Disease relevance of est

• This method allowed identification of Pseudomonas putida NRRL B-18435 as a source of this activity and the cloning of a new esterase gene, estZ [1].
• Although the E. coli genome encodes several proteins with esterase activity, neither wild-type strains nor KO11 contained significant ethyl acetate esterase activity [1].

High impact information on est

• EST can hydrolyze the methyl ester group without affecting the acetylthiol ester moiety in dl-MATI [2].
• Stereoselective esterase from Pseudomonas putida IFO12996 reveals alpha/beta hydrolase folds for D-beta-acetylthioisobutyric acid synthesis [2].
• Esterase (EST) from Pseudomonas putida IFO12996 catalyzes the stereoselective hydrolysis of methyl dl-beta-acetylthioisobutyrate (dl-MATI) to produce d-beta-acetylthioisobutyric acid (DAT), serving as a key intermediate for the synthesis of angiotensin-converting enzyme inhibitors [2].
• The examination of substrate specificity of EST toward other linear esters revealed that the enzyme showed specific activity toward methyl esters and that it recognized the configuration at C-2 [2].
• The EST gene was cloned and expressed in Escherichia coli; the recombinant protein is a non-disulfide-linked homotrimer with a monomer molecular weight of 33,000 in both solution and crystalline states, indicating that these ESTs function as trimers [2].

Chemical compound and disease context of est

• Amino acid homology to the active site of a Pseudomonas putida esterase and inhibitor studies of the enzyme imply involvement of a serine residue in catalysis [3].

Biological context of est

• An inducible esterase catalyzing the hydrolysis of cocaine to ecgonine methyl ester and benzoic acid was identified and purified 22-fold [4].
• The investigation of growth kinetics and host cell viability showed that the presence of the EstA translocator domain in the outer membrane neither inhibits cell growth nor affects cell viability [5].
• The complete nucleotides of the DNA fragment containing the esterase gene were sequenced and found to include a single open reading frame of 828 bp coding for a protein of 276 amino acid residues [6].
• Nucleotide sequence of the gene for a thermostable esterase from Pseudomonas putida MR-2068 [6].

Associations of est with chemical compounds

• This was then metabolized to pyruvate; the other product was presumed to be the 4-methyl ester of oxalacetic acid, for which cell extracts contained an inducible, specific esterase [7].

Analytical, diagnostic and therapeutic context of est

• The use of a novel recombinant heroin esterase in the development of an illicit drugs biosensor [8].
• Transcription analysis using RT-PCR showed that adh1 is cotranscribed with the putative acyl-CoA synthetase and esterase genes during growth on OPEO(n) [9].

References