An Overview on Thermal Adaptation of Esterases and Lipases Belonging to the HSL Family: New Insight on the Computational Analysis
The molecular mechanisms of adaptation to the environment of an organism are reflected on different levels, with regards to DNA, genes and proteins expression, which are intrinsically adapted to the particular physical/chemical state.
Amino acid composition is strictly related to environmental adaptation and, in this review, we present an up to date overview on thermal adaptation of esterases and lipases belonging to the HSL family. In particular, we discuss results obtained by different analyses on these enzymes and we re-analyze them from a statistical standpoint.
Keywords: Archaea; Archaeoglobus fulgidus; Bacillus subtilis; Bacteria; Carboxylesterase; Esterase; Eukarya; HSL family; HSL-like group; Lactobacillus plantarum; Lipases; Psychrophilic enzymes; Rhodococcus; Staphylococcus aureans; X-ray crystal structures; abyssal ocean; alanine; alpine regions; applications in biotechnology; biocatalyst; biophysical studies; cap-domain; cholinesterases; cold ecosystems; computational analysis; crystal structure analysis; determinants of thermal adaptation; dimethyl arsenic acid; electrostatic; enzymatic activity; glycine; hydrolase; hydrophobic interactions; mammalian Hormone-Sensitive Lipase; oligomeric state; phenol; proline; psychrophiles; psychrophilic organisms; salt bridge; secondary activities; temperature of the organisms; thermotolerant; three-dimensional structures
Document Type: Research Article
Publication date: January 1, 2011
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