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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Autor principal:	Martin B. L. McAndrew (22683641) (author)
Altres autors:	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)
Publicat:	2025
Matèries:	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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