(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Thiotrichales: NE > Piscirickettsiaceae: NE > Cycloclasticus: NE > Cycloclasticus zancles: NE > Cycloclasticus zancles 78-ME: NE
Carbon-carbon_bond_hydrolase : 9gamm-s5tv80Cycloclasticus zancles 78-ME, EH62 ,2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoate hydrolase, 9gamm-s5u059Cycloclasticus zancles 78-ME, EH19, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase. LYsophospholipase_carboxylesterase : 9gamm-s5t532Cycloclasticus zancles 78-ME, EH34 Dual esterases-meta-cleavage product (MCP) hydrolases from the a/b hydrolase family
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.) Cycloclasticus zancles 7-ME: N, E.
Cycloclasticus sp. DSM 27168: N, E.
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 MNIENESLYEKKYIDVDGINTCYIEAGEGEPLVLIHGGGAGANGYGNWFA CLPLFAKSFRTIAVDMVGFGLTDSPDPSDFEYSQKARYEHIANFIKKMGL EKVNLVGNSMGGATAMGVAVEYPELCERLILMGSAGLNTELDIAALKPVL GYDYTKEGMIRLIKVLTNDSFQITSEMIDYRHANSVDPKNEASYAATMDW VRKAGGLFYEEDYIASVQQKTLVVNGKDDQVVPLSSAHKFLELMDNSWGY IMPHCGHWAMIEYPDDFSSAVSAFIKSH
Esterases receive special attention because their wide distribution in biological systems and environments and their importance for physiology and chemical synthesis. The prediction of esterases substrate promiscuity level from sequence data and the molecular reasons why certain such enzymes are more promiscuous than others, remain to be elucidated. This limits the surveillance of the sequence space for esterases potentially leading to new versatile biocatalysts and new insights into their role in cellular function. Here we performed an extensive analysis of the substrate spectra of 145 phylogenetically and environmentally diverse microbial esterases, when tested with 96 diverse esters. We determined the primary factors shaping their substrate range by analyzing substrate range patterns in combination with structural analysis and protein-ligand simulations. We found a structural parameter that helps ranking (classifying) promiscuity level of esterases from sequence data at 94% accuracy. This parameter, the active site effective volume, exemplifies the topology of the catalytic environment by measuring the active site cavity volume corrected by the relative solvent accessible surface area (SASA) of the catalytic triad. Sequences encoding esterases with active site effective volumes (cavity volume/SASA) above a threshold show greater substrate spectra, which can be further extended in combination with phylogenetic data. This measure provides also a valuable tool for interrogating substrates capable of being converted. This measure, found to be transferred to phosphatases of the haloalkanoic acid dehalogenase superfamily and possibly other enzymatic systems, represents a powerful tool for low-cost bioprospecting for esterases with broad substrate ranges, in large scale sequence datasets.
