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CMP-Neu5Ac hydroxylase

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.
Fig. 14. Redox-protein compounds involved in the formation of Neu5Gc by CMP-Neu5Ac hydroxylase [ 188, 680,681]. Fig. 14. Redox-protein compounds involved in the formation of Neu5Gc by CMP-Neu5Ac hydroxylase [ 188, 680,681].
Schlenzka, W., Shaw, L., and Schauer, R., 1993b, Purification of CMP-Neu5Ac hydroxylase from pig submandibular gland and inhibition of the enzyme by rabbit anti-(hydroxylase) antiserum,... [Pg.63]

The hydroxylase in supernatants of various tissues exhibits an apparent for CMP-Neu5Ac ranging from 18 (xM for the enzyme from A. rubens (Schlenzka et al., 1993a) through to 2.5 (xM for the hydroxylase in pig submandibular glands (Muchmore et al., 1989), 1.3 xM for the mouse liver enzyme (Shaw and Schauer, 1989), and 0.6 (xM for the hydroxylase from rat small intestine (Bouhours and Bouhours, 1989). Although the complex substrate and cofactor... [Pg.26]

See other pages where CMP-Neu5Ac hydroxylase is mentioned: [Pg.329]    [Pg.322]    [Pg.324]    [Pg.326]    [Pg.1348]    [Pg.1349]    [Pg.1350]    [Pg.26]    [Pg.26]    [Pg.27]    [Pg.27]    [Pg.28]    [Pg.28]    [Pg.29]    [Pg.31]    [Pg.329]    [Pg.322]    [Pg.324]    [Pg.326]    [Pg.1348]    [Pg.1349]    [Pg.1350]    [Pg.26]    [Pg.26]    [Pg.27]    [Pg.27]    [Pg.28]    [Pg.28]    [Pg.29]    [Pg.31]    [Pg.182]    [Pg.322]    [Pg.323]    [Pg.261]    [Pg.1351]    [Pg.27]    [Pg.202]    [Pg.227]   
See also in sourсe #XX -- [ Pg.78 ]

See also in sourсe #XX -- [ Pg.230 ]



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