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

Stefan Marsden, Lorina Gjonaj, Stephen Eustace, Ulf Hanefeld

Research output: Contribution to journalArticleScientificpeer-review

13 Citations (Scopus)
58 Downloads (Pure)


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.
Original languageEnglish
Pages (from-to)1808-1814
Issue number10
Publication statusPublished - 2017


  • aldehydes
  • C−C coupling
  • enzyme catalysis
  • kinetics
  • thermodynamics


Dive into the research topics of 'Separating Thermodynamics from Kinetics: A New Understanding of the Transketolase Reaction'. Together they form a unique fingerprint.

Cite this