Psychrophilic enzymes: from folding to function and biotechnology

G Feller - Scientifica, 2013 - Wiley Online Library
Psychrophiles thriving permanently at near‐zero temperatures synthesize cold‐active
enzymes to sustain their cell cycle. Genome sequences, proteomic, and transcriptomic …

Enzymes from piezophiles

T Ichiye - Seminars in cell & developmental biology, 2018 - Elsevier
The discovery of microbial communities in extreme conditions that would seem hostile to life
leads to the question of how the molecules making up these microbes can maintain their …

Unraveling the role of protein dynamics in dihydrofolate reductase catalysis

LYP Luk, J Javier Ruiz-Pernia, WM Dawson… - Proceedings of the …, 2013 - pnas.org
Protein dynamics have controversially been proposed to be at the heart of enzyme catalysis,
but identification and analysis of dynamical effects in enzyme-catalyzed reactions have …

Distinctive microbial community structure in highly stratified deep-sea brine water columns

S Bougouffa, JK Yang, OO Lee, Y Wang… - Applied and …, 2013 - journals.asm.org
Atlantis II and Discovery are two hydrothermal and hypersaline deep-sea pools in the Red
Sea rift that are characterized by strong thermohalo-stratification and temperatures steadily …

Protein motions and dynamic effects in enzyme catalysis

LYP Luk, EJ Loveridge, RK Allemann - Physical Chemistry Chemical …, 2015 - pubs.rsc.org
The role of protein motions in promoting the chemical step of enzyme catalysed reactions
remains a subject of considerable debate. Here, a unified view of the role of protein …

Thermal adaptation of enzymes: impacts of conformational shifts on catalytic activation energy and optimum temperature

I Maffucci, D Laage, F Sterpone… - … –A European Journal, 2020 - Wiley Online Library
Thermal adaptation of enzymes is essential for both living organism development in extreme
conditions and efficient biocatalytic applications. However, the molecular mechanisms …

Chemical ligation and isotope labeling to locate dynamic effects during catalysis by dihydrofolate reductase

LYP Luk, JJ Ruiz‐Pernía, AS Adesina… - Angewandte …, 2015 - Wiley Online Library
Chemical ligation has been used to alter motions in specific regions of dihydrofolate
reductase from E. coli and to investigate the effects of localized motional changes on …

Pressure dependence of activity and stability of dihydrofolate reductases of the deep-sea bacterium Moritella profunda and Escherichia coli

E Ohmae, C Murakami, S Tate, K Gekko, K Hata… - … et Biophysica Acta (BBA …, 2012 - Elsevier
To understand the pressure-adaptation mechanism of deep-sea enzymes, we studied the
effects of pressure on the enzyme activity and structural stability of dihydrofolate reductase …

Differences in thermal structural changes and melting between mesophilic and thermophilic dihydrofolate reductase enzymes

I Maffucci, D Laage, G Stirnemann… - Physical Chemistry …, 2020 - pubs.rsc.org
A key aspect of life's evolution on Earth is the adaptation of proteins to be stable and work in
a very wide range of temperature conditions. A detailed understanding of the associated …

The role of large-scale motions in catalysis by dihydrofolate reductase

EJ Loveridge, LH Tey, EM Behiry… - Journal of the …, 2011 - ACS Publications
Dihydrofolate reductase has long been used as a model system to study the coupling of
protein motions to enzymatic hydride transfer. By studying environmental effects on hydride …