Microbial Enzymes Mined from the Urania Deep-Sea Hypersaline Anoxic Basin (Articolo in rivista)

Type
Label
  • Microbial Enzymes Mined from the Urania Deep-Sea Hypersaline Anoxic Basin (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.chembiol.2005.05.020 (literal)
Alternative label
  • Ferrer, M.; Golyshina, O.V.; Chernikova, T.N.; Khachane, A.N.; Dos Santos, V.A.P.M.; Yakimov, M.M.; Timmis, K.N.; Golyshin, P.N.; (2005)
    Microbial Enzymes Mined from the Urania Deep-Sea Hypersaline Anoxic Basin
    in Chemistry & biology (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ferrer, M.; Golyshina, O.V.; Chernikova, T.N.; Khachane, A.N.; Dos Santos, V.A.P.M.; Yakimov, M.M.; Timmis, K.N.; Golyshin, P.N.; (literal)
Pagina inizio
  • 895 (literal)
Pagina fine
  • 904 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 12 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 10 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 8 (literal)
Note
  • PubMe (literal)
  • Scopus (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Microbiology, GBF - German Research Centre for Biotechnology, 38124 Braunschweig, Germany Institute of Catalysis, CSIC, Cantoblanco, 28049 Madrid, Spain Istituto Per l'Ambiente Marino Costiero, CNR, 98100 Messina, Italy Institute of Microbiology, Technical University Braunschweig, 38124 Braunschweig, Germany (literal)
Titolo
  • Microbial Enzymes Mined from the Urania Deep-Sea Hypersaline Anoxic Basin (literal)
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) (literal)
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