Journal Article

FZJ-2016-06319

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png A membrane-bound esterase PA2949 from Pseudomonas aeruginosa is expressed and purified from Escherichia coli

Kovacic, F. (Corresponding author)FZJ* ; Bleffert, F.FZJ* ; Caliskan, M. ; Wilhelm, S. ; Granzin, J.FZJ* ; Batra-Safferling, R.FZJ* ; Jaeger, K.-E.FZJ*

2016
Elsevier on behalf of the Federation of European Biochemical Societies Cambridge

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Please use a persistent id in citations: http://hdl.handle.net/2128/12856  doi:10.1002/2211-5463.12061

Abstract: 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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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)
2. Institut für Molekulare Enzymtechnologie (HHUD) (IMET)

Research Program(s):

1. 553 - Physical Basis of Diseases (POF3-553) (POF3-553)
2. 581 - Biotechnology (POF3-581) (POF3-581)

Appears in the scientific report 2016

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Database coverage:
; ; ; ; BIOSIS Previews ; DOAJ Seal ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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