This title appears in the Scientific Report :
2016
Please use the identifier:
http://dx.doi.org/10.1002/2211-5463.12061 in citations.
Please use the identifier: http://hdl.handle.net/2128/12856 in citations.
A membrane-bound esterase PA2949 from Pseudomonas aeruginosa is expressed and purified from Escherichia coli
A membrane-bound esterase PA2949 from Pseudomonas aeruginosa is expressed and purified from Escherichia coli
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,...
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Personal Name(s): | Kovacic, Filip (Corresponding author) |
---|---|
Bleffert, Florian / Caliskan, Muttalip / Wilhelm, Susanne / Granzin, Joachim / Batra-Safferling, Renu / Jaeger, Karl-Erich | |
Contributing Institute: |
Institut für Molekulare Enzymtechnologie (HHUD); IMET Strukturbiochemie; ICS-6 |
Published in: | FEBS Open Bio, 6 (2016) 5, S. 484 - 493 |
Imprint: |
Cambridge
Elsevier on behalf of the Federation of European Biochemical Societies
2016
|
PubMed ID: |
27419054 |
DOI: |
10.1002/2211-5463.12061 |
Document Type: |
Journal Article |
Research Program: |
Biotechnology Physical Basis of Diseases |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/12856 in citations.
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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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