{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,8]],"date-time":"2026-01-08T00:18:58Z","timestamp":1767831538377,"version":"3.49.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1989,10,15]]},"abstract":"<jats:p>The finding that N-glycoloylneuraminic acid (Neu5Gc) in pig submandibular gland is synthesized by hydroxylation of the sugar nucleotide CMP-Neu5Ac [Shaw &amp; Schauer (1988) Biol. Chem. Hoppe-Seyler 369, 477-486] prompted us to investigate further the biosynthesis of this sialic acid in mouse liver. Free [14C]Neu5Ac, CMP-[14C]Neu5Ac and [14C]Neu5Ac glycosidically bound by Gal alpha 2-3- and Gal alpha 2-6-GlcNAc beta 1-4 linkages to fetuin were employed as potential substrates in experiments with fractionated mouse liver homogenates. The only substrate to be hydroxylated was the CMP-Neu5Ac glycoside. The product of the reaction was identified by chemical and enzymic methods as CMP-Neu5Gc. All of the CMP-Neu5Ac hydroxylase activity was detected in the high-speed supernatant fraction. The hydroxylase required a reduced nicotinamide nucleotide [NAD(P)H] coenzyme and molecular oxygen for activity. Furthermore, the activity of this enzyme was enhanced by exogenously added Fe2+ or Fe3+ ions, all other metal salts tested having a negligible or inhibitory influence. This hydroxylase is therefore tentatively classified as a monooxygenase. The cofactor requirement and CMP-Neu5Ac substrate specificity are identical to those of the enzyme in high-speed supernatants of pig submandibular gland, suggesting that this is a common route of Neu5Gc biosynthesis. The relevance of these results to the regulation of Neu5Gc expression in sialoglycoconjugates is discussed.<\/jats:p>","DOI":"10.1042\/bj2630355","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:14:21Z","timestamp":1439241261000},"page":"355-363","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":55,"title":["Detection of CMP-<i>N<\/i>-acetylneuraminic acid hydroxylase activity in fractionated mouse liver"],"prefix":"10.1042","volume":"263","author":[{"given":"L","family":"Shaw","sequence":"first","affiliation":[{"name":"Biochemisches Institut, Christian-Albrechts-Universitat Kiel, Olshausenstrasse 40, D-2300 Kiel 1, Federal Republic of Germany."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R","family":"Schauer","sequence":"additional","affiliation":[{"name":"Biochemisches Institut, Christian-Albrechts-Universitat Kiel, Olshausenstrasse 40, D-2300 Kiel 1, Federal Republic of Germany."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/263\/2\/355\/597814\/bj2630355.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/263\/2\/355\/597814\/bj2630355.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T18:09:49Z","timestamp":1637863789000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/263\/2\/355\/24588\/Detection-of-CMP-N-acetylneuraminic-acid"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1989,10,15]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1989,10,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2630355","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1989,10,15]]}}}