(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 > Betaproteobacteria: NE > Burkholderiales: NE > Burkholderiaceae: NE > Burkholderia: NE > Burkholderia gladioli: 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 MNHPDIDTHSRNAAAPLPFVLVHGAWHGAWAYERLGAALAARGHASVAHD LPAHGINARYPAAFWQGDAQALAQEPSPVAATTLDDYTGQVLRAIDAACA LGHPRVVLVGHSMGGVAITAAAERAPERIAALVYLAAFMPASGVPGLDYV RAPENHGEMLASLICASPRAIGALRINPASRDAAYLATLKQALFEDVDEA TFRAVTRLMSSDVPTAPFATPIATTAERWGSIARHYVTCAEDRVILPALQ RRFIAEADAFLPERPTRVHALDSSHSPFLSQPDTLAELLTGIARNTAI
Reference
Title: Cloning and characterization of EstC from Burkholderia gladioli, a novel-type esterase related to plant enzymes Reiter B, Glieder A, Talker D, Schwab H Ref: Applied Microbiology & Biotechnology, 54:778, 2000 : PubMed
By screening a genomic library of Burkholderia gladioli (formerly Pseudomonas marginata) for clones exhibiting esterolytic activity, the gene for a novel-type esterase (EstC) showing significant homology to plant enzymes could be isolated. High homology was found to two hydroxynitrile lyases originating from Hevea brasiliensis (tropical rubber tree) and Manihot esculenta (cassava), and to two proteins from Oryza sativa (rice) that are specifically induced upon infection by Pseudomonas syringae pv. syringae. The sequenced ORF encodes for a protein of 298 amino acids. The enzyme was efficiently overexpressed in Escherichia coli, purified and characterized with respect to enzymatic capabilities. The enzyme was able to hydrolyze a variety of esterase substrates of low to medium carbonic acid chain length, but no triglycerides were hydrolyzed. Despite the high sequence homology, no hydroxynitrile lyase activity could be recognized.
