(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Archaea: NE > Euryarchaeota: NE > Thermococci: NE > Thermococcales: NE > Thermococcaceae: NE > Pyrococcus: NE > Pyrococcus furiosus: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Pyrococcus furiosus COM1: N, E.
Molecular evidence
Database
No mutation 4 structures(e.g. : 5G59, 5G5C, 5G5M... more)(less) 5G59: Structure of the Pyrococcus Furiosus Esterase Pf2001 with space group P3121, 5G5C: Structure of the Pyrococcus Furiosus Esterase Pf2001 with space group C2221, 5G5M: Structure of the Pyrococcus Furiosus Esterase Pf2001 with space group P21, 5LCN: Structure of the Pyrococcus Furiosus Esterase Pf2001 with space group P212121 No kinetic
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 MIIEILVAALVLFLVFTAFVGYKMVNPPRVVGNWTPKDLSFEYKDVEITT EDNVKLSGWWIDNGSDKTVIPLHGYTSSRWAEHYMRPVIEFLLKEGYNVL AFDFRAHGKSGGKYTTVGDKEILDLKAGVKWLKDNYPEKSKRIGVIGFSM GALVAIRGLSEVKEICCGVADSPPIYLDKTGARGMKYFAKLPEWLYSFVK PFSELFSGGRPINVLNYTNSIKKPLFLIIGRRDTLVKVEEVQEFYERNKH VNPNVELWVTDAPHVRTIQVFPEEWKSRVGEFLKRWMG
Lipases and esterases constitute a group of enzymes that catalyze the hydrolysis or synthesis of ester bonds. A major biotechnological interest corresponds to thermophilic esterases, due to their intrinsic stability at high temperatures. The Pf2001 esterase from Pyrococcus furiosus reaches its optimal activity between 70 degrees C and 80 degrees C. The crystal structure of the Pf2001 esterase shows two different conformations: monomer and dimer. The structures reveal important rearrangements in the "cap" subdomain between monomer and dimer, by the formation of an extensive intertwined helical interface. Moreover, the dimer interface is essential for the formation of the hydrophobic channel for substrate selectivity, as confirmed by mutagenesis and kinetic analysis. We also provide evidence for dimer formation at high temperatures, a process that correlates with its enzymatic activation. Thus, we propose a temperature-dependent activation mechanism of the Pf2001 esterase via dimerization that is necessary for the substrate channel formation in the active-site cleft.
Pyrococcus furiosus hypothetical protein pf2001
