{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T10:39:16Z","timestamp":1791110356582,"version":"4.1.0"},"reference-count":32,"publisher":"National Academy of Sciences","issue":"49","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2004,12,7]]},"abstract":"<jats:p>\n                    Chains of inorganic polyphosphate (poly-P) with hundreds of P\n                    <jats:sub>i<\/jats:sub>\n                    residues linked by phosphoanhydride bonds, as in ATP, are found in every bacterial, fungal, plant, and animal cell, in which they perform various functions. In the spore-forming\n                    <jats:italic>Bacillus cereus<\/jats:italic>\n                    , we have identified three principal enzymes and genes involved in the metabolism of poly-P, namely, (\n                    <jats:italic>i<\/jats:italic>\n                    ) poly-P kinase (PPK), which synthesizes poly-P reversibly from ATP, (\n                    <jats:italic>ii<\/jats:italic>\n                    ) exopolyphosphatase (PPX), which hydrolyzes poly-P to P\n                    <jats:sub>i<\/jats:sub>\n                    , and (\n                    <jats:italic>iii<\/jats:italic>\n                    ) poly-P\/AMP phosphotransferase (PAP), which uses poly-P as a donor to convert AMP to ADP, reversibly. In the null mutant of\n                    <jats:italic>ppk<\/jats:italic>\n                    , poly-P levels are reduced to &lt;5% of the WT; in the\n                    <jats:italic>ppx<\/jats:italic>\n                    mutant, the PPK activity is elevated 10-fold, and the accumulation of poly-P is elevated \u22481,000-fold. All of the null mutants of\n                    <jats:italic>ppk<\/jats:italic>\n                    ,\n                    <jats:italic>ppx<\/jats:italic>\n                    , and\n                    <jats:italic>pap<\/jats:italic>\n                    showed defects in motility and biofilm formation, but sporulation efficiency was impaired only in the\n                    <jats:italic>ppx<\/jats:italic>\n                    mutant. These enzymes and genes in\n                    <jats:italic>B. cereus<\/jats:italic>\n                    are nearly identical to those in the very closely related pathogen\n                    <jats:italic>Bacillus anthracis<\/jats:italic>\n                    , and, thus, they may provide attractive targets for the treatment of anthrax.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0407787101","type":"journal-article","created":{"date-parts":[[2004,11,30]],"date-time":"2004-11-30T20:14:05Z","timestamp":1101845645000},"page":"17061-17065","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":103,"title":["Inorganic polyphosphate in\n                    <i>Bacillus cereus<\/i>\n                    : Motility, biofilm formation, and sporulation"],"prefix":"10.1073","volume":"101","author":[{"given":"Xiaobing","family":"Shi","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Narayana N.","family":"Rao","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arthur","family":"Kornberg","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2004,11,30]]},"reference":[{"key":"e_1_3_2_1_2","unstructured":"Kulaev I. 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