T
Tapani Reinikainen
Researcher at VTT Technical Research Centre of Finland
Publications - 39
Citations - 3044
Tapani Reinikainen is an academic researcher from VTT Technical Research Centre of Finland. The author has contributed to research in topics: Trichoderma reesei & Cellulase. The author has an hindex of 24, co-authored 39 publications receiving 2945 citations. Previous affiliations of Tapani Reinikainen include École Polytechnique Fédérale de Lausanne.
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Journal ArticleDOI
The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei.
Christina Divne,Jerry Ståhlberg,Tapani Reinikainen,Laura Ruohonen,Göran Pettersson,J. Knowles,TT Teeri,T.A. Jones +7 more
TL;DR: The structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined and refined and may account for many of the previously poorly understood macroscopic properties of the enzyme and its interaction with solid cellulose.
Journal ArticleDOI
The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes.
Gerard J. Kleywegt,J.-Y. Zou,Christina Divne,Gideon J. Davies,Irmgard Sinning,Jerry Ståhlberg,Tapani Reinikainen,M Srisodsuk,Tuula T. Teeri,T.A. Jones +9 more
TL;DR: Comparison of the structure of EG I with several related enzymes reveals structural similarities, and differences that relate to their biological function in degrading particular substrates, and a possible structural explanation of the drastically different pH profiles of T. reesei and H. insolens EG I is proposed.
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Identification of functionally important amino acids in the cellulose-binding domain of Trichoderma reesei cellobiohydrolase I.
Markus Linder,Maija-Liisa Mattinen,Maarit Kontteli,Gunnar Lindeberg,Jerry Ståhlberg,Torbjörn Drakenberg,Tapani Reinikainen,Göran Pettersson,Arto Annila +8 more
TL;DR: It was found that at least two tyrosine residues and a glutamine residue on the flat face were essential for tight binding of the CBD to cellulose, although in some cases decreased binding could clearly be ascribed to conformational perturbations.
Journal ArticleDOI
Investigation of the function of mutated cellulose-binding domains of Trichoderma reesei cellobiohydrolase I.
Tapani Reinikainen,Laura Ruohonen,Tarja K. Nevanen,Leif Laaksonen,P. J. Kraulis,T. Alwyn Jones,Jonathan Knowles,Tuula T. Teeri +7 more
TL;DR: The hypothesis that both surfaces of the CBD are involved in the interaction of the binding domain with crystalline cellulose is supported, suggesting that the interaction with the pyranose ring of the substrate with an aromatic side chain is important.
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Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose.
TL;DR: It is evident that the presence of a functional CBD is increasingly important for CBH I toward higher enzyme to cellulose ratios and the putative hinge removed by the first deletion facilitates CBD-driven binding and dense packing of the wild type enzyme on the cellulose surface.