Skip to ContentSkip to Navigation
Research GBB Research Principal Investigators Dr. Andy-Mark Thunnissen


Dr. Andy-Mark Thunnissen
Dr. Andy-Mark Thunnissen

Dr. Andy-Mark Thunnissen was trained in biophysical chemistry (PhD in 1995) and is an expert in the area of protein X-ray crystallography. He received his PhD at the University of Groningen in 1995. Following postdoc work at UC Berkeley, where he studied drug-bound complexes of human cyclin-dependent kinase 2, he returned to the University of Groningen in 1997. His current research interest focuses on the structure/function characterization and analysis of biotechnologically relevant enzymes. He participates in multidisciplinary research projects, involving synthetic chemistry, microbiology, molecular biology and X-ray crystallography, aimed at novel enzyme design or structured-guided engineering of tailored enzymes with altered or improved characteristics. Studied enzymes include cytochrome P450 monooxygenases, lyases, tautomerases, transaminases and glycosyltransferases.

Thunnissen has published 40 peer-reviewed papers with >2000 citations; his h-index is 19 (Google Scholar) and 17 (Web of Science).

Three top publications 2010-2016

1.        Jozwik IK, Kiss, FM, Gricman L, Abdulmughni A, Brill E, Zapp J, Pleiss J, Bernhardt R, Thunnissen, AMWH (2016) Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium. FEBS Journal 283(22): 4128-4148.

2.        van der Meer JY, Poddar H, Baas BJ, Miao YF, Rahimi M, Kunzendorf A, van Merkerk R, Tepper PG, Geertsema EM, Thunnissen, AMWH, Quax WJ, Poelarends GJ (2016) Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases. Nature Communications 7: 10911.

3.        Raj H, Szymanski W, de Villiers J, Rozeboom HJ, Veetil VP, Reis CR, de Villiers M, Dekker FJ, de Wildeman S, Quax WJ, Thunnissen AMWH, Feringa BL, Janssen DB, Poelarends GJ (2012), Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids. Nature Chemistry 4(6): 478-484.

Last modified:04 July 2017 10.12 a.m.