A5034388372- Enzyme Production and Characterization
- Enzyme Structure and Function
- Biofuel production and bioconversion
- Enzyme Catalysis and Immobilization
- Enzyme-mediated dye degradation
- Carbohydrate Chemistry and Synthesis
- Amino Acid Enzymes and Metabolism
- Food Allergy and Anaphylaxis Research
- Protein Structure and Dynamics
- Allergic Rhinitis and Sensitization
- Glycosylation and Glycoproteins Research
- Monoclonal and Polyclonal Antibodies Research
- Diet, Metabolism, and Disease
- Lysosomal Storage Disorders Research
- Mass Spectrometry Techniques and Applications
- Contact Dermatitis and Allergies
- Microbial Metabolic Engineering and Bioproduction
- Biochemical and Molecular Research
- melanin and skin pigmentation
- Microbial Metabolism and Applications
- Microbial Metabolites in Food Biotechnology
- Chemical Synthesis and Analysis
- Metal-Catalyzed Oxygenation Mechanisms
- Protein purification and stability
- Studies on Chitinases and Chitosanases
University of Eastern Finland
2016-2025
Finland University
2013-2023
Uppsala University
1990-2009
Joensuu Science Park
1991-2004
University of Warwick
2004
University of Graz
2004
University of Helsinki
1988-1998
Institute for Molecular Medicine Finland
1996
The enzymatic degradation of cellulose is an important process, both ecologically and commercially. three-dimensional structure a cellulase, the core CBHII from fungus Trichoderma reesei reveals α-β protein with fold similar to but different widely occurring barrel topology first observed in triose phosphate isomerase. active site located at carboxyl-terminal end parallel β barrel, enclosed tunnel through which threads. Two aspartic acid residues, center are probable catalytic residues.
CAZypedia was initiated in 2007 to create a comprehensive, living encyclopedia of the carbohydrate-active enzymes (CAZymes) and associated carbohydrate-binding modules involved synthesis, modification degradation complex carbohydrates. is closely connected with actively curated CAZy database, which provides sequence-based foundation for biochemical, mechanistic structural characterization these diverse proteins. Now celebrating its 10th anniversary online, successful example dynamic,...
Abstract The Ntn‐hydrolases (N‐terminal nucleophile) are a superfamily of diverse enzymes that has recently been characterized. All the proteins in this family activated autocatalytically; they contain an N‐terminally located catalytic nucleophile, and cleave amide bond. In present study, structures four compared more detail. Although amino acid sequence homology is almost completely absent, share similar αββα‐core structure. central β‐sheets core were found to have different packing angles,...
Hydrophobins are proteins specific to filamentous fungi. have several important roles in fungal physiology, for example, adhesion, formation of protective surface coatings, and the reduction tension water, which allows growth aerial structures. show remarkable biophysical properties, they most powerful surface-active known. To this point molecular basis function group has been largely unknown. We now determined crystal structure hydrophobin HFBII from Trichoderma reesei at 1.0 A resolution....
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructural Comparison of Two Major endo-1,4-Xylanases from Trichoderma reeseiAnneli Torronen and Juha RouvinenCite this: Biochemistry 1995, 34, 3, 847–856Publication Date (Print):January 1, 1995Publication History Published online1 May 2002Published inissue 1 January 1995https://pubs.acs.org/doi/10.1021/bi00003a019https://doi.org/10.1021/bi00003a019research-articleACS PublicationsRequest reuse permissionsArticle Views661Altmetric-Citations169LEARN...
The crystal structures of thermophilic xylanases from Chaetomium thermophilum and Nonomuraea flexuosa were determined at 1.75 2.1 A resolution, respectively. Both enzymes have the overall fold typical to family 11 with two highly twisted beta-sheets forming a large cleft. comparison 12 both mesophilic organisms showed that different are very similar. sequence identity differences correlated well structural differences. Several minor modifications appeared be responsible for increased thermal...
Hydrophobins are small fungal proteins that highly surface active and possess a unique ability to form amphiphilic membranes through spontaneous self-assembly. The first crystal structure of hydrophobin, Trichoderma reesei HFBII, revealed the structural basis for function this protein--a patch consisting hydrophobic side chains on protein surface. Here, structures native variant T. hydrophobin HFBI presented, revealing same overall functional as in HFBII structure. However, some flexibility...
Twelve members of the family 11 xylanases, including both mesophilic and thermophilic proteins, were studied using molecular dynamics (MD). Simulations xylanases carried out in an explicit water environment at four different temperatures, 300, 400, 500 600 K. A difference thermotolerance between became clear: endured heat higher simulation temperatures better than ones. The unfolding pathways seemed to be similar for all simulations regardless protein. initiates N-terminal region or...
Background Narcolepsy results from immune-mediated destruction of hypocretin secreting neurons in hypothalamus, however the triggers and disease mechanisms are poorly understood. Vaccine-attributable risk narcolepsy reported so far with AS03 adjuvanted H1N1 vaccination Pandemrix has been manifold compared to Arepanrix, which contained differently produced viral antigen preparation. Hence, antigenic differences antibody response these vaccines were investigated. Methods Findings Increased...
Trichoderma reesei cellobiohydrolase Cel6A (formerly CBHII) has a tunnel shaped active site with four internal subsites for the glucose units. We have predicted an additional ring stacking interaction sixth moiety tryptophan residue (W272) found on domain surface. Mutagenesis of this selectively impairs enzyme function crystalline cellulose but not soluble or amorphous substrates. Our data shows that W272 forms subsite at entrance and suggests it specialised role in degradation, possibly...
Phytic acid (myo-inositol hexakisphosphate, InsP(6)) hydrolysis by Bacillus phytase (PhyC) was studied. The enzyme hydrolyses only three phosphates from phytic acid. Moreover, the seems to prefer of every second phosphate over that adjacent ones. Furthermore, it is very likely has two alternative pathways for acid, resulting in different myo-inositol trisphosphate end products: Ins(2,4,6)P(3) and Ins(1,3,5)P(3). These results, together with inhibition studies fluoride, vanadate, substrate a...
Although knowledge of the IgE cross-reactivity between allergens is important for understanding mechanisms allergy, regulation allergic immune response and development efficient modes allergen immunotherapy, animal poorly known.The aim this study was to characterize cross-reactivities lipocalin proteins, including five animal-derived one human endogenous lipocalin, tear (TL).The recombinant proteins were validated by chromatography mass spectrometry. The IgE-binding capacity confirmed IgE....
Laccases are copper-containing enzymes used in various applications, such as textile bleaching. Several crystal structures of laccases from fungi and bacteria available, but ascomycete types fungal (asco-laccases) have been rather unexplored, to date only the structure Melanocarpus albomyces laccase (MaL) has published. We now solved another asco-laccase, Thielavia arenaria (TaLcc1), at 2.5 Å resolution. The loops near T1 copper, forming substrate-binding pockets two asco-laccases, differ...
The C-terminus of the fungal laccase from Melanocarpus albomyces (MaL) is processed during secretion at a processing site conserved among ascomycete laccases. three-dimensional structure MaL has been solved as one first complete structures. According to crystal MaL, four C-terminal amino acids mature protein penetrate into tunnel leading towards trinuclear site. carboxylate group forms hydrogen bond with side chain His140, which also coordinates type 3 copper. In order analyze role...
Crystal structures of native and α‐ d ‐galactose‐bound Bacillus circulans sp. alkalophilus β‐galactosidase (Bca‐β‐gal) were determined at 2.40 2.25 Å resolutions, respectively. Bca‐β‐gal is a member family 42 glycoside hydrolases, forms 460 kDa hexameric structure in crystal. The protein consists three domains, which the catalytic domain has an (α/β) 8 barrel with cluster sulfur‐rich residues inside β‐barrel. shape active site clearly more open compared to only homologous available Protein...