Institute of Biotechnology and Department of Biological and Environmental Sciences, University of Helsinki, Helsinki
The Human UDP-Glucuronosyltransferases: Studies on Substrate Binding and Catalytic Mechanism
Professor Risto Juvonen, Department of Pharmacology and Toxicology, University of Kuopio, Finland
Docent Tuomas Haltia, Department of Biological and Environmental Sciences, University of Helsinki, Finland
Professor Michael W. H. Coughtrie, Biochemical Pharmacology,
Division of Molecular and Translational Medicine, Ninewells Hospital
and Medical School, University of Dundee
Professor Carl G. Gahmberg, Department of Biological and Environmental Sciences, University of Helsinki, Finland
- Kurkela M, Patana AS, Mackenzie PI, Court MH, Tate CG, Hirvonen J, Goldman A & Finel M. (2007) Interactions with other human UDP-glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6. Pharmacogenet Genomics. 17:115-26.
- Patana AS, Kurkela M, Goldman A & Finel M. (2007) The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site. Mol Pharmacol. 72:604-11.
- Xiong Y, Patana AS, Miley MJ, Zielinska AK, Bratton SM, Miller GP, Goldman A, Finel M, Redinbo MR & Radominska-Pandya A. (2008) The first aspartic acid of the DQxD motif for human UDP-glucuronosyltransferase 1A10 interacts with UDP-glucuronic acid during catalysis. Drug Metab Dispos. 36:517-22.
- Patana A-S, Kurkela M, Finel M & Goldman A. (2008) Mutation analysis in UGT1A9 suggests a relationship between substrate and catalytic residues in UDP-glucuronosyltransferases. PEDS. 21:537-43.