{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T18:50:30Z","timestamp":1790707830999,"version":"4.1.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1994,1,15]]},"abstract":"<jats:p>This study was undertaken to search for the endogenous dithiol cofactor of the reductases of the vitamin K cycle. As a starting point, the redox-active lipophilic endogenous compounds lipoic acid and lipoamide were looked at. The study shows that microsomes contain NADH-dependent lipoamide reductase activity. Reduced lipoamide stimulates microsomal vitamin K epoxide reduction with kinetics comparable with those for the synthetic dithiol dithiothreitol (DTT). Reduced lipoic acid shows higher (4-fold) Km values. No reductase activity with lipoic acid was found to be present in microsomes or cytosol. The reduced-lipoamide-stimulated vitamin K epoxide reductase is as sensitive to warfarin and salicylate inhibition as is the DTT-stimulated one. Both vitamin K epoxide reductase and lipoamide reductase activity are recovered in the rough microsomes. NADH\/lipoamide-stimulated vitamin K epoxide reduction is uncoupled by traces of Triton X-100, suggesting that microsomal lipoamide reductase and vitamin K epoxide reductase are associated. The results suggest that the vitamin K cycle obtains reducing equivalents from NADH through microsomal lipoamide reductase.<\/jats:p>","DOI":"10.1042\/bj2970277","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:36:00Z","timestamp":1439242560000},"page":"277-280","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Microsomal lipoamide reductase provides vitamin K epoxide reductase with reducing equivalents"],"prefix":"10.1042","volume":"297","author":[{"given":"H H W","family":"Thijssen","sequence":"first","affiliation":[{"name":"Department of Pharmacology, University of Limburg, Maastricht, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Y P G","family":"Janssen","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, University of Limburg, Maastricht, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L T M","family":"Vervoort","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, University of Limburg, Maastricht, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/297\/2\/277\/724016\/bj2970277.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/297\/2\/277\/724016\/bj2970277.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T22:22:12Z","timestamp":1637706132000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/297\/2\/277\/30016\/Microsomal-lipoamide-reductase-provides-vitamin-K"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,1,15]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1994,1,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2970277","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1994,1,15]]}}}