{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T13:40:57Z","timestamp":1792503657564,"version":"4.5.0"},"reference-count":161,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T00:00:00Z","timestamp":1792454400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T00:00:00Z","timestamp":1792454400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"abstract":"<jats:p>\n                    ATP phosphoribosyltransferase (ATPPRT) catalyses the first reaction of L\u2010histidine biosynthesis: the condensation of ATP and 5\u2010phospho\u2010\u03b1\u2010\n                    <jats:italic>\n                      <jats:sc>d<\/jats:sc>\n                    <\/jats:italic>\n                    \u2010ribose 1\u2010pyrophosphate to form\n                    <jats:italic>N<\/jats:italic>\n                    <jats:sup>1<\/jats:sup>\n                    \u2010(5\u2010phospho\u2010\u03b2\u2010\n                    <jats:italic>\n                      <jats:sc>d<\/jats:sc>\n                    <\/jats:italic>\n                    \u2010ribosyl)\u2010ATP with the release of inorganic pyrophosphate. L\u2010Histidine allosterically inhibits ATPPRT as a mechanism to regulate this energy\u2010intensive pathway in histidine\u2010synthesising organisms, such as bacteria, archaea and plants. Absent in humans and essential in many disease\u2010causing bacteria, such as\n                    <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n                    and\n                    <jats:italic>Acinetobacter baumannii<\/jats:italic>\n                    , ATPPRT is a promising drug target for novel antibiotic development. Furthermore, ATPPRT is a target of synthetic biology efforts to maximise L\u2010histidine production in bacteria. Here we provide a brief overview of allosteric concepts and review the structure, catalysis and allosteric mechanism of bacterial ATPPRTs, which exist in two forms in nature, a long and a short form. We highlight recent findings on ATPPRT catalysis, allosteric regulation, inhibition and activation, discuss open questions in the field, and possible industrial and biomedical applications.\n                  <\/jats:p>","DOI":"10.1111\/febs.70769","type":"journal-article","created":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T12:55:56Z","timestamp":1792500956000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Catalysis and allostery in bacterial\n                    <scp>ATP<\/scp>\n                    phosphoribosyltransferases"],"prefix":"10.1111","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-4480-5611","authenticated-orcid":false,"given":"Lillian G.","family":"Bates","sequence":"first","affiliation":[{"name":"School of Biology, Biomedical Sciences Research Complex University of St Andrews  UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1308-8190","authenticated-orcid":false,"given":"Rafael G.","family":"da Silva","sequence":"additional","affiliation":[{"name":"School of Biology, Biomedical Sciences Research Complex University of St Andrews  UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,10,20]]},"reference":[{"key":"e_1_2_21_2_1","first-page":"21","volume-title":"Dynamics of Growth Processes","author":"Novick A","year":"1954"},{"key":"e_1_2_21_3_1","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/S0021-9258(19)77271-8","article-title":"Isoleucine and valine metabolism in Escherichia coli: V. \u03b1\u2010ketoisovaleric acid accumulation","volume":"205","author":"Adelberg EA","year":"1953","journal-title":"J Biol 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