The mechanism used by proteins to maintain their thermostability throughout a wide range of temperature has been extensively investigated. Different aspects have been reported which explain protein thermal stability such as protein flexibility, loops length, number of charged residues, hydrophobic and ionic interactions, electrostatic interactions and their pathways, number and dimension of internal cavities. All these features have an effect on the protein global structure, but they are not the unique mechanism which explains the protein thermal stability.
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: Carboxylesterase, computational analysis, crystal structure analysis, HSL family, determinants of thermal adaptation, Lipases, temperature of the organisms, psychrophilic organisms, enzymatic activity, applications in biotechnology, psychrophiles, cold ecosystems, abyssal ocean, alpine regions, Psychrophilic enzymes, hydrophobic interactions, salt bridge, glycine, biophysical studies, X-ray crystal structures, electrostatic, alanine, Esterase, cholinesterases, Eukarya, Bacteria, Archaea, mammalian Hormone-Sensitive Lipase, three-dimensional structures, Archaeoglobus fulgidus, Bacillus subtilis, cap-domain, Rhodococcus, dimethyl arsenic acid, phenol, hydrolase, Lactobacillus plantarum, proline, oligomeric state, HSL-like group, biocatalyst, secondary activities, Staphylococcus aureans, thermotolerant
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