Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum.
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TLDR
Structural comparison of Aa MDH and Tf MDH suggests that the increased relative flexibility of active site residues, favorable surface charge distribution for substrate and cofactor, and the reduced intersubunit ion pair interactions may be the major factors for the efficient catalytic activity of A a MDH at low temperatures.About:
This article is published in Journal of Biological Chemistry.The article was published on 1999-04-23 and is currently open access. It has received 176 citations till now. The article focuses on the topics: Malate dehydrogenase.read more
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Journal ArticleDOI
Psychrophilic enzymes: Hot topics in cold adaptation
Georges Feller,Charles Gerday +1 more
TL;DR: The ability to thrive at temperatures that are close to, or below, the freezing point of water requires a vast array of adaptations to maintain the metabolic rates and sustained growth compatible with life in these severe environmental conditions.
Journal ArticleDOI
Cold-adapted enzymes.
TL;DR: This review addresses the structure, function, and stability of cold-adapted enzymes, highlighting the challenges for immediate and future consideration.
Journal ArticleDOI
Cold-adapted enzymes: from fundamentals to biotechnology.
Charles Gerday,M. Aittaleb,Mostafa Bentahir,Jean-Pierre Chessa,Paule Claverie,Tony Collins,Salvino D'Amico,Joëlle Dumont,Geneviève Garsoux,Daphné Georlette,Anne Hoyoux,Thierry G. A. Lonhienne,Marie-Alice Meuwis,Georges Feller +13 more
TL;DR: Using X-ray crystallography,Psychrophilic enzymes produced by cold-adapted microorganisms display a high catalytic efficiency and are most often, if not always, associated with high thermosensitivity.
Journal ArticleDOI
C-h⋯π-interactions in proteins
TL;DR: A non-redundant set of 1154 protein structures from the Protein Data Bank was examined with respect to close interactions between C-H-donor and pi-acceptor groups as mentioned in this paper.
Journal ArticleDOI
Extremophiles as a source for novel enzymes.
TL;DR: Novel developments in the cultivation and production of extremophiles, but also developments related to the cloning and expression of their genes in heterologous hosts, will increase the number of enzyme-driven transformations in chemical, food, pharmaceutical and other industrial applications.
References
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Crystallographic R Factor Refinement by Molecular Dynamics
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