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The coenzyme carries a glutamic acid-derived tail, the length of which influences the metabolism of\n            <jats:named-content content-type=\"genus-species\">M. tuberculosis<\/jats:named-content>\n            . Mutations that eliminate the production of F\n            <jats:sub>420<\/jats:sub>\n            with longer tails make\n            <jats:named-content content-type=\"genus-species\">M. tuberculosis<\/jats:named-content>\n            resistant to two new tuberculosis drugs. This report describes that the synthesis of longer glutamyl tails of F\n            <jats:sub>420<\/jats:sub>\n            requires concerted actions of two enzymes, one of which reduces the coenzyme prior to the action of the other, which catalyzes polyglutamylation. This knowledge will help to develop more effective tuberculosis (TB) drugs. Remarkably, the introduction of multiple glutamate residues into the sidechain of folate (vitamin B\n            <jats:sub>9<\/jats:sub>\n            ) requires similar concerted actions, where one enzyme reduces the vitamin to tetrahydrofolate and the other catalyzes polyglutamylation; folate is required for DNA and amino acid synthesis. Thus, the reported research has also revealed a key similarity between two important cellular systems.\n          <\/jats:p>","DOI":"10.1128\/jb.00375-18","type":"journal-article","created":{"date-parts":[[2018,9,21]],"date-time":"2018-09-21T17:57:55Z","timestamp":1537552675000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":11,"title":["Coenzyme F\n            <sub>420<\/sub>\n            -Dependent Glucose-6-Phosphate Dehydrogenase-Coupled Polyglutamylation of Coenzyme F\n            <sub>420<\/sub>\n            in Mycobacteria"],"prefix":"10.1128","volume":"200","author":[{"given":"Endang","family":"Purwantini","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Virginia Tech, Blacksburg, Virginia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Usha","family":"Loganathan","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Virginia Tech, Blacksburg, Virginia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Biswarup","family":"Mukhopadhyay","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Virginia Tech, Blacksburg, Virginia, USA"},{"name":"Biocomplexity Institute, Virginia Tech, Blacksburg, Virginia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1007\/s002030100290"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00615a002"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.140.1.20-27.1979"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.55.4.940-945.1989"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2017.01000"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.59.070190.002035"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.00070-15"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M109.074310"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01035-15"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0812883106"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0081985"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0030114"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2010.07356.x"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1111\/mmi.12127"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1023\/A:1014447700775"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1271\/bbb.68.1345"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja403516u"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1164571"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.str.2011.11.001"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1038\/35016103"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.02693-13"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tube.2017.12.006"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.172.10.6061-6065.1990"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0812665106"},{"key":"e_1_3_2_26_2","doi-asserted-by":"crossref","first-page":"8009","DOI":"10.1016\/S0021-9258(19)39031-3","article-title":"DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans","volume":"265","author":"Eker AP","year":"1990","unstructured":"Eker AP, Kooiman P, Hessels JK, Yasui A. 1990. 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