Disease relevance of aesT

• Other proteins, including a His-tagged overexpressed esterase from the related organism Acinetobacter calcoaceticus BD4, showed no enhancement [1].
• Cloning and expression in Escherichia coli of an esterase-coding gene from the oil-degrading bacterium Acinetobacter calcoaceticus RAG-1 [2].
• The esterase (molecular mass, 34.5 kDa) was cloned and overexpressed in Escherichia coli BL21(DE3) behind the phage T7 promoter with the His tag system [1].
• To further detect Salmonella typhi and the rare beige or colorless colonies atypical of Salmonella isolates, a C8 esterase detection spot test was carried out [3].
• Biotyping is an appropriate method for screening of strains, and ribotyping and esterase electrophoresis could be used as additional methods to delineate outbreaks of nosocomial infections caused by A. baumannii [4].

High impact information on aesT

• Benzaldehyde dehydrogenase I had an NAD+-activated esterase activity with 4-nitrophenol acetate as substrate, and the dehydrogenase activity was inhibited by a range of thiol-blocking reagents [5].
• Benzaldehyde dehydrogenase II, but not benzyl alcohol dehydrogenase, exhibited esterase activity with 4-nitrophenyl acetate as substrate [6].
• Knockout mutations in hcaG indicate that this gene encodes a membrane-associated esterase that hydrolyzes chlorogenate to quinate, which is metabolized in the periplasm, and caffeate, which is metabolized by intracellular enzymes [7].
• The overexpressed esterase was recovered from the inclusion bodies by solubilization with deoxycholate and, after slow dialysis, was purified by metal chelation affinity chromatography [1].
• A mutant of ADP1 with a Km(r) cassette introduced into salE had lost the ability to utilize only ethyl and methyl salicylates of the esters tested as sole carbon sources, and no esterase activity against ethyl salicylate could be detected in cell extracts [8].

Biological context of aesT

• The original esterase-positive plasmid pRA17 carried a 2.2-kb insert from a partial MboI digest of RAG-1 DNA, which gave a single band with RAG-1 DNA following Southern hybridization [2].
• The 27 lipase-deficient transconjugants which were isolated exhibited several different phenotypes, including gelatinase mutants, esterase mutants, and putative auxotrophs [9].
• The N-terminal sequence of the first 20 amino acids of the heterologous expressed esterase corresponded to that obtained from the nucleotide sequence [10].
• These cells also produced an esterase (measured by the hydrolysis of beta-naphthyl acetate) [11].
• The rRNA gene restriction patterns (using EcoRI and PvuII as restriction endonucleases) and the esterase electrophoretic profiles were determined on 31 strains, using as comparison strain isolates from another intensive care unit of our hospital and from two other French hospitals [4].

Anatomical context of aesT

• The localization of hydrolytic enzymes, phosphatase, esterase, lipase and palmitoyl-CoA hydrolase was analysed in the cytosol, cytoplasmic membrane, periplasmic fraction, outer membrane and culture supernatant in dependence on the growth rate of the bacteria [12].

Associations of aesT with chemical compounds

• Its product, SalE, was shown to have esterase activity against short-chain alkyl esters of 4-nitrophenol but was also able to hydrolyze ethyl salicylate to ethanol and salicylic acid [8].
• Insertional inactivation of xcpR in A. calcoaceticus ADP1 by transcriptional fusion to lacZ abolishes secretion of lipase and esterase and leads to lack of growth on dodecane and slower growth on hexadecane [13].
• Comparison with homologous proteins from both eukaryotic and prokaryotic organisms suggest that the RAG-1 esterase exhibits sequence motifs characteristic of both serine proteases and of lipases [10].
• The role of esterase in the release of cell-bound emulsifier and the contribution of capsular polysaccharide to the emulsification activity were observed [14].
• Each esterase was defined by its spectrum of hydrolytic activity toward five synthetic substrates and its sensitivity to di-isopropyl fluorophosphate [15].

Physical interactions of aesT

• Deletion of estA only partially abolished cell-bound esterase activity in A. calcoaceticus, indicating that BD413 forms at least two esterases [16].

Other interactions of aesT

• Downstream of the Acinetobacter calcoaceticus estA gene, encoding a cell-bound esterase, an open reading frame (orf) was identified, which may encode a protein with a mass of 20.4 kDa [17].
• The est gene encoding an esterase from Acinetobacter lwoffii RAG-1 was cloned into E. coli under the control of the PL promoter of the phage lambda [10].
• The activities of isocitrate lyase, esterase, and lipase by the psychrotrophic Acinetobacter sp. strain HH1-1 were monitored during incubation at 25 degreesC, 5 degreesC, and after a 25 degreesC to 5 degreesC down shift in growth temperature [18].

Analytical, diagnostic and therapeutic context of aesT

• Similarly, a series of esterase-defective mutants were generated by site-directed mutagenesis, cloned, and overexpressed in E. coli [1].
• Four EcoRI ribotypes, four PvuII ribotypes and six esterase profiles were identified [4].
• Esterase from the oil-degrading Acinetobacter lwoffii RAG-1: sequence analysis and over-expression in Escherichia coli [10].
• After breaking of the cells, most of the cell-bound lipase and esterase activity was solubilized, even after very high speed centrifugation [11].

References