Ms. Tatu Meyer

Mini Academic CV

University degrees:

First degree or intermediate examination:

  • Vordiplom(Biology), 1999, Heinrich-Heine University, Düsseldorf, Germany

Second degree and/or intermediate examination:

  • Diplom(Biology), 2008, Heinrich-Heine University, Düsseldorf, Germany


  • Smits S.H.J, Meyer T, Mueller A, van Os N, Stoldt M, et al. (2010). Insights into the Mechanism of Ligand Binding to Octopine Dehydrogenase from Pecten maximus by NMR and Crystallography. PLoS One.

BioStruct PhD project

Biochemical and structural characterisation of opine dehydrogenases
Opine dehydrogenases (OpDHs) terminate anaerobic glycolysis in many marine invertebrates. OpDHs catalyse the reversible, reductive condensation of an α-keto acid with the amino group of an amino acid, using NADH as a co-substrate. The resulting products are called opines. The octopine dehydrogenase (OcDH) from Pecten maximus, a member of the OpDH family, only uses L-arginine as its amino acid substrate. During the reductive condensation reaction of L-arginine with pyruvate, a second chiral centre is formed. This capability to synthesise a product (opine) with one, new chiral centre with perfect selectivity, from one chiral and one achiral precursor, potentially makes OpDHs biotechnologically important candidates for an enzyme-based chiral synthesis. The aim of this project is to alter the substrate specificity of OcDH by site-directed mutagenesis in order to create novel opines. Furthermore, mutants will be created to change the stereoselectivity. These OcDH mutants will be characterised via biochemical methods as well as by x-ray crystallography. Solving these structures as apo or substrate bound will provide further insights into substrate recognition, binding and the underlying reaction mechanisms. Other enzymes of this family are the alanopine and strombine dehydrogenase from Arenicola marina. Interestingly, their substrates differ only in one methyl chain but initial experiments revealed a significant difference in their kinetics. Thus the reaction mechanism of these two enzymes will be characterised using the same experimental approach outlined above.


Topic Supervisor:

undefined Prof. Dr. Lutz Schmitt, Institute for Biochemistry, Heinrich Heine University Duesseldorf, Schmitt Group

Complementary Supervisor:

undefinedProf. Dr. Georg Groth, Institute for Plant Biochemistry, Heinrich Heine University Duesseldorf, Groth Group

Responsible for the content: E-MailBioStruct Office