Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA.

Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA.

<p><b>(A)</b> Purified <i>P. aeruginosa</i> TesA with N-terminal tag (PaTesA). <b>(B)</b> Representative example of nitrocefin hydrolysis by PaTesA. Red nested curves represent a series of spectral measurements taken over time. Blue curves indicate the contr...

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Détails bibliographiques
Auteur principal: Martin B. L. McAndrew (22683641) (author)
Autres auteurs: Jonathan Cook (3435386) (author), Amy Gill (14910614) (author), Kavya Sahoo (22683644) (author), Clare Thomas (7943747) (author), Phillip J. Stansfeld (1267617) (author), Allister Crow (263807) (author)
Publié: 2025
Sujets:
Biophysics
Biochemistry
Microbiology
Cell Biology
Molecular Biology
Biotechnology
Developmental Biology
Cancer
Hematology
Biological Sciences not elsewhere classified
Chemical Sciences not elsewhere classified
Information Systems not elsewhere classified
tolc efflux pump
multifunctional hydrolytic enzyme
extracts hydrophobic compounds
extracting hydrophobic molecules
capture implied long
bacterial cell envelope
active site residues
lipid hydrolase complex
escherichia coli </
data suggests ybbap
abc superfamily ’
div >< p
coli </
abc superfamily
thioester substrates
tesa complex
structural characterization
remarkable diversity
new function
mechanotransmission mechanism
inner membrane
extensively characterized
experimentally confirm
complete ybbap
>, three
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