P. Väljamäe

发表

Synergistic cellulose hydrolysis can be described in terms of fractal‐like kinetics

Göran Pettersson, G. Pettersson, G. Johansson, 2003, Biotechnology and bioengineering.

Mechanism of substrate inhibition in cellulose synergistic degradation.

G. Pettersson, G. Johansson, P. Väljamäe, 2001, European journal of biochemistry.

When substrate inhibits and inhibitor activates: implications of β-glucosidases

P. Väljamäe, Silja Kuusk, Priit Väljamäe, 2017, Biotechnology for Biofuels.

Kinetic Characterization of a Putatively Chitin-Active LPMO Reveals a Preference for Soluble Substrates and Absence of Monooxygenase Activity

V. Eijsink, M. Sørlie, D. Petrović, 2021, ACS catalysis.

Enzyme processivity changes with the extent of recalcitrant polysaccharide degradation

M. Sørlie, P. Väljamäe, Silje B Lorentzen, 2014, FEBS letters.

Kinetics of H2O2-driven catalysis by a lytic polysaccharide monooxygenase from the fungus Trichoderma reesei

P. Väljamäe, Silja Kuusk, 2021, The Journal of biological chemistry.

Kinetic insights into the role of the reductant in H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase

V. Eijsink, M. Sørlie, P. Väljamäe, 2018, The Journal of Biological Chemistry.

Slow Off-rates and Strong Product Binding Are Required for Processivity and Efficient Degradation of Recalcitrant Chitin by Family 18 Chitinases*

M. Sørlie, P. Väljamäe, P. Kuusk, 2015, The Journal of Biological Chemistry.

The Predominant Molecular State of Bound Enzyme Determines the Strength and Type of Product Inhibition in the Hydrolysis of Recalcitrant Polysaccharides by Processive Enzymes*

M. Sørlie, P. Väljamäe, Silja Kuusk, 2015, The Journal of Biological Chemistry.

H2O2 in Liquid Fractions of Hydrothermally Pretreated Biomasses: Implications of Lytic Polysaccharide Monooxygenases

K. Niemelä, Ville Pihlajaniemi, P. Väljamäe, 2021, ACS Sustainable Chemistry & Engineering.

The liquid fraction from hydrothermal pretreatment of wheat straw provides lytic polysaccharide monooxygenases with both electrons and H2O2 co-substrate

J. Büchs, V. Eijsink, N. Aro, 2019, Biotechnology for Biofuels.

Selecting β-glucosidases to support cellulases in cellulose saccharification

P. Väljamäe, Priit Väljamäe, Hele Teugjas, 2013, Biotechnology for Biofuels.

Processivity of Cellobiohydrolases Is Limited by the Substrate*

P. Väljamäe, Mihhail Kurašin, Priit Väljamäe, 2010, The Journal of Biological Chemistry.

A pyranose dehydrogenase-based biosensor for kinetic analysis of enzymatic hydrolysis of cellulose by cellulases.

M. Toscano, K. Jensen, P. Westh, 2014, Enzyme and microbial technology.

Thermodynamic Relationships with Processivity in Serratia marcescens Family 18 Chitinases.

Christina M. Payne, G. Mathiesen, M. Sørlie, 2015, The journal of physical chemistry. B.

Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

V. Eijsink, P. Väljamäe, Bastien Bissaro, 2020, Nature Communications.

The dissociation mechanism of processive cellulases

J. Ståhlberg, M. Crowley, G. Beckham, 2019, Proceedings of the National Academy of Sciences.

Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate

Göran Pettersson, G. Pettersson, G. Johansson, 2004, Biotechnology and Bioengineering.

Endo-exo Synergism in Cellulose Hydrolysis Revisited*

P. Väljamäe, Mihhail Kurašin, Hele Teugjas, 2012, The Journal of Biological Chemistry.

Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis

P. Väljamäe, Jürgen Jalak, Priit Väljamäe, 2010, Biotechnology and bioengineering.

Enzyme kinetics by GH7 cellobiohydrolases on chromogenic substrates is dictated by non‐productive binding: insights from crystal structures and MD simulation

Christina M. Payne, Japheth E. Gado, J. Ståhlberg, 2022, The FEBS journal.

Reducing end-specific fluorescence labeled celluloses for cellulase mode of action

P. Väljamäe, Hele Teugjas, Riin Velleste, 2010 .

Surface character of pulp fibres studied using endoglucanases.

L. Hildén, G. Johansson, P. Väljamäe, 2005, Journal of biotechnology.

Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as 'burst' kinetics on fluorescent polymeric model substrates.

G. Johansson, P. Väljamäe, Kalle Kipper, 2005, The Biochemical journal.

The kinetics of cellulose enzymatic hydrolysis Implications of the synergism between enzymes

P. Väljamäe, Priit Väljamäe, 2002 .

The kinetics of cellulose enzymatic hydrolysis

P. Väljamäe, Priit Väljamäe, 2002 .

Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I.

G. Pettersson, G. Johansson, P. Väljamäe, 1999, European journal of biochemistry.

Kinetics of H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase

V. Eijsink, Zarah Forsberg, M. Sørlie, 2017, The Journal of Biological Chemistry.

Measuring processivity.

V. Eijsink, S. Horn, K. Vårum, 2012, Methods in enzymology.

Product inhibition of cellulases studied with 14C-labeled cellulose substrates

P. Väljamäe, Priit Väljamäe, Hele Teugjas, 2013, Biotechnology for Biofuels.

Kinetics of H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase.

V. Eijsink, Zarah Forsberg, M. Sørlie, 2018, The Journal of Biological Chemistry.

Capillary electrophoretic monitoring of hydrothermal pre-treatment and enzymatic hydrolysis of willow: Comparison with HPLC and NMR

M. Vaher, M. Kaljurand, M. Koel, 2012 .

The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface-erosion model.

G. Pettersson, G. Johansson, P. Väljamäe, 1998, European journal of biochemistry.

Yeast mitochondrial DNA polymerase is a highly processive single-subunit enzyme.

J. Sedman, P. Väljamäe, Katrin Viikov, 2011, Mitochondrion.

Anomeric Selectivity and Product Profile of a Processive Cellulase.

Johan P. Olsen, P. Westh, K. Borch, 2017, Biochemistry.

Human Chitotriosidase Is an Endo-Processive Enzyme

M. Sørlie, P. Väljamäe, Silja Kuusk, 2017, PloS one.

Multi-Mode Binding of Cellobiohydrolase Cel7A from Trichoderma reesei to Cellulose

P. Väljamäe, Jürgen Jalak, Priit Väljamäe, 2014, PloS one.

Thermodynamic Signatures of Substrate Binding for Three Thermobifida fusca Cellulases with Different Modes of Action.

Christina M. Payne, M. Sørlie, P. Väljamäe, 2019, Biochemistry.

Strong cellulase inhibitors from the hydrothermal pretreatment of wheat straw

P. Väljamäe, Riin Kont, Mihhail Kurašin, 2013, Biotechnology for Biofuels.

Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A*

P. Westh, K. Borch, P. Väljamäe, 2016, The Journal of Biological Chemistry.