{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,3]],"date-time":"2026-11-03T08:26:28Z","timestamp":1793694388249,"version":"4.5.1"},"reference-count":56,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2026,7,28]],"date-time":"2026-07-28T00:00:00Z","timestamp":1785196800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,7,28]],"date-time":"2026-07-28T00:00:00Z","timestamp":1785196800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100010570","name":"Nieders\u00e4chsisches Ministerium f\u00fcr Wissenschaft und Kultur","doi-asserted-by":"publisher","award":["21\u201078904\u201063\u20105\/19"],"award-info":[{"award-number":["21\u201078904\u201063\u20105\/19"]}],"id":[{"id":"10.13039\/501100010570","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2026,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    The emergence of antibiotic resistance in bacteria is a major threat to global public health. To combat increasingly drug\u2010resistant bacteria like\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                    <\/jats:styled-content>\n                    , new targets for pharmaceuticals need to be explored. One such potential target for\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>P. aeruginosa<\/jats:italic>\n                    <\/jats:styled-content>\n                    infections is the diaminopimelate epimerase DapF, a protein that plays an essential role in bacterial lysine and peptidoglycan synthesis. In this study, the diaminopimelate epimerase of\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                    <\/jats:styled-content>\n                    PA14 (PA14_69690) is characterized by a crystal structure at 1.69\u2009\u00c5 resolution, revealing a homodimer in the open conformation in which one of the monomers was found inactivated by disulfide formation between the two catalytic cysteines of the active site. Further, the influence of substrate and product on the stability of the enzyme has been investigated, finding that both significantly increase the melting temperature. We determined enzyme kinetic parameters with a coupled enzyme assay. With\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>\n                      <jats:italic>M<\/jats:italic>\n                    <\/jats:sub>\n                    \u2009=\u2009211\u2009\u03bcM (95% confidence interval: 169\u2013267\u2009\u03bcM) and\n                    <jats:italic>k<\/jats:italic>\n                    <jats:sub>cat<\/jats:sub>\n                    of 76\u2009s\n                    <jats:sup>\u22121<\/jats:sup>\n                    (95% confidence interval: 69\u201385\u2009s\n                    <jats:sup>\u22121<\/jats:sup>\n                    ),\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>P. aeruginosa<\/jats:italic>\n                    <\/jats:styled-content>\n                    PA14 DapF has activity levels comparable to homologues from other bacterial species. Finally, we show that a previously observed interaction between DapF and the Nudix hydrolase RppH in\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>E. coli<\/jats:italic>\n                    <\/jats:styled-content>\n                    is conserved in\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>P. aeruginosa<\/jats:italic>\n                    <\/jats:styled-content>\n                    . Soluble recombinant\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>P. aeruginosa<\/jats:italic>\n                    <\/jats:styled-content>\n                    RppH could only be obtained when the hydrolase was co\u2010expressed with DapF, hinting at a moonlighting chaperone activity of\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>P. aeruginosa<\/jats:italic>\n                    <\/jats:styled-content>\n                    DapF. The catalytic activity of DapF was not affected by complex formation with RppH.\n                  <\/jats:p>","DOI":"10.1002\/prot.70161","type":"journal-article","created":{"date-parts":[[2026,7,29]],"date-time":"2026-07-29T01:30:47Z","timestamp":1785288647000},"page":"2002-2012","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structural and Biochemical Characterization of the Diaminopimelate Epimerase\n                    <scp>DapF<\/scp>\n                    From\n                    <scp>\n                      <i>Pseudomonas aeruginosa<\/i>\n                      PA14\n                    <\/scp>"],"prefix":"10.1002","volume":"94","author":[{"given":"Philipp","family":"Schneider","sequence":"first","affiliation":[{"name":"Department Structure and Function of Proteins Helmholtz Centre for Infection Research  Braunschweig Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudia","family":"Hanko","sequence":"additional","affiliation":[{"name":"Department Structure and Function of Proteins Helmholtz Centre for Infection Research  Braunschweig Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Konrad","family":"B\u00fcssow","sequence":"additional","affiliation":[{"name":"Department Structure and Function of Proteins Helmholtz Centre for Infection Research  Braunschweig Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan","family":"Schmelz","sequence":"additional","affiliation":[{"name":"Department Structure and Function of Proteins Helmholtz Centre for Infection Research  Braunschweig Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wulf","family":"Blankenfeldt","sequence":"additional","affiliation":[{"name":"Department Structure and Function of Proteins Helmholtz Centre for Infection Research  Braunschweig Germany"},{"name":"Institute for Biochemistry, Biotechnology and Bioinformatics Technische Universit\u00e4t Braunschweig  Braunschweig Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,7,28]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"publisher","DOI":"10.1136\/bmj.2.2746.353"},{"key":"e_1_2_10_3_1","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/17.6.689"},{"key":"e_1_2_10_4_1","first-page":"226","article-title":"On the Antibacterial Action of Cultures of a Penicillium","volume":"10","author":"Fleming A.","year":"1929","journal-title":"British Journal of Experimental Pathology"},{"key":"e_1_2_10_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.mib.2019.10.008"},{"key":"e_1_2_10_6_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.8153615"},{"key":"e_1_2_10_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.livsci.2020.104251"},{"key":"e_1_2_10_8_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0046505"},{"key":"e_1_2_10_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tim.2011.04.005"},{"key":"e_1_2_10_10_1","unstructured":"World Health Organization \u201cTen Threats to Global Health in 2019 \u201d(2019)."},{"key":"e_1_2_10_11_1","unstructured":"World Health Organization \u201cAntibiotic Resistance \u201d(2020)."},{"key":"e_1_2_10_12_1","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.15.2.194-222.2002"},{"key":"e_1_2_10_13_1","first-page":"1627","article-title":"Infections Caused by \n                     Pseudomonas aeruginosa","volume":"54","author":"Bodey G. 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