formation of two highly polar compounds. Over the last 30 years, the reaction has unanimously been described in literature as irreversible because of the concomitant release of CO 2 if using lithium hydroxypyruvate (LiHPA) as a substrate. Following the reaction over a longer period of time however, we have now found it to be initially kinetically controlled. Contrary to previous suggestions, for the non‐natural conversion of synthetically more interesting apolar substrates, the complete change of active‐site polarity is therefore not necessary. From docking studies it was revealed that water and hydrogen‐bond networks are essential for substrate binding, thus allowing aliphatic aldehydes to be converted in the charged active site of transketolase.