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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| Бусад зохиолчид: | , , , , , |
| Хэвлэсэн: |
2025
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Шошго нэмэх
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| _version_ | 1849927626481729536 |
|---|---|
| author | Martin B. L. McAndrew (22683641) |
| author2 | Jonathan Cook (3435386) Amy Gill (14910614) Kavya Sahoo (22683644) Clare Thomas (7943747) Phillip J. Stansfeld (1267617) Allister Crow (263807) |
| author2_role | author author author author author author |
| author_facet | Martin B. L. McAndrew (22683641) Jonathan Cook (3435386) Amy Gill (14910614) Kavya Sahoo (22683644) Clare Thomas (7943747) Phillip J. Stansfeld (1267617) Allister Crow (263807) |
| author_role | author |
| dc.creator.none.fl_str_mv | Martin B. L. McAndrew (22683641) Jonathan Cook (3435386) Amy Gill (14910614) Kavya Sahoo (22683644) Clare Thomas (7943747) Phillip J. Stansfeld (1267617) Allister Crow (263807) |
| dc.date.none.fl_str_mv | 2025-11-25T18:39:41Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pbio.3003427.s008 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/figure/Nitrocefin_and_p-nitrophenyl_butyrate_hydrolysis_assays_for_Pseudomonas_i_aeruginosa_i_TesA_/30714782 |
| dc.rights.none.fl_str_mv | CC BY 4.0 info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | 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 |
| dc.title.none.fl_str_mv | Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA. |
| dc.type.none.fl_str_mv | Image Figure info:eu-repo/semantics/publishedVersion image |
| description | <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 control, where the enzyme was substituted for protein-free buffer. <b>(C)</b> Plots of the change in absorption at 488 nm for enzyme-catalyzed reaction (<i>red</i> dots) and the control (<i>blue</i> dots). A fit from a single exponential function is shown in black. <b>(D)</b> Photograph of two wells after ~18h showing the color change associated with nitrocefin hydrolysis. Underlying data is provided in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s028" target="_blank">S11 Data</a>–<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s030" target="_blank">S13 Data</a>.</p> <p>(TIFF)</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_afb2197d359f399072270d2d648f9bb7 |
| identifier_str_mv | 10.1371/journal.pbio.3003427.s008 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30714782 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA.Martin B. L. McAndrew (22683641)Jonathan Cook (3435386)Amy Gill (14910614)Kavya Sahoo (22683644)Clare Thomas (7943747)Phillip J. Stansfeld (1267617)Allister Crow (263807)BiophysicsBiochemistryMicrobiologyCell BiologyMolecular BiologyBiotechnologyDevelopmental BiologyCancerHematologyBiological Sciences not elsewhere classifiedChemical Sciences not elsewhere classifiedInformation Systems not elsewhere classifiedtolc efflux pumpmultifunctional hydrolytic enzymeextracts hydrophobic compoundsextracting hydrophobic moleculescapture implied longbacterial cell envelopeactive site residueslipid hydrolase complexescherichia coli </data suggests ybbapabc superfamily ’div >< pcoli </abc superfamilythioester substratestesa complexstructural characterizationremarkable diversitynew functionmechanotransmission mechanisminner membraneextensively characterizedexperimentally confirmcomplete ybbap>, three<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 control, where the enzyme was substituted for protein-free buffer. <b>(C)</b> Plots of the change in absorption at 488 nm for enzyme-catalyzed reaction (<i>red</i> dots) and the control (<i>blue</i> dots). A fit from a single exponential function is shown in black. <b>(D)</b> Photograph of two wells after ~18h showing the color change associated with nitrocefin hydrolysis. Underlying data is provided in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s028" target="_blank">S11 Data</a>–<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s030" target="_blank">S13 Data</a>.</p> <p>(TIFF)</p>2025-11-25T18:39:41ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.pbio.3003427.s008https://figshare.com/articles/figure/Nitrocefin_and_p-nitrophenyl_butyrate_hydrolysis_assays_for_Pseudomonas_i_aeruginosa_i_TesA_/30714782CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/307147822025-11-25T18:39:41Z |
| spellingShingle | Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA. Martin B. L. McAndrew (22683641) 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 |
| status_str | publishedVersion |
| title | Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA. |
| title_full | Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA. |
| title_fullStr | Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA. |
| title_full_unstemmed | Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA. |
| title_short | Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA. |
| title_sort | Nitrocefin and p-nitrophenyl butyrate hydrolysis assays for Pseudomonas <i>aeruginosa</i> TesA. |
| topic | 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 |