{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T20:27:12Z","timestamp":1777321632315,"version":"3.51.4"},"reference-count":29,"publisher":"Proceedings of the National Academy of Sciences","issue":"26","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2002,12,24]]},"abstract":"<jats:p>\n            Synthesis of inorganic polyphosphate (poly P) from the terminal phosphate of ATP is catalyzed reversibly by poly P kinase (PPK, now designated PPK1) initially isolated from\n            <jats:italic>Escherichia coli<\/jats:italic>\n            . PPK1 is highly conserved in many bacteria, including some of the major pathogens such as\n            <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n            . In a null mutant of\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            lacking\n            <jats:italic>ppk1<\/jats:italic>\n            , we have discovered a previously uncharacterized PPK activity (designated PPK2) distinguished from PPK1 by the following: synthesis of poly P from GTP or ATP, a preference for Mn\n            <jats:sup>2+<\/jats:sup>\n            over Mg\n            <jats:sup>2+<\/jats:sup>\n            , and a stimulation by poly P. The reverse reaction, a poly P-driven nucleoside diphosphate kinase synthesis of GTP from GDP, is 75-fold greater than the forward reaction, poly P synthesis from GTP. The gene encoding PPK2 (\n            <jats:italic>ppk2<\/jats:italic>\n            ) was identified from the amino acid sequence of the protein purified near 1,000-fold, to homogeneity. The 5\u2032-end is 177 bp upstream of the annotated genome sequence of a \u201cconserved hypothetical protein\u201d;\n            <jats:italic>ppk2<\/jats:italic>\n            (1,074 bp) encodes a protein of 357 aa with a molecular mass of 40.8 kDa. Sequences homologous to PPK2 are present in two other proteins in\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            , in two Archaea, and in 32 other bacteria (almost all with PPK1 as well); these include rhizobia, cyanobacteria,\n            <jats:italic>Streptomyces<\/jats:italic>\n            , and several pathogenic species. Distinctive features of the poly P-driven nucleoside diphosphate kinase activity and structural aspects of PPK2 are among the subjects of an accompanying report.\n          <\/jats:p>","DOI":"10.1073\/pnas.262655199","type":"journal-article","created":{"date-parts":[[2002,12,23]],"date-time":"2002-12-23T18:14:48Z","timestamp":1040667288000},"page":"16678-16683","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":224,"title":["A polyphosphate kinase (PPK2) widely conserved in bacteria"],"prefix":"10.1073","volume":"99","author":[{"given":"Haiyu","family":"Zhang","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307"}]},{"given":"Kazuya","family":"Ishige","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307"}]},{"given":"Arthur","family":"Kornberg","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307"}]}],"member":"341","published-online":{"date-parts":[[2002,12,16]]},"reference":[{"key":"e_1_3_3_1_2","unstructured":"Kulaev I. 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