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Microbial enzymes mined from the Urania deep-sea hypersaline anoxic basin.
- Source :
-
Chemistry & biology [Chem Biol] 2005 Aug; Vol. 12 (8), pp. 895-904. - Publication Year :
- 2005
-
Abstract
- We created a metagenome expression library from the brine:seawater interface of the Urania hypersaline basin, screened it for esterases, and characterized five of these. Two had no significant sequence homology to known esterases, hydrolyzed both carboxylesters and thioesters, and exhibited unusual, habitat-specific characteristics (preference for high hydrostatic pressure and salinity). One has an unusual structural signature incorporating three catalytic active centers mediating distinct hydrolytic activities and an adaptive tertiary-quaternary structure that alters between three molecular states, according to the prevailing physicochemical conditions. Some of the esterases have high activities, specificities, enantioselectivities, and exceptional stability in polar solvents, and they are therefore potentially useful for industrial biotransformations. One possesses the highest enantioselectivity toward an ester of the important chiral synthon solketal (E: 126[S]; 98%ee).
- Subjects :
- Bacteria, Anaerobic enzymology
Bacterial Proteins chemistry
Bacterial Proteins metabolism
Base Sequence
Ecosystem
Esterases chemistry
Hydrostatic Pressure
Molecular Sequence Data
Oceans and Seas
Phylogeny
Sodium Chloride
Stereoisomerism
Substrate Specificity
Bacterial Proteins isolation & purification
Esterases isolation & purification
Esterases metabolism
Marine Biology methods
Subjects
Details
- Language :
- English
- ISSN :
- 1074-5521
- Volume :
- 12
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Chemistry & biology
- Publication Type :
- Academic Journal
- Accession number :
- 16125101
- Full Text :
- https://doi.org/10.1016/j.chembiol.2005.05.020