Rosser SJ

References (3)

Title : Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain - Jensen_2016_PLoS.One_11_e0166128
Author(s) : Jensen MV , Horsfall LE , Wardrope C , Togneri PD , Marles-Wright J , Rosser SJ
Ref : PLoS ONE , 11 :e0166128 , 2016
Abstract : Proteins in the serine esterase family are widely distributed in bacterial phyla and display activity against a range of biologically produced and chemically synthesized esters. A serine esterase from the psychrophilic bacterium Pseudoalteromonas arctica with a C-terminal OsmC-like domain was recently characterized; here we report on the identification and characterization of further putative esterases with OsmC-like domains constituting a new esterase family that is found in a variety of bacterial species from different environmental niches. All of these proteins contained the Ser-Asp-His motif common to serine esterases and a highly conserved pentapeptide nucleophilic elbow motif. We produced these proteins heterologously in Escherichia coli and demonstrated their activity against a range of esterase substrates. Two of the esterases characterized have activity of over two orders of magnitude higher than other members of the family, and are active over a wide temperature range. We determined the crystal structure of the esterase domain of the protein from Rhodothermus marinus and show that it conforms to the classical alpha/beta hydrolase fold with an extended 'lid' region, which occludes the active site of the protein in the crystal. The expansion of characterized members of the esterase family and demonstration of activity over a wide-range of temperatures could be of use in biotechnological applications such as the pharmaceutical, detergent, bioremediation and dairy industries.
ESTHER : Jensen_2016_PLoS.One_11_e0166128
PubMedSearch : Jensen_2016_PLoS.One_11_e0166128
PubMedID: 27851780
Gene_locus related to this paper: rhom4-d0mhy8

Title : Crystal structure of a bacterial cocaine esterase -
Author(s) : Larsen NA , Turner JM , Stevens J , Rosser SJ , Basran A , Lerner RA , Bruce NC , Wilson IA
Ref : Nat Struct Biol , 9 :17 , 2002
PubMedID: 11742345
Gene_locus related to this paper: rhosm-cocE

Title : Gene cloning and nucleotide sequencing and properties of a cocaine esterase from Rhodococcus sp. strain MB1 - Bresler_2000_Appl.Environ.Microbiol_66_904
Author(s) : Bresler MM , Rosser SJ , Basran A , Bruce NC
Ref : Applied Environmental Microbiology , 66 :904 , 2000
Abstract : A strain of Rhodococcus designated MB1, which was capable of utilizing cocaine as a sole source of carbon and nitrogen for growth, was isolated from rhizosphere soil of the tropane alkaloid-producing plant Erythroxylum coca. A cocaine esterase was found to initiate degradation of cocaine, which was hydrolyzed to ecgonine methyl ester and benzoate; both of these esterolytic products were further metabolized by Rhodococcus sp. strain MB1. The structural gene encoding a cocaine esterase, designated cocE, was cloned from Rhodococcus sp. strain MB1 genomic libraries by screening recombinant strains of Rhodococcus erythropolis CW25 for growth on cocaine. The nucleotide sequence of cocE corresponded to an open reading frame of 1,724 bp that codes for a protein of 574 amino acids. The amino acid sequence of cocaine esterase has a region of similarity with the active serine consensus of X-prolyl dipeptidyl aminopeptidases, suggesting that the cocaine esterase is a serine esterase. The cocE coding sequence was subcloned into the pCFX1 expression plasmid and expressed in Escherichia coli. The recombinant cocaine esterase was purified to apparent homogeneity and was found to be monomeric, with an M(r) of approximately 65,000. The apparent K(m) of the enzyme (mean +/- standard deviation) for cocaine was measured as 1.33 +/- 0.085 mM. These findings are of potential use in the development of a linked assay for the detection of illicit cocaine.
ESTHER : Bresler_2000_Appl.Environ.Microbiol_66_904
PubMedSearch : Bresler_2000_Appl.Environ.Microbiol_66_904
PubMedID: 10698749
Gene_locus related to this paper: rhosm-cocE