{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T16:40:15Z","timestamp":1792255215072,"version":"4.4.0"},"reference-count":29,"publisher":"National Academy of Sciences","issue":"25","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2001,12,4]]},"abstract":"<jats:p>\u03b2-Lactamases are the resistance enzymes for \u03b2-lactam\n antibiotics, of which four classes are known. \u03b2-lactamases hydrolyze\n the \u03b2-lactam moieties of these antibiotics, rendering them inactive.\n It is shown herein that the class D OXA-10 \u03b2-lactamase depends\n critically on an unusual carbamylated lysine as the basic residue for\n both the enzyme acylation and deacylation steps of catalysis. The\n formation of carbamylated lysine is reversible. Evidence is presented\n that this enzyme is dimeric and carbamylated in living bacteria.\n High-resolution x-ray structures for the native enzyme were determined\n at pH values of 6.0, 6.5, 7.5, and 8.5. Two dimers are present per\n asymmetric unit. One monomer in each dimer was carbamylated at pH 6.0,\n whereas all four monomers were fully carbamylated at pH 8.5. At the\n intermediate pH values, one monomer of each dimer was carbamylated, and\n the other showed a mixture of carbamylated and non-carbamylated\n lysines. It would appear that, as the pH increased for the sample,\n additional lysines were \u201ctitrated\u201d by carbamylation. A handful of\n carbamylated lysines are known from protein crystallographic data, all\n of which have been attributed roles in structural stabilization (mostly\n as metal ligands) of the proteins. This paper reports a previously\n unrecognized role for a noncoordinated carbamylate lysine as a\n basic residue involved in mechanistic reactions of an enzyme, which\n indicates another means for expansion of the catalytic capabilities of\n the amino acids in nature beyond the 20 common amino acids in\n development of biological catalysts.<\/jats:p>","DOI":"10.1073\/pnas.241442898","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:35:07Z","timestamp":1027679707000},"page":"14280-14285","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":232,"title":["Critical involvement of a carbamylated lysine in catalytic function of class D \u03b2-lactamases"],"prefix":"10.1073","volume":"98","author":[{"given":"Dasantila","family":"Golemi","sequence":"first","affiliation":[{"name":"Groupe de Cristallographie Biologique, Institut de\r Pharmacologie et de Biologie Structurale du Centre National de la\r Recherche Scientifique, 205 Route de Narbonne, 31077-Toulouse Cedex,\r France; and Institute for Drug Design and the Department of Chemistry,\r Wayne State University, 5101 Cass Avenue, Detroit, MI 48202-3489"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laurent","family":"Maveyraud","sequence":"additional","affiliation":[{"name":"Groupe de Cristallographie Biologique, Institut de\r Pharmacologie et de Biologie Structurale du Centre National de la\r Recherche Scientifique, 205 Route de Narbonne, 31077-Toulouse Cedex,\r France; and Institute for Drug Design and the Department of Chemistry,\r Wayne State University, 5101 Cass Avenue, Detroit, MI 48202-3489"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergei","family":"Vakulenko","sequence":"additional","affiliation":[{"name":"Groupe de Cristallographie Biologique, Institut de\r Pharmacologie et de Biologie Structurale du Centre National de la\r Recherche Scientifique, 205 Route de Narbonne, 31077-Toulouse Cedex,\r France; and Institute for Drug Design and the Department of Chemistry,\r Wayne State University, 5101 Cass Avenue, Detroit, MI 48202-3489"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Pierre","family":"Samama","sequence":"additional","affiliation":[{"name":"Groupe de Cristallographie Biologique, Institut de\r Pharmacologie et de Biologie Structurale du Centre National de la\r Recherche Scientifique, 205 Route de Narbonne, 31077-Toulouse Cedex,\r France; and Institute for Drug Design and the Department of Chemistry,\r Wayne State University, 5101 Cass Avenue, Detroit, MI 48202-3489"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shahriar","family":"Mobashery","sequence":"additional","affiliation":[{"name":"Groupe de Cristallographie Biologique, Institut de\r Pharmacologie et de Biologie Structurale du Centre National de la\r Recherche Scientifique, 205 Route de Narbonne, 31077-Toulouse Cedex,\r France; and Institute for Drug Design and the Department of Chemistry,\r Wayne State University, 5101 Cass Avenue, Detroit, MI 48202-3489"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2001,11,27]]},"reference":[{"key":"e_1_3_3_1_2","volume-title":"Chem. 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