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Beta-galactoside alpha-2,3-sialyltransferase

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Enzyme
beta-galactoside alpha-2,3-sialyltransferase
Identifiers
EC no.2.4.99.4
CAS no.71124-51-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a beta-galactoside alpha-2,3-sialyltransferase (EC 2.4.99.4) is an enzyme that catalyzes the chemical reaction

CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R {\displaystyle \rightleftharpoons } CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D- galactosaminyl-R

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

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-galactoside alpha-2,3-N-acetylneuraminyl-transferase. This enzyme participates in 7 metabolic pathways: O-glycan biosynthesis, keratan sulfate biosynthesis, glycosphingolipid biosynthesis - lactoseries, glycosphingolipid biosynthesis - globoseries, glycosphingolipid biosynthesis - ganglioseries, glycan structures - biosynthesis 1, and glycan structures - biosynthesis 2.

Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 2EX0, 2EX1, 2IHJ, 2IHK, 2IHZ, 2II6, 2IIB, 2IIQ, and 2ILV.

References

Transferases: glycosyltransferases (EC 2.4)
2.4.1: Hexosyl-
transferases
Glucosyl-
Galactosyl-
Glucuronosyl-
Fucosyl-
Mannosyl-
2.4.2: Pentosyl-
transferases
Ribose
ADP-ribosyltransferase
Phosphoribosyltransferase
Other
Other
2.4.99: Sialyl
transferases
Enzymes
Activity
Regulation
Classification
Kinetics
Types
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