ArticleGlycoconjugate journal2000
Characterisation of the enzymatic 4-O-acetylation of sialic acids in microsomes from equine submandibular glands.
Article in Glycoconjugate journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Exploration of the Sialic Acid World.Advances in carbohydrate chemistry and biochemistry · 2018Review
- Functions and Biosynthesis of O-Acetylated Sialic Acids.Topics in current chemistry · 2015Review
- Sialic acid metabolism and sialyltransferases: natural functions and applications.Applied microbiology and biotechnology · 2012Review
- Modifications of glycans: biological significance and therapeutic opportunities.ACS chemical biology · 2012Review
- The human Cas1 protein: a sialic acid-specific O-acetyltransferase?Glycobiology · 2011Article
- Chemo-enzymatic synthesis of C-9 acetylated sialosides.Carbohydrate research · 2008Article
- Carbohydrate post-glycosylational modifications.Organic & biomolecular chemistry · 2007Article
- Highly efficient chemoenzymatic synthesis of naturally occurring and non-natural alpha-2,6-linked sialosides: a P. damsela alpha-2,6-sialyltransferase with extremely flexible donor-substrate specificity.Angewandte Chemie (International ed. in English) · 2006Article
- Localisation and distribution of O-acetylated N-acetylneuraminic acids, the endogenous substrates of the hemagglutinin-esterases of murine coronaviruses, in mouse tissue.Glycoconjugate journal · 2006Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microsomes prepared from equine submandibular glands and incubated with tritium-labelled AcCoA incorporated acid-insoluble radioactivity in a manner dependent on time, protein, membrane integrity and AcCoA concentration, with incorporation being optimal at 37 degrees C and pH 6.6. Under the experimental conditions used a K(M) of 32.1 microM for AcCoA and a V(max) of 1.2 pmol/mg protein x min was obtained. The incorporation of acid-insoluble radioactivity was also inhibited by CoA in a competitive manner (K(i)=240 microM), as well as by para-chloromercuribenzoate, 3'-dephospho-CoA, 5'-IDP, 5'-ADP, beta-NAD and 4,4'-diisothiocyanatostilbene-2,2'-disulfonate. We demonstrate here that this incorporation of radioactivity into endogenous sialic acid is due to the action of an AcCoA:sialate-4-O-acetyltransferase [EC 2.3.1.44]. Radio thin-layer chromatography analyses of propionic acid-released sialic acids showed that the incorporation of radioactivity correlated with the formation of a radiolabelled species that co-migrated with authentic Neu4,5Ac2. Saponification experiments using NaOH, mouse hepatitis virus strain S and Influenza C/JJ/50 virus also showed that the transfer of [3H]acetyl groups from [3H]AcCoA to endogenous sialic acid acceptors was occurring exclusively at carbon 4 of the pyranose ring.
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