{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T17:20:34Z","timestamp":1791220834689,"version":"4.1.0"},"reference-count":20,"publisher":"American Society for Microbiology","issue":"15","license":[{"start":{"date-parts":[[2006,8,1]],"date-time":"2006-08-01T00:00:00Z","timestamp":1154390400000},"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":["J Bacteriol"],"published-print":{"date-parts":[[2006,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Tricarballylate is the causative agent of grass tetany, a ruminant disease characterized by acute magnesium deficiency. Tricarballylate toxicity has been attributed to its ability to chelate magnesium and to inhibit aconitase, a Krebs cycle enzyme. Neither the ruminant nor the normal rumen flora can catabolize tricarballylate to ameliorate its toxic effects. However, the gram-negative enterobacterium\n            <jats:italic>Salmonella enterica<\/jats:italic>\n            can use tricarballylate as a carbon and energy source, providing an opportunity to study the genes and enzymes required for tricarballylate catabolism. The tricarballylate utilization (\n            <jats:italic>tcu<\/jats:italic>\n            ) genes are organized into two transcriptional units, i.e.,\n            <jats:italic>tcuR<\/jats:italic>\n            and\n            <jats:italic>tcuABC<\/jats:italic>\n            . Here, we report the initial biochemical analysis of TcuA. TcuA catalyzed the oxidation of tricarballylate to\n            <jats:italic>cis<\/jats:italic>\n            -aconitate. The apparent\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            of TcuA for tricarballylate was 3.8\u2009\u00b1 0.4 mM, with a\n            <jats:italic>V<\/jats:italic>\n            <jats:sub>max<\/jats:sub>\n            of 7.9 \u00b1 0.3 mM min\n            <jats:sup>\u22121<\/jats:sup>\n            , turnover number (\n            <jats:italic>k<\/jats:italic>\n            <jats:sub>cat<\/jats:sub>\n            ) of 6.7 \u00d7 10\n            <jats:sup>\u22122<\/jats:sup>\n            s\n            <jats:sup>\u22121<\/jats:sup>\n            , and a catalytic efficiency (\n            <jats:italic>k<\/jats:italic>\n            <jats:sub>cat<\/jats:sub>\n            \/\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            ) of 17.8 M\n            <jats:sup>\u22121<\/jats:sup>\n            s\n            <jats:sup>\u22121<\/jats:sup>\n            . Optimal activity was measured at pH 7.5 and 30\u00b0C. The enzyme was inactivated at 45\u00b0C. One mole of FAD was present per mole of TcuA. We propose a role for TcuB as an electron shuttle protein responsible for oxidizing FADH\n            <jats:sub>2<\/jats:sub>\n            back to FAD in TcuA.\n          <\/jats:p>","DOI":"10.1128\/jb.00514-06","type":"journal-article","created":{"date-parts":[[2006,7,19]],"date-time":"2006-07-19T22:43:47Z","timestamp":1153349027000},"page":"5479-5486","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":47,"title":["The FAD-Dependent Tricarballylate Dehydrogenase (TcuA) Enzyme of\n            <i>Salmonella enterica<\/i>\n            Converts Tricarballylate into\n            <i>cis<\/i>\n            -Aconitate"],"prefix":"10.1128","volume":"188","author":[{"given":"Jeffrey A.","family":"Lewis","sequence":"first","affiliation":[{"name":"Department of Bacteriology, University of Wisconsin\u2014Madison, Madison, Wisconsin 53726"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jorge C.","family":"Escalante-Semerena","sequence":"additional","affiliation":[{"name":"Department of Bacteriology, University of Wisconsin\u2014Madison, Madison, Wisconsin 53726"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1385\/1-59259-266-X:9","volume":"131","year":"1999","unstructured":"Aliverti, A., B. Curti, and M. A. Vanoni. 1999. Identifying and quantitating FAD and FMN in simple and in iron-sulfur-containing flavoproteins, p. 9-23. In S. K. Chapman and G. A. Reid (ed.), Flavoprotein protocols, vol. 131. Humana Press, Totowa, N.J.","journal-title":"Flavoprotein protocols"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.186.3.595-600.2004"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.62.3.293-300.1951"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_3_2_6_2","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1126\/science.150.3697.766","volume":"150","year":"1965","unstructured":"Burau, R., and P. R. Stout. 1965. trans-Aconitic acid in range grasses in early spring. Science 150 : 766-767.","journal-title":"Science"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.100.1.215-219.1969"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(83)80284-8"},{"key":"e_1_3_2_9_2","doi-asserted-by":"crossref","first-page":"19094","DOI":"10.1074\/jbc.M100244200","volume":"276","year":"2001","unstructured":"Horswill, A. R., A. R. Dudding, and J. C. Escalante-Semerena. 2001. Studies of propionate toxicity in Salmonella enterica identify 2-methylcitrate as a potent inhibitor of cell growth. J. Biol. Chem. 276 : 19094-19101.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_10_2","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","volume":"157","year":"1982","unstructured":"Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 : 105-132.","journal-title":"J. Mol. Biol."},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1038\/227680a0"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.186.6.1629-1637.2004"},{"key":"e_1_3_2_13_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1385\/1-59259-266-X:1","volume":"131","year":"1999","unstructured":"Macheroux, P. 1999. UV-visible spectroscopy as a tool to study flavoproteins, p. 1-7. In S. K. Chapman and G. A. Reid (ed.), Flavoprotein protocols, vol. 131. Humana Press, Totowa, N.J.","journal-title":"Flavoprotein protocols"},{"key":"e_1_3_2_14_2","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1074\/jbc.M411884200","volume":"280","year":"2005","unstructured":"McGoldrick, H. M., C. A. Roessner, E. Raux, A. D. Lawrence, K. J. McLean, A. W. Munro, S. Santabarbara, S. E. Rigby, P. Heathcote, A. I. Scott, and M. J. Warren. 2005. Identification and characterization of a novel vitamin B12 (cobalamin) biosynthetic enzyme (CobZ) from Rhodobacter capsulatus, containing flavin, heme, and Fe-S cofactors. J. Biol. Chem. 280 : 1086-1094.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.49.1.120-126.1985"},{"key":"e_1_3_2_16_2","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1079\/BJN19860095","volume":"56","year":"1986","unstructured":"Russell, J. B., and N. Forsberg. 1986. Production of tricarballylic acid by rumen microorganisms and its potential toxicity in ruminant tissue metabolism. Br. J. Nutr. 56 : 153-162.","journal-title":"Br. J. Nutr."},{"key":"e_1_3_2_17_2","first-page":"10.6.1","volume":"1","year":"1991","unstructured":"Sasse, J. 1991. Detection of proteins, p. 10.6.1-10.6.8. In F. A. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 1. Wiley Interscience, New York, N.Y.","journal-title":"Current protocols in molecular biology"},{"key":"e_1_3_2_18_2","doi-asserted-by":"crossref","first-page":"4572","DOI":"10.1021\/bi00315a010","volume":"23","year":"1984","unstructured":"Schloss, J. V., M. H. Emptage, and W. W. Cleland. 1984. pH profiles and isotope effects for aconitase from Saccharomycopsis lipolytica, beef heart, and beef liver. a-Methyl-cis-aconitate and threo-Ds-a-methylisocitrate as substrates. Biochemistry 23 : 4572-4580.","journal-title":"Biochemistry"},{"key":"e_1_3_2_19_2","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1093\/jn\/118.2.183","volume":"118","year":"1988","unstructured":"Schwartz, R., M. Topley, and J. B. Russell. 1988. Effect of tricarballylic acid, a nonmetabolizable rumen fermentation product of trans-aconitic acid, on Mg, Ca and Zn utilization of rats. J. Nutr. 118 : 183-188.","journal-title":"J. Nutr."},{"key":"e_1_3_2_20_2","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1093\/oxfordjournals.jbchem.a123537","volume":"110","year":"1991","unstructured":"Shimamoto, T., H. Izawa, H. Daimon, N. Ishiguro, M. Shinagawa, Y. Sakano, M. Tsuda, and T. Tsuchiya. 1991. Cloning and nucleotide sequence of the gene (citA) encoding a citrate carrier from Salmonella typhimurium. J. Biochem. (Tokyo) 110 : 22-28.","journal-title":"J. Biochem. (Tokyo)"},{"key":"e_1_3_2_21_2","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1006\/bbrc.1996.1381","volume":"226","year":"1996","unstructured":"Shimamoto, T., K. Negishi, M. Tsuda, and T. Tsuchiya. 1996. Mutational analysis of the CitA citrate transporter from Salmonella typhimurium: altered substrate specificity. Biochem. Biophys. Res. Commun. 226 : 481-487.","journal-title":"Biochem. Biophys. Res. 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