Priit Väljamäe

发表

Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis

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

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

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

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

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

Human Chitotriosidase Is an Endo-Processive Enzyme

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

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.

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.

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.

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

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

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.

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.

Strong cellulase inhibitors from the hydrothermal pretreatment of wheat straw

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

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

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

Selecting β-glucosidases to support cellulases in cellulose saccharification

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

Endo-exo Synergism in Cellulose Hydrolysis Revisited*

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

Processivity of Cellobiohydrolases Is Limited by the Substrate*

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

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.

Measuring processivity.

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

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.

Enzyme processivity changes with the extent of recalcitrant polysaccharide degradation

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

The dissociation mechanism of processive cellulases

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

Thermodynamic Relationships with Processivity in Serratia marcescens Family 18 Chitinases.

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

The kinetics of cellulose enzymatic hydrolysis

P. Väljamäe, Priit Väljamäe, 2002 .

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

P. Väljamäe, Priit Väljamäe, 2002 .

Dye-decolorizing peroxidase of Thermobifida halotolerance displays complex kinetics with both substrate inhibition and apparent positive cooperativity.

Hegne Pupart, Priit Väljamäe, Tiit Lukk, 2024, Archives of biochemistry and biophysics.

Dye-Decolorizing Peroxidase of Streptomyces coelicolor (ScDyPB) Exists as a Dynamic Mixture of Kinetically Different Oligomers

Hegne Pupart, Priit Väljamäe, Tiit Lukk, 2024, ACS omega.

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

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

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.

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.

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.