Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.99 Transferring other glycosyl groups
ID:2.4.99.1
Description:Beta-galactoside alpha-(2,6)-sialyltransferase.
Alternative Name: Lactosylceramide-alpha-2,6-N-sialyltransferase.
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase.
Beta-galactoside alpha-2,6-sialyltransferase.
Beta-galactosamide alpha-2,6-sialyltransferase.
Cath: 3.90.1480.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.99.1
BRENDA Enzyme Link: BRENDA 2.4.99.1
KEGG Enzyme Link: KEGG2.4.99.1
BioCyc Enzyme Link: BioCyc 2.4.99.1
ExPASy Enzyme Link: ExPASy2.4.99.1
EC2PDB Enzyme Link: EC2PDB 2.4.99.1
ExplorEnz Enzyme Link: ExplorEnz 2.4.99.1
PRIAM enzyme-specific profiles Link: PRIAM 2.4.99.1
IntEnz Enzyme Link: IntEnz 2.4.99.1
MEDLINE Enzyme Link: MEDLINE 2.4.99.1
MSA:

2.4.99.1;

Phylogenetic Tree:

2.4.99.1;

Uniprot:
M-CSA:
RHEA:52104 a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP + H(+)
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[*:7]-[OH;+0:8]>>[*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:8]-[*:7].[*:6]-[OH;+0:5]
Reaction
Core-to-Core More
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose.Paulson JC, Beranek WE, Hill RL1977 Apr 10849932
Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase.Spiro MJ, Spiro RG1968 Dec 255726897
The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum.Bartholomew BA, Jourdian GW, Roseman S1973 Aug 254723915
Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin.Hickman J, Ashwell G, Morell AG, van den Hamer CJ, Scheinberg IH1970 Feb 254313609
Enzymatic properties of beta-D-galactoside alpha2 leads to 6 sialytransferase from bovine colostrum.Paulson JC, Rearick JI, Hill RL1977 Apr 10849933
The sialyltransferase "sialylmotif" participates in binding the donor substrate CMP-NeuAc.Datta AK, Paulson JC1995 Jan 277829476
Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type.Schachter H, Narasimhan S, Gleeson P, Vella G19836366476
Primary structure of beta-galactoside alpha 2,6-sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor.Weinstein J, Lee EU, McEntee K, Lai PH, Paulson JC1987 Dec 253121604
The structure of human α-2,6-sialyltransferase reveals the binding mode of complex glycans.Kuhn B, Benz J, Greif M, Engel AM, Sobek H, Rudolph MG2013 Sep23999306
Universal phosphatase-coupled glycosyltransferase assay.Wu ZL, Ethen CM, Prather B, Machacek M, Jiang W2011 Jun21081508
Probing the substrate specificity of four different sialyltransferases using synthetic beta-D-Galp-(1-->4)-beta-D-GlcpNAc-(1-->2)-alpha-D-Manp-(1-->O) (CH(2))7CH3 analogues general activating effect of replacing N-acetylglucosamine by N-propionylglucosamine.Rohfritsch PF, Joosten JA, Krzewinski-Recchi MA, Harduin-Lepers A, Laporte B, Juliant S, Cerutti M, Delannoy P, Vliegenthart JF, Kamerling JP2006 Apr16439063
Comparison of the enzymatic properties of mouse beta-galactoside alpha2,6-sialyltransferases, ST6Gal I and II.Takashima S, Tsuji S, Tsujimoto M2003 Aug12966079
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 P2003 Mar12603328
Characterization of the second type of human beta-galactoside alpha 2,6-sialyltransferase (ST6Gal II), which sialylates Galbeta 1,4GlcNAc structures on oligosaccharides preferentially. Genomic analysis of human sialyltransferase genes.Takashima S, Tsuji S, Tsujimoto M2002 Nov 2912235148
Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide alpha 2,6-N-acetylneuraminyltransferase (EC 2.4.99.-).Albarracin I, Lassaga FE, Caputto R1988 Sep 12460092

RHEA:21552 beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide(d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = CMP + H(+) + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[*:7]-[OH;+0:8]>>[*:7]-[O;H0;+0:8]-[C;H0;+0:2](-[*:1])(-[*:3])-[*:4].[*:6]-[OH;+0:5]
Reaction
Core-to-Core More
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide alpha 2,6-N-acetylneuraminyltransferase (EC 2.4.99.-).Albarracin I, Lassaga FE, Caputto R1988 Sep 12460092

RHEA:11836 CMP-N-acetyl-beta-neuraminate + N-acetyllactosamine = CMP + H(+) + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[*:7]-[OH;+0:8]>>[*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:8]-[*:7].[*:6]-[OH;+0:5]
Reaction
Core-to-Core More
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Enzymatic properties of beta-D-galactoside alpha2 leads to 6 sialytransferase from bovine colostrum.Paulson JC, Rearick JI, Hill RL1977 Apr 10849933
The sialyltransferase "sialylmotif" participates in binding the donor substrate CMP-NeuAc.Datta AK, Paulson JC1995 Jan 277829476
Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type.Schachter H, Narasimhan S, Gleeson P, Vella G19836366476
Primary structure of beta-galactoside alpha 2,6-sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor.Weinstein J, Lee EU, McEntee K, Lai PH, Paulson JC1987 Dec 253121604
The structure of human α-2,6-sialyltransferase reveals the binding mode of complex glycans.Kuhn B, Benz J, Greif M, Engel AM, Sobek H, Rudolph MG2013 Sep23999306
Universal phosphatase-coupled glycosyltransferase assay.Wu ZL, Ethen CM, Prather B, Machacek M, Jiang W2011 Jun21081508
Probing the substrate specificity of four different sialyltransferases using synthetic beta-D-Galp-(1--&amp;gt;4)-beta-D-GlcpNAc-(1--&amp;gt;2)-alpha-D-Manp-(1--&amp;gt;O) (CH(2))7CH3 analogues general activating effect of replacing N-acetylglucosamine by N-propionylglucosamine.Rohfritsch PF, Joosten JA, Krzewinski-Recchi MA, Harduin-Lepers A, Laporte B, Juliant S, Cerutti M, Delannoy P, Vliegenthart JF, Kamerling JP2006 Apr16439063
Comparison of the enzymatic properties of mouse beta-galactoside alpha2,6-sialyltransferases, ST6Gal I and II.Takashima S, Tsuji S, Tsujimoto M2003 Aug12966079
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 P2003 Mar12603328
Characterization of the second type of human beta-galactoside alpha 2,6-sialyltransferase (ST6Gal II), which sialylates Galbeta 1,4GlcNAc structures on oligosaccharides preferentially. Genomic analysis of human sialyltransferase genes.Takashima S, Tsuji S, Tsujimoto M2002 Nov 2912235148