“Beta-galactoside alpha-2,6-sialyltransferase”的意思、由来-开放百科全书

词条

Beta-galactoside alpha-2,6-sialyltransferase

释义

References

{{enzyme
| Name = beta-galactoside alpha-2,6-sialyltransferase
| EC_number = 2.4.99.1
| CAS_number = 9075-81-4
| IUBMB_EC_number = 2/4/99/1
| GO_code = 0003835
| image =
| width =
| caption =
}}

In enzymology, a beta-galactoside alpha-2,6-sialyltransferase ({{EC number|2.4.99.1}}) is an enzyme that catalyzes the chemical reaction

CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D- glucosamine

Thus, the two substrates of this enzyme are CMP-N-acetylneuraminate and beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine, whereas its 3 products are CMP, alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-, and glucosamine.

This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:beta-D-galactosyl-1,4-N-acetyl-beta-D-glucos amine alpha-2,6-N-acetylneuraminyltransferase. This enzyme participates in n-glycan biosynthesis and glycan structures - biosynthesis 1.

References

{{cite journal | vauthors = Bartholomew BA, Jourdian GW, Roseman S | date = 1973 | title = The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum | journal = J. Biol. Chem. | volume = 248 | pages = 5751–62 | pmid = 4723915 | issue = 16 }}
{{cite journal | vauthors = Hickman J, Ashwell G, Morell AG, van den Hamer CJ, Scheinberg IH | date = 1970 | title = Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin | journal = J. Biol. Chem. | volume = 245 | pages = 759–66 | pmid = 4313609 | issue = 4 }}
{{cite journal | vauthors = Paulson JC, Beranek WE, Hill RL | date = 1977 | title = Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose | journal = J. Biol. Chem. | volume = 252 | pages = 2356–62 | pmid = 849932 | issue = 7 }}
{{cite journal | vauthors = Schachter H, Narasimhan S, Gleeson P, Vella G | date = 1983 | title = Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type | journal = Methods Enzymol. | volume = 98 | pages = 98–134 | pmid = 6366476 | doi = 10.1016/0076-6879(83)98143-0 }}
{{cite journal | vauthors = Spiro MJ, Spiro RG | date = 1968 | title = Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase | journal = J. Biol. Chem. | volume = 243 | pages = 6520–8 | pmid = 5726897 | issue = 24 }}

2 : EC 2.4.99|Enzymes of unknown structure

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