ST3GAL3,4,6 transfer Neu5Ac to Type 2 chain to form Type 2 MSGG

Stable Identifier
Reaction [transition]
Homo sapiens
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The alpha-2,3-sialyltransferases ST3GAL3,4 and 6 (Kitagawa & Paulson 1993, Okajima et al. 1999, Kitagawa & Paulson 1994) located on the Golgi membrane, mediate the transfer of sialic acid (Neu5Ac, N-acetylneuraminic acid) in an α2,3 linkage to the terminal galactose of Gal-beta-1,4-GlcNAc- sequences found on glycoproteins and glycolipids to form Type 2 monosialylgalactosylgloboside (Type 2 MSGG).

Increased sialylation has been associated with malignant transformation and metastasis. ST3GAL6 is highly expressed in patients with multiple myeloma (MM). Knockdown of ST3GAL6 has been shown to prolong survival in mice (Glavey et al. 2014).

Literature References
PubMed ID Title Journal Year
8333853 Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase

Kitagawa, H, Paulson, JC

Biochem Biophys Res Commun 1993
10206952 Molecular cloning of a novel alpha2,3-sialyltransferase (ST3Gal VI) that sialylates type II lactosamine structures on glycoproteins and glycolipids

Kiso, M, Fukumoto, S, Miyazaki, H, Urano, T, Furukawa, K, Furukawa, K, Ishida, H, Okajima, T

J Biol Chem 1999
8288606 Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups

Kitagawa, H, Paulson, JC

J Biol Chem 1994
Catalyst Activity

beta-galactoside (CMP) alpha-2,3-sialyltransferase activity of ST3GAL3,4,6 [Golgi membrane]

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