{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T06:57:12Z","timestamp":1791615432455,"version":"4.3.4"},"reference-count":54,"publisher":"American Society for Microbiology","issue":"19","license":[{"start":{"date-parts":[[2015,10,1]],"date-time":"2015-10-01T00:00:00Z","timestamp":1443657600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2015,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Phosphorus is an important macronutrient, but its availability in soil is limited. Many soil microorganisms improve the bioavailability of phosphate by releasing it from various organic compounds, including phytate. To investigate the diversity of phytate-hydrolyzing bacteria in soil, we sampled soils of various ecological habitats, including forest, private homesteads, large agricultural complexes, and urban landscapes. Bacterial isolate\n            <jats:named-content content-type=\"genus-species\">Pantoea<\/jats:named-content>\n            sp. strain 3.5.1 with the highest level of phytase activity was isolated from forest soil and investigated further. The\n            <jats:named-content content-type=\"genus-species\">Pantoea<\/jats:named-content>\n            sp. 3.5.1\n            <jats:italic>agpP<\/jats:italic>\n            gene encoding a novel glucose-1-phosphatase with high phytase activity was identified, and the corresponding protein was purified to apparent homogeneity, sequenced by mass spectroscopy, and biochemically characterized. The AgpP enzyme exhibits maximum activity and stability at pH 4.5 and at 37\u00b0C. The enzyme belongs to a group of histidine acid phosphatases and has the lowest\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            values toward phytate, glucose-6-phosphate, and glucose-1-phosphate. Unexpectedly, stimulation of enzymatic activity by several divalent metal ions was observed for the AgpP enzyme. High-performance liquid chromatography (HPLC) and high-performance ion chromatography (HPIC) analyses of phytate hydrolysis products identify\n            <jats:sc>dl<\/jats:sc>\n            -\n            <jats:italic>myo<\/jats:italic>\n            -inositol 1,2,4,5,6-pentakisphosphate as the final product of the reaction, indicating that the\n            <jats:named-content content-type=\"genus-species\">Pantoea<\/jats:named-content>\n            sp. AgpP glucose-1-phosphatase can be classified as a 3-phytase. The identification of the\n            <jats:named-content content-type=\"genus-species\">Pantoea<\/jats:named-content>\n            sp. AgpP phytase and its unusual regulation by metal ions highlight the remarkable diversity of phosphorus metabolism regulation in soil bacteria. Furthermore, our data indicate that natural forest soils harbor rich reservoirs of novel phytate-hydrolyzing enzymes with unique biochemical features.\n          <\/jats:p>","DOI":"10.1128\/aem.01384-15","type":"journal-article","created":{"date-parts":[[2015,7,25]],"date-time":"2015-07-25T03:34:15Z","timestamp":1437795255000},"page":"6790-6799","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":55,"title":["Novel Glucose-1-Phosphatase with High Phytase Activity and Unusual Metal Ion Activation from Soil Bacterium Pantoea sp. Strain 3.5.1"],"prefix":"10.1128","volume":"81","author":[{"given":"Aliya D.","family":"Suleimanova","sequence":"first","affiliation":[{"name":"Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, Kazan, Republic of Tatarstan, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Astrid","family":"Beinhauer","sequence":"additional","affiliation":[{"name":"Department of Food Technology and Bioprocess Engineering, Max Rubner Institut, Karlsruhe, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liia R.","family":"Valeeva","sequence":"additional","affiliation":[{"name":"Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, Kazan, Republic of Tatarstan, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Inna B.","family":"Chastukhina","sequence":"additional","affiliation":[{"name":"Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, Kazan, Republic of Tatarstan, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nelly P.","family":"Balaban","sequence":"additional","affiliation":[{"name":"Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, Kazan, Republic of Tatarstan, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2689-7410","authenticated-orcid":false,"given":"Eugene V.","family":"Shakirov","sequence":"additional","affiliation":[{"name":"Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, Kazan, Republic of Tatarstan, Russia"},{"name":"Department of Integrative Biology, University of Texas at Austin, Austin, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ralf","family":"Greiner","sequence":"additional","affiliation":[{"name":"Department of Food Technology and Bioprocess Engineering, Max Rubner Institut, Karlsruhe, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Margarita R.","family":"Sharipova","sequence":"additional","affiliation":[{"name":"Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, Kazan, Republic of Tatarstan, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/461716a"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0018829"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6941.2009.00762.x"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1002\/jssc.201400026"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.pep.2009.10.001"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00253-003-1345-0"},{"key":"e_1_3_3_8_2","first-page":"291","article-title":"Microorganisms as phytase producers","volume":"81","author":"Mukhametzianova AD","year":"2012","unstructured":"Mukhametzianova AD, Akhmetova AI, Sharipova MR. 2012. 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