{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,15]],"date-time":"2026-05-15T12:45:19Z","timestamp":1778849119052,"version":"3.51.4"},"reference-count":33,"publisher":"Wiley","issue":"24","license":[{"start":{"date-parts":[[2002,12,11]],"date-time":"2002-12-11T00:00:00Z","timestamp":1039564800000},"content-version":"vor","delay-in-days":10,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[2002,12]]},"abstract":"\n The pathway of the oxidation of propionate to pyruvate in\n Escherichia coli<\/jats:italic>\n involves five enzymes, only two of which, methylcitrate synthase and 2\u2010methylisocitrate lyase, have been thoroughly characterized. Here we report that the isomerization of (2\n S<\/jats:italic>\n ,3\n S<\/jats:italic>\n )\u2010methylcitrate to (2\n R<\/jats:italic>\n ,3\n S<\/jats:italic>\n )\u20102\u2010methylisocitrate requires a novel enzyme, methylcitrate dehydratase (PrpD), and the well\u2010known enzyme, aconitase (AcnB), of the tricarboxylic acid cycle. AcnB was purified as 2\u2010methylaconitate hydratase from\n E.\u2003coli<\/jats:italic>\n cells grown on propionate and identified by its N\u2010terminus. The enzyme has an apparent\n K<\/jats:italic>\n m<\/jats:sub>\n of 210\u2003\u00b5\n m<\/jats:sc>\n for (2\n R<\/jats:italic>\n ,3\n S<\/jats:italic>\n )\u20102\u2010methylisocitrate but shows no activity with (2\n S<\/jats:italic>\n ,3\n S<\/jats:italic>\n )\u2010methylcitrate. On the other hand, PrpD is specific for (2\n S<\/jats:italic>\n ,3\n S<\/jats:italic>\n )\u2010methylcitrate (\n K<\/jats:italic>\n m<\/jats:sub>\n \u2003=\u2003440\u2003\u00b5\n m<\/jats:sc>\n ) and catalyses in addition only the hydration of\n cis<\/jats:italic>\n \u2010aconitate at a rate that is five times lower. The product of the dehydration of enzymatically synthesized (2\n S<\/jats:italic>\n ,3\n S<\/jats:italic>\n )\u2010methylcitrate was designated\n cis<\/jats:italic>\n \u20102\u2010methylaconitate because of its ability to form a cyclic anhydride at low pH. Hence, PrpD catalyses an unusual\n syn<\/jats:italic>\n elimination, whereas the addition of water to\n cis<\/jats:italic>\n \u20102\u2010methylaconitate occurs in the usual\n anti<\/jats:italic>\n manner. The different stereochemistries of the elimination and addition of water may be the reason for the requirement for the novel methylcitrate dehydratase (PrpD), the sequence of which seems not to be related to any other enzyme of known function. Northern\u2010blot experiments showed expression of\n acnB<\/jats:italic>\n under all conditions tested, whereas the RNA of enzymes of the\n prp<\/jats:italic>\n operon (PrpE, a propionyl\u2010CoA synthetase, and PrpD) was exclusively present during growth on propionate. 2D gel electrophoresis showed the production of all proteins encoded by the\n prp<\/jats:italic>\n operon during growth on propionate as sole carbon and energy source, except PrpE, which seems to be replaced by acetyl\u2010CoA synthetase. This is in good agreement with investigations on\n Salmonella enterica<\/jats:italic>\n LT2, in which disruption of the\n prpE<\/jats:italic>\n gene showed no visible phenotype.\n <\/jats:p>","DOI":"10.1046\/j.1432-1033.2002.03336.x","type":"journal-article","created":{"date-parts":[[2003,3,11]],"date-time":"2003-03-11T13:37:33Z","timestamp":1047389853000},"page":"6184-6194","source":"Crossref","is-referenced-by-count":125,"title":["Oxidation of propionate to pyruvate in\n Escherichia coli<\/i>"],"prefix":"10.1111","volume":"269","author":[{"given":"Matthias","family":"Brock","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Claudia","family":"Maerker","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexandra","family":"Sch\u00fctz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Uwe","family":"V\u00f6lker","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wolfgang","family":"Buckel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2002,12,11]]},"reference":[{"key":"e_1_2_25_2_2","doi-asserted-by":"publisher","DOI":"10.1271\/bbb1961.38.2571"},{"key":"e_1_2_25_3_2","doi-asserted-by":"publisher","DOI":"10.1271\/bbb1961.39.2035"},{"key":"e_1_2_25_4_2","doi-asserted-by":"publisher","DOI":"10.1271\/bbb1961.41.169"},{"key":"e_1_2_25_5_2","doi-asserted-by":"publisher","DOI":"10.1271\/bbb1961.45.2823"},{"key":"e_1_2_25_6_2","doi-asserted-by":"publisher","DOI":"10.1271\/bbb.59.2013"},{"key":"e_1_2_25_7_2","doi-asserted-by":"publisher","DOI":"10.1271\/bbb.59.1825"},{"key":"e_1_2_25_8_2","doi-asserted-by":"publisher","DOI":"10.1007\/s002030050518"},{"key":"e_1_2_25_9_2","doi-asserted-by":"crossref","first-page":"5615","DOI":"10.1128\/JB.181.18.5615-5623.1999","article-title":"Salmonella typhimurium LT2 catabolizes propionate via the 2\u2010 methylcitric acid cycle","volume":"181","author":"Horswill A.R.","year":"1999","journal-title":"J. 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