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| Hauptseite > Publikationsdatenbank > A membrane-bound esterase PA2949 from Pseudomonas aeruginosa is expressed and purified from Escherichia coli > print |
| Hauptseite > Publikationsdatenbank > A membrane-bound esterase PA2949 from Pseudomonas aeruginosa is expressed and purified from Escherichia coli > print |
| 001 | 821075 | ||
| 005 | 20220930130110.0 | ||
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| 100 | 1 | _ | |a Kovacic, Filip |0 P:(DE-Juel1)131480 |b 0 |e Corresponding author |
| 245 | _ | _ | |a A membrane-bound esterase PA2949 from Pseudomonas aeruginosa is expressed and purified from Escherichia coli |
| 260 | _ | _ | |a Cambridge |c 2016 |b Elsevier on behalf of the Federation of European Biochemical Societies |
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| 520 | _ | _ | |a Pseudomonas aeruginosa strain 1001 produces an esterase (EstA) that can hydrolyse the racemic methyl ester of b-acetylthioisobutyrate to produce the (D)-enantiomer, which serves as a precursor of captopril, a drug used for treatment of hypertension. We show here that PA2949 from P. aeruginosa PA01, a homologue of EstA, can efficiently be expressed in an enzymatically active form in E. coli. The enzyme is membrane-associated as demonstrated by cell fractionation studies. PA2949 was purified to homogeneity after solubilisation with the nonionic detergent, Triton X-100, and was shown to possess a conserved esterase catalytic triad consisting of Ser137–His258–Asp286. Our results should allow the development of an expression and purification strategy to produce this biotechnologically relevant esterase in a pure form with a high yield. |
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