Separating Thermodynamics from Kinetics: A New Understanding of the Transketolase Reaction

Marsden, S.R.; Gjonaj, L.; Eustace, S.J.; Hanefeld, U.

doi:10.1002/cctc.201601649

Separating Thermodynamics from Kinetics

Title

Separating Thermodynamics from Kinetics: A New Understanding of the Transketolase Reaction

Author

Marsden, S.R. (TU Delft BT/Biocatalysis)
Gjonaj, L. (TU Delft BT/Biocatalysis)
Eustace, S.J. (TU Delft BT/Biocatalysis)
Hanefeld, U. (TU Delft BT/Biocatalysis)

Date

2017

Abstract

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 CO2 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.

Subject

aldehydes
C−C coupling
enzyme catalysis
kinetics
thermodynamics

To reference this document use:

http://resolver.tudelft.nl/uuid:5e596321-a133-454e-b4de-f36e833fc9ad

DOI

https://doi.org/10.1002/cctc.201601649

ISSN

1867-3880

Source

ChemCatChem, 9 (10), 1808-1814

Part of collection

Institutional Repository