Anne-Sisko Patana

6.2.2009
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

Reviewers:

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

Opponent:

Professor Michael W. H. Coughtrie, Biochemical Pharmacology, Division of Molecular and Translational Medicine, Ninewells Hospital and Medical School, University of Dundee

Custos:

Professor Carl G. Gahmberg, Department of Biological and Environmental Sciences, University of Helsinki, Finland

Publications:

  1. 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.
  2. 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.
  3. 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.
  4. 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.