Search results for ST8SIA3

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Protein (1 results from a total of 1)

Identifier: R-HSA-1022124
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: ST8SIA3: O43173

Reaction (3 results from a total of 3)

Identifier: R-HSA-975902
Species: Homo sapiens
Compartment: Golgi membrane, Golgi lumen
Addition of sialic acid to galactose-containing N-glycan. Sialic acid 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 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 sialic acid to galactose 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 galactose 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).
Identifier: R-HSA-1022133
Species: Homo sapiens
Compartment: Golgi membrane, Golgi lumen
Addition of sialic acid (Neu5Ac) to galactose-containing N-glycan. Sialic acid 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 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).
Identifier: R-HSA-1022129
Species: Homo sapiens
Compartment: Golgi membrane, Golgi lumen
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).
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