(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > unclassified sequences: NE > environmental samples: NE > prokaryotic environmental samples: NE > uncultured prokaryote: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MKVELPQGGYQGLAGDGVVEFRGVPFALPPVGELRFKAPRPLPDSDRSVN ADRYPLPSLQVKNPLMGVEDSGEDCLYLNIWVPEGEGPFPVMLWYHGGGY IAGSVSQPLYNGAALAASQKVVVVHAAYRLGAHGFADFATIAPELEADSN LGLRDQVAALEWVNRHIEAFGGRPDRVTLFGESAGGFSVATLMATPRARP LFQAAIVQSGAGDFALAPEEVAKVTSAFVEALPGDGSAADKLRQADPKAW IAAQNQALRTLVKRGLRDTTPQFAMNFQPMVDGDLLPRLPVDAIADGEAR DIALMASVCRDEYHFFQYAGPMAGFPSVEELRRFDEAEILRRFQRALPQH GQQALSYYQRTVTPDPQRSNMDWFSAMETDRLFRVPTLRLLDAQAAHRDD TRGLQFTWTSQQFGVPMGACHVIDVPFVFGVTDTPAGMFFTGGGEPARAL AAEVQKVWGDFAHGRAVQGPAWKDTRRVRQFGPGDAEAALLDADGEALWA DIIPVPGTAKPGQGA
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).