Markus Alahuhta

Research Scientist

Photo of Markus Alahuhta
(303) 384-7850
At NREL Since: 

Markus Alahuhta received his Ph.D. in Biochemistry and Protein X-ray Crystallography from the University of Oulu, Department of Biochemistry, Finland. Under the guidance of Professor Rik Wierenga in the Structural Enzymology Group, Dr. Alahuhta studied the monomeric variants of triosephosphate isomerase in the context of a structure-based protein-engineering project aimed at changing the substrate specificity. This project included solving multiple structures of different engineered variants, planning of mutations, and sub-angstrom resolution X-ray diffraction studies of the proton-transfer mechanisms of triosephosphate isomerase.

Dr. Alahuhta joined NREL in August 2008 in the group of Dr. Mike Himmel. His main interest lies in solving structures of cellulose degrading and binding enzymes together with Dr. Vladimir Lunin to better understand their function and how they could be improved through structure-based engineering. This research targets both fungal and bacterial proteins. His recent publications have focused on the function of bacterial cellulosomal enzyme complexes.

Selected Publications 

  1. Alahuhta, M.; Xu, Q.; Bomble, Y.J.; Brunecky, R.; Adney, W.S.; Ding, S-Y.; Himmel, M.E.; Lunin, V.V. (2010). "The Unique Binding Mode of Cellulosomal CBM4 from Clostridium thermocellum Cellobiohydrolase." A. J. Mol. Biol. (402); pp. 374-387.
  2. Alahuhta, M.; Xu, Q.; Brunecky, R.; Adney, W.S.; Ding, S-Y.; Himmel, M.E.; Lunin, V.V. (2010). "Structure of a fibronectin type III-like module from Clostridium thermocellum." Acta Cryst. (33333); pp. 878-880.
  3. Alahuhta, M.; Wierenga, R.K. (2010). "Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: New insight in the proton transfer reaction mechanism." PROTEINS (78); pp. 1878-1888.
  4. Alahuhta, M.; Salin, M.; Casteleijn, M.G.; Kemmer, K.; El Sayed, I.; Augustyns, K.; Neubauer, P.; Wierenga, R.K. (2008). "Structure-based protein engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating a competent active site." Prot. Eng. Des. Sel (21); pp. 257-266.
  5. Casteleijn, M.G.; Alahuhta, M.; Groebel. K.; El Sayed, I.; Augustyns, K.; Lambeir, A.M.; Neubauer, P.; Wierenga, R.K. (2006). "Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase." Biochemistry (45); pp. 15483-15494.
  6. Alahuhta, M.; Luo, Y.; Ding, S-Y.; Himmel, M.E.; Lunin, V.V. (2011). "Structure of CBM4 from Clostridium thermocellum cellulase K." Acta Cryst. F (67); pp. 527-530.