(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 cepacia complex: NE > Burkholderia cepacia: 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.) Burkholderia cepacia JBK9: N, E.
Burkholderia cepacia GG4: N, E.
Burkholderia cepacia ATCC 25416: N, E.
Pseudomonas cepacia: 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 MARSMRSRVVAGAVACAMSVAPFAGTTALMTLATTHAAMAATAPADNYAA TRYPIILVHGLTGTDKYAGVLEYWYGIQEDLQQHGATVYVANLSGFQSDD GPNGRGEQLLAYVKTVLAATGAAKVNLVGHSQGGLTSRYVAAVAPDLVAS VTTIGTPHRGSEFADFVQSVLAYDPTGLSSTVIAAFVNVFGILTSSSHNT NQDALASLKTLTTSQAATYNQNYPSAGLGAPGSCQTGAPTETVGGNTHLL YSWAGTAIQPTLSLFGVTGAQDTSTIPLVDPANALDPSTLALFGTGTVMI NRGSGQNDGLVSKCSALYGKVLSTSYKWNHIDEINQLLGVRGAYAEDPVA VIRTHANRLQLAGV
To understand the origin of high enantioselectivity of Burkholderia cepacia lipase (BCL) toward secondary alcohol, (R,S)-1-phenoxy-2-hydroxybutane (1), and its ester (E1), we determined the crystal structure of BCL complexed with phosphonate analogue of S-E1 and accomplished a series of MM, MC, and QM/MM studies. We have found that the inhibitor in the S configuration binds into the BCL active site in the same manner as the R isomer, with an important difference: while in case of the R-inhibitor the H-bond between its alcohol oxygen and catalytic His286 can be formed, in the case of the S-inhibitor this is not possible. Molecular modeling for both E1 enantiomers revealed orientations in which all hydrogen bonds characteristic of productive binding are formed. To check the possibility of chemical transformation, four different orientations of the substrate (two for each enantiomer) were chosen, and a series of ab initio QM/MM calculations were accomplished. Starting from the covalent complex, we modeled the ester (E1) hydrolysis and the alcohol (1) esterification. The calculations revealed that ester release is possible starting with all four covalent complexes. Alcohol release from the BCL-E1 complex in which the S-substrate is bound in the same manner as the S-inhibitor in the crystal structure however is not possible. These results show that the crystallographically determined binding modes should be taken with caution when modeling chemical reactions.
Burkholderia cepacia (Pseudomonas cepacia) cholesterol esterase
