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

词条

Lactosylceramide alpha-2,6-N-sialyltransferase

释义

References

{{enzyme
| Name = lactosylceramide alpha-2,6-N-sialyltransferase
| EC_number = 2.4.99.11
| CAS_number = 55071-95-9
| IUBMB_EC_number = 2/4/99/11
| GO_code = 0047287
| image =
| width =
| caption =
}}

In enzymology, a lactosylceramide alpha-2,6-N-sialyltransferase ({{EC number|2.4.99.11}}) is an enzyme that catalyzes the chemical reaction

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

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

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:lactosylceramide alpha-2,6-N-acetylneuraminyltransferase. Other names in common use include cytidine monophosphoacetylneuraminate-lactosylceramide, sialyltransferase, CMP-acetylneuraminate-lactosylceramide-sialyltransferase, CMP-N-acetylneuraminic acid:lactosylceramide sialyltransferase, CMP-sialic acid:lactosylceramide sialyltransferase, cytidine monophosphoacetylneuraminate-lactosylceramide, and sialyltransferase.

References

{{cite journal | vauthors = Albarracin I, Lassaga FE, Caputto R | date = 1988 | title = Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide alpha 2,6-N-acetylneuraminyltransferase (EC 2.4.99.-) | journal = Biochem. J. | volume = 254 | pages = 559–65 | pmid = 2460092 | issue = 2 | pmc = 1135114 }}
{{cite journal | vauthors = Landa CA, Maccioni HJ, Arce A, Caputto R | date = 1977 | title = The biosynthesis of brain gangliosides. Separation of membranes with different ratios of ganglioside sialylating activity to gangliosides | journal = Biochem. J. | volume = 168 | pages = 325–32 | pmid = 606237 | issue = 3 | pmc = 1183776 }}

2 : EC 2.4.99|Enzymes of unknown structure

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