J
Jukka Vidgren
Researcher at Orion Corporation
Publications - 14
Citations - 1902
Jukka Vidgren is an academic researcher from Orion Corporation. The author has contributed to research in topics: Enzyme & Active site. The author has an hindex of 10, co-authored 14 publications receiving 1843 citations. Previous affiliations of Jukka Vidgren include Lund University.
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Journal ArticleDOI
Kinetics of human soluble and membrane-bound catechol O-methyltransferase: a revised mechanism and description of the thermolabile variant of the enzyme.
Timo Lotta,Jukka Vidgren,Carola Tilgmann,I. Ulmanen,Krister Melén,Ilkka Julkunen,Jyrki Taskinen +6 more
TL;DR: Comparison of velocity parameters, substrate selectivity, and regioselectivity of the methylation of both enzyme forms, and a revised mechanism for the reaction cycle are discussed.
Journal ArticleDOI
Crystal structure of catechol O-methyltransferase
TL;DR: The atomic structure of COMT is solved to 2.0 Å resolution, which provides new insights into the mechanism of the methyl transfer reaction, and the co-enzyme-binding domain is strikingly similar to that of an AdoMet-dependent DNA methylase10, indicating that all Ado met methylases may have a common structure.
Journal ArticleDOI
Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-.
TL;DR: A complex of carbonic anhydrase (CA) with one of its substrates, bicarbonate, has been studied crystallographically and the importance of residues Thr‐199 and Glu‐106 in controlling the binding orientation of HCO 3− is discussed as well as the catalytic mechanism.
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Refined structure of the acetazolamide complex of human carbonic anhydrase II at 1.9 Å
TL;DR: The binding of acetazolamide to human carbonic anhydrase II (HCA II) has been investigated by X-ray crystallography and the bound inhibitor is clearly resolved in the active site of the enzyme.
Journal ArticleDOI
Refined structure of the aminobenzolamide complex of human carbonic anhydrase II at 1.9 A and sulphonamide modelling of bovine carbonic anhydrase III.
TL;DR: The binding of aminobenzolamide to human carbonic anhydrase (HCA II) has been investigated by X-ray crystallography and it was evident that Phe 198 prevents an optimal interaction with sulphonamides.