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Sialate 9-0-acetyltransferase

Fig. 13. Metabolism scheme of sialic acids. Anabolic (solid arrow) and catabolic (dashed arrow) reactions are indicated. For literature see the text. Enzymes 1, CMP-sialate synthase (EC 2.7.7.43) 2, sialyltransferases (EC 2.4.99.1.) 3, CMP-Neu5Ac hydroxylase (EC 1.14.99.18) 4, acetyl-CoA sialate 4-0-acetyltransferase (EC 2.3.1.44) 5, acetyl-CoA sialate 7(9)-0-acetyltransferase (EC 2.3.1.45) 6,. S-adenosyl-L-methionine sialate 8-O-methyltransferase (proposed EC 2.1.1.78) 7, sialate 4- or 9-0-acetylesterases (EC 3.1.1.53) 8, sialidase (EC 3.2.1.18) 9, sialate-pyruvate lyase (aldolase EC 4.1.3.3). Both Neu5Ac and Neu5Gc can be O-acetylated by the two O-acetyltransferases. There may also exist a sulfotransferase, since sulfated sialic acids have been found in e.g. echinoderms [13,577]. ( ), Sialic-acid-accepting nascent glycoconjugate. Fig. 13. Metabolism scheme of sialic acids. Anabolic (solid arrow) and catabolic (dashed arrow) reactions are indicated. For literature see the text. Enzymes 1, CMP-sialate synthase (EC 2.7.7.43) 2, sialyltransferases (EC 2.4.99.1.) 3, CMP-Neu5Ac hydroxylase (EC 1.14.99.18) 4, acetyl-CoA sialate 4-0-acetyltransferase (EC 2.3.1.44) 5, acetyl-CoA sialate 7(9)-0-acetyltransferase (EC 2.3.1.45) 6,. S-adenosyl-L-methionine sialate 8-O-methyltransferase (proposed EC 2.1.1.78) 7, sialate 4- or 9-0-acetylesterases (EC 3.1.1.53) 8, sialidase (EC 3.2.1.18) 9, sialate-pyruvate lyase (aldolase EC 4.1.3.3). Both Neu5Ac and Neu5Gc can be O-acetylated by the two O-acetyltransferases. There may also exist a sulfotransferase, since sulfated sialic acids have been found in e.g. echinoderms [13,577]. ( ), Sialic-acid-accepting nascent glycoconjugate.
The complete pattern of sialic acid side-chain G-acetylation may require several sialate O-acetyltransferases each with a specificity for only one position. On the other hand, the primary insertion place for the O-acetyl function may be the H07 group alone from where the ester group migrates even under physiological conditions to the 9 position, presumably via C8 [7,23], leaving H07 ready for a new transfer. Thus, for complete side-... [Pg.326]

Lrhorfi LA, Srinivasan GV, Schauer R (2007) Properties and partial purification of sialate 0-acetyltransferase from bovine submandibular glands. Biol Chem 388 297-306... [Pg.97]

Figure 3. Two models for the O-acetylation of Sia in Golgi-membranes of bovine submandibular glands. A, as CMP-glycoside, before the transfer onto nascent glycoconjugates (mucin) and B, after this transfer. OAT, sialate-7(9)-0-acetyltransferase ST, sialyltransferase M, O-acetylisomerase. For further details see the text. Figure 3. Two models for the O-acetylation of Sia in Golgi-membranes of bovine submandibular glands. A, as CMP-glycoside, before the transfer onto nascent glycoconjugates (mucin) and B, after this transfer. OAT, sialate-7(9)-0-acetyltransferase ST, sialyltransferase M, O-acetylisomerase. For further details see the text.
Acetylation has been found in horse, donkey, guinea pig, and Echidna (Corfield and Schauer, 1982a) and requires a different 0-acetyltransferase, acetyl-CoA sialate 4-0-acetyltransferase (EC 2.3.1.44), which has been described for equine submandibular gland as a membrane-associated enzyme (Schauer, 1978b, 1987b). [Pg.22]

See other pages where Sialate 9-0-acetyltransferase is mentioned: [Pg.326]    [Pg.326]    [Pg.328]    [Pg.364]    [Pg.65]    [Pg.1345]    [Pg.1352]    [Pg.22]   
See also in sourсe #XX -- [ Pg.11 , Pg.230 ]



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