Experts and Doctors on catalytic domain in Oulu, Northern Ostrobothnia, Finland


Locale: Oulu, Northern Ostrobothnia, Finland
Topic: catalytic domain

Top Publications

  1. Haikarainen T, Venkannagari H, Narwal M, Obaji E, Lee H, Nkizinkiko Y, et al. Structural basis and selectivity of tankyrase inhibition by a Wnt signaling inhibitor WIKI4. PLoS ONE. 2013;8:e65404 pubmed publisher
    ..Our results form a structural basis for further development of potent and selective tankyrase inhibitors based on the WIKI4 scaffold. ..
  2. Lehtiö L, Chi N, Krauss S. Tankyrases as drug targets. FEBS J. 2013;280:3576-93 pubmed publisher
    ..A highly potent dual-site inhibitor is also available. Within the last few years, tankyrase inhibitors have proved to be useful chemical probes and potential lead compounds, especially for specific cancers. ..
  3. Alahuhta M, Wierenga R. Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanism. Proteins. 2010;78:1878-88 pubmed publisher
    ..The new findings are discussed in the context of the current knowledge of the TIM reaction mechanism. ..
  4. Soini Y, Karihtala P, Mantyniemi A, Turunen N, Paakko P, Kinnula V. Glutamate-L-cysteine ligase in breast carcinomas. Histopathology. 2004;44:129-35 pubmed
    ..Even though the overall expression of GLCL was associated with improved survival, no such effect was observed separately in the group receiving chemotherapy. ..
  5. Sharma S, Bhaumik P, Schmitz W, Venkatesan R, Hiltunen J, Conzelmann E, et al. The enolization chemistry of a thioester-dependent racemase: the 1.4 Å crystal structure of a reaction intermediate complex characterized by detailed QM/MM calculations. J Phys Chem B. 2012;116:3619-29 pubmed publisher
    ..7 Å of the chiral C2-carbon, with smaller shifts (approximately 1 Å) of the carbon atom of the 2-methyl group, the C3-atom of the fatty acid tail, and the C1-carbon and O1-oxygen atoms of the thioester moiety. ..
  6. Haikarainen T, Waaler J, Ignatev A, Nkizinkiko Y, Venkannagari H, Obaji E, et al. Development and structural analysis of adenosine site binding tankyrase inhibitors. Bioorg Med Chem Lett. 2016;26:328-333 pubmed publisher
    ..The structural analysis allows further rational development of this compound class as a potent and selective tankyrase inhibitor. ..
  7. Holster T, Pakkanen O, Soininen R, Sormunen R, Nokelainen M, Kivirikko K, et al. Loss of assembly of the main basement membrane collagen, type IV, but not fibril-forming collagens and embryonic death in collagen prolyl 4-hydroxylase I null mice. J Biol Chem. 2007;282:2512-9 pubmed
    ..The primary cause of death of the null embryos was thus most likely an abnormal assembly of collagen IV. ..
  8. Alanen H, Salo K, Pirneskoski A, Ruddock L. pH dependence of the peptide thiol-disulfide oxidase activity of six members of the human protein disulfide isomerase family. Antioxid Redox Signal. 2006;8:283-91 pubmed
    ..In the light of this data potential differential functions for these enzymes are discussed. ..
  9. Saaranen M, Salo K, Latva Ranta M, Kinnula V, Ruddock L. The C-terminal active site cysteine of Escherichia coli glutaredoxin 1 determines the glutathione specificity of the second step of peptide deglutathionylation. Antioxid Redox Signal. 2009;11:1819-28 pubmed publisher
    ..coli Grx1 for glutathione over the corresponding tripeptide Glu-Cys-Gly, which has a normal peptide bond linking Glu-Cys instead of the gamma-linkage present in glutathione, in the second step of deglutathionylation. ..

More Information


  1. Karala A, Ruddock L. Bacitracin is not a specific inhibitor of protein disulfide isomerase. FEBS J. 2010;277:2454-62 pubmed publisher
    ..These results suggest that the use of bacitracin as a specific inhibitor of PDI in cellular systems requires urgent re-evaluation. ..
  2. Myllykoski M, Raasakka A, Han H, Kursula P. Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand binding and molecular conformation. PLoS ONE. 2012;7:e32336 pubmed publisher
    ..Our results provide a detailed picture of the CNPase active site during its catalytic cycle, and suggest a specific function for the previously uncharacterized N-terminal domain. ..
  3. Wierenga R, Kapetaniou E, Venkatesan R. Triosephosphate isomerase: a highly evolved biocatalyst. Cell Mol Life Sci. 2010;67:3961-82 pubmed publisher
    ..Two proton shuttling mechanisms, the classical and the criss-cross mechanism, are responsible for the interconversion of the substrates of this enolising enzyme...
  4. Venkatesan R, Wierenga R. Structure of mycobacterial ?-oxidation trifunctional enzyme reveals its altered assembly and putative substrate channeling pathway. ACS Chem Biol. 2013;8:1063-73 pubmed publisher
    ..Our studies highlight the molecular properties of mtTFE, significantly extending the structural knowledge on this type of very interesting multifunctional enzymes...
  5. Mehtälä M, Lensink M, Pietikäinen L, Hiltunen J, Glumoff T. On the molecular basis of D-bifunctional protein deficiency type III. PLoS ONE. 2013;8:e53688 pubmed publisher
    ..Structure-function considerations of the variant proteins matched well with the available data of the patients. ..
  6. Kasaragod P, Schmitz W, Hiltunen J, Wierenga R. The isomerase and hydratase reaction mechanism of the crotonase active site of the multifunctional enzyme (type-1), as deduced from structures of complexes with 3S-hydroxy-acyl-CoA. FEBS J. 2013;280:3160-75 pubmed publisher
    ..The structural variability of loop-2 between MFE1 and its monofunctional homologues correlates with differences in the respective substrate preferences and catalytic rates. ..
  7. Meriläinen G, Poikela V, Kursula P, Wierenga R. The thiolase reaction mechanism: the importance of Asn316 and His348 for stabilizing the enolate intermediate of the Claisen condensation. Biochemistry. 2009;48:11011-25 pubmed publisher
    ..Cys89, Asn316, and His348 form the CNH-catalytic triad of the thiolase superfamily. Our findings are also discussed in the context of the importance of this triad for the catalytic mechanism of other enzymes of the thiolase superfamily...
  8. Chen Z, Pudas R, Sharma S, Smart O, Juffer A, Hiltunen J, et al. Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties. J Mol Biol. 2008;379:830-44 pubmed publisher
    ..Furthermore, the kinetic analysis of the wild-type MECR/ETR1 shows a bimodal distribution of catalytic efficiencies, in agreement with the notion that two major products are generated by the mitochondrial FAS II pathway. ..
  9. Raasakka A, Myllykoski M, Laulumaa S, Lehtimäki M, Härtlein M, Moulin M, et al. Determinants of ligand binding and catalytic activity in the myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase. Sci Rep. 2015;5:16520 pubmed publisher
  10. Kursula P, Sikkilä H, Fukao T, Kondo N, Wierenga R. High resolution crystal structures of human cytosolic thiolase (CT): a comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS I. J Mol Biol. 2005;347:189-201 pubmed
    ..The second oxyanion hole is in both structures shaped by corresponding main chain peptide NH-groups. The possible importance of bound water molecules at the catalytic site of thiolase for the reaction mechanism is discussed. ..