Skip to main content
padlock icon - secure page this page is secure

An Overview on Thermal Adaptation of Esterases and Lipases Belonging to the HSL Family: New Insight on the Computational Analysis

Buy Article:

$68.00 + tax (Refund Policy)

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.

No References
No Citations
No Supplementary Data
No Article Media
No Metrics

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

More about this publication?
  • Current Chemical Biology aims to publish full-length and mini reviews on exciting new developments at the chemistry-biology interface, covering topics relating to Chemical Synthesis, Science at Chemistry-Biology Interface and Chemical Mechanisms of Biological Systems.

    Current Chemical Biology covers the following areas: Chemical Synthesis (Syntheses of biologically important macromolecules including proteins, polypeptides, oligonucleotides, oligosaccharides etc.; Asymmetric synthesis; Combinatorial synthesis; Diversity-oriented synthesis; Template-directed synthesis; Biomimetic synthesis; Solid phase biomolecular synthesis; Synthesis of small biomolecules: amino acids, peptides, lipids, carbohydrates and nucleosides; and Natural product synthesis).

    Science at Chemistry-Biology Interface (Chemical informatics; Macromolecular catalysts and receptors; Enzymatic synthesis; Biosynthetic engineering; Combinatorial biosynthesis; Plant cell based chemistry; Bacterial and viral cell based chemistry; Chemistry of cellular processes in plants/animals; Receptor chemistry; Cell signaling chemistry; Drug design through understanding of disease processes; Synthetic biology; New high throughput screening techniques; Small molecular array fabrication; Chemical genomics; Chemical and biological approaches to carbohydrates proteins and nucleic acids design; Chemical and biological regulation of biosynthetic pathways; and Unnatural biomolecular analogs).
  • Editorial Board
  • Information for Authors
  • Subscribe to this Title
  • Ingenta Connect is not responsible for the content or availability of external websites
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more