ST3GAL4 transfers Neu5Ac to terminal Gal of N-glycans

Stable Identifier
R-HSA-1022129
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
Addition of alpha-2,3-sialic acid to N-glycan over a galactose by ST3GAL4
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Addition of sialic acid (Neu5Ac) to galactose-containing N-glycan. Neu5Ac is usually found at terminal positions of the N-glycan. This imparts a negative charge at neutral pH which affects the chemico-physical and biological properties of the N-glycans (for a review, see Schauer 2000); moreover, this modification can lead to the addition of extraordinarily long antennae such as polysialic acid (hundreds of sials) or polylactosamine repeats (dozens of disaccharide repeats) (Harduin-Lepers 2001), while the number of modifications on the antennae of N-glycans is usually lower.
There are over 20 sialyltransferases known in humans, 5 of which are known to act on N-glycans. Beta-galactoside alpha-2,6-sialyltransferase 1 (ST6GAL1) is the only sialyltransferase known to transfer Neu5Ac to galactose (Gal) on N-Glycans (Dall'Olio 2000). A second beta-Galactoside alpha-2,6-sialyltransferase has been characterized, but this enzyme acts mainly on oligosaccharides (Krzewinski-Recchi et al. 2003). Neu5Ac can also be added via an alpha-2,3-linkage to Gal on N-glycans by CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4 (ST3GAL4) (Ellies et al. 2002). ST8Sia II (ST8SIA2), ST8Sia III (ST8SIA3), and ST8Sia IV (ST8SIA6) have alpha-2,8-activity (Angata et al. 1997, Angata et al. 2000; Angata & Fuduka 2003).

Literature References
PubMed ID Title Journal Year
11530204 The human sialyltransferase family

Harduin-Lepers, A, Vallejo-Ruiz, V, Krzewinski-Recchi, MA, Samyn-Petit, B, Julien, S, Delannoy, P

Biochimie 2001
11425186 The sialyl-alpha2,6-lactosaminyl-structure: biosynthesis and functional role

Dall'Olio, F

Glycoconj J 2000
10766765 Differential biosynthesis of polysialic acid on neural cell adhesion molecule (NCAM) and oligosaccharide acceptors by three distinct alpha 2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III

Angata, K, Suzuki, M, McAuliffe, J, Ding, Y, Hindsgaul, O, Fukuda, M

J Biol Chem 2000
11421344 Achievements and challenges of sialic acid research

Schauer, R

Glycoconj J 2000
12603328 Identification and functional expression of a second human beta-galactoside alpha2,6-sialyltransferase, ST6Gal II

Krzewinski-Recchi, MA, Julien, S, Juliant, S, Teintenier-Lelièvre, M, Samyn-Petit, B, Montiel, MD, Mir, AM, Cerutti, M, Harduin-Lepers, A, Delannoy, P

Eur J Biochem 2003
12097641 Sialyltransferase ST3Gal-IV operates as a dominant modifier of hemostasis by concealing asialoglycoprotein receptor ligands

Ellies, LG, Ditto, D, Levy, GG, Wahrenbrock, M, Ginsburg, D, Varki, A, Le, DT, Marth, JD

Proc Natl Acad Sci U S A 2002
12765789 Polysialyltransferases: major players in polysialic acid synthesis on the neural cell adhesion molecule

Angata, K, Fukuda, M

Biochimie 2003
9054414 Human STX polysialyltransferase forms the embryonic form of the neural cell adhesion molecule. Tissue-specific expression, neurite outgrowth, and chromosomal localization in comparison with another polysialyltransferase, PST

Angata, K, Nakayama, J, Fredette, B, Chong, K, Ranscht, B, Fukuda, M

J Biol Chem 1997
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
beta-galactoside (CMP) alpha-2,3-sialyltransferase activity of ST3GAL4 [Golgi membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created