Genomes and Genes
Experts and Doctors on catalytic domain in Oulu, Northern Ostrobothnia, Finland
Locale: Oulu, Northern Ostrobothnia, Finland
Topic: catalytic domain
- 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. ..
- 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. ..
- 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...
- 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...
- 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. ..
- 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. ..
- 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...
- 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. ..
- 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. ..