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Information on EC 2.4.99.3 - alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9NSC7

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IUBMB Comments
alpha-N-Acetylgalactosamine linked to threonine or serine is also an acceptor, when substituted at the 3-position.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: Q9NSC7
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-2,6-ST, alpha-N-acetylgalactosaminylprotein alpha2-->6 sialyltransferase, alpha2,6-sialyltransferase, alpha2,6-sialyltransferase II, CMP-N-acetylneuraminate:alpha-N-acetylgalactosaminide alpha2-->6 sialyltransferase, CMP-Neu5Ac: RGalNAcalpha1-O-Ser/Thralpha2,6-sialyltransferase, CMP-Neu5Ac:GalNAc alpha2,6-sialyltransferase, CMP-NeuAc:galactoside (alpha2-6)-sialyltransferase, CMP-sialic acid:alpha-N-acetylgalactosaminide(R-->Galbeta1-->3GalNAcalpha1-->O-Ser/Thr) alpha2-->6 sialyltransferase, CMPNeu5Ac:GalNAalpha2,6-sialyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-2,6-ST
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alpha-N-acetylgalactosaminylprotein alpha2-->6 sialyltransferase
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alpha2,6-sialyltransferase
247
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alpha2,6-sialyltransferase II
305572
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CMP-N-acetylneuraminate:alpha-N-acetylgalactosaminide alpha2-->6 sialyltransferase
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CMP-Neu5Ac: RGalNAcalpha1-O-Ser/Thralpha2,6-sialyltransferase
247
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CMP-Neu5Ac:GalNAc alpha2,6-sialyltransferase
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CMP-NeuAc:galactoside (alpha2-6)-sialyltransferase
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CMP-sialic acid:alpha-N-acetylgalactosaminide(R-->Galbeta1-->3GalNAcalpha1-->O-Ser/Thr) alpha2-->6 sialyltransferase
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CMPNeu5Ac:GalNAalpha2,6-sialyltransferase
247
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mucin sialyltransferase
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sialyltransferase
247
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sialyltransferase 7A
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sialyltransferase, cytidine monophosphoacetylneuraminate-alpha-acetylgalactosaminide alpha2-->6-
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ST6
247
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ST6Gal-I
247
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ST6GalNAc I
247
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ST6GalNAc-I
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ST6GalNAc-II
ST6GalNAcI
247
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STM
267066
i.e. human ST6GalNAc-II
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycosyl group transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
CMP-N-acetylneuraminate:glycano-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein alpha-2,6-N-acetylneuraminyltransferase
alpha-N-Acetylgalactosamine linked to threonine or serine is also an acceptor, when substituted at the 3-position.
CAS REGISTRY NUMBER
COMMENTARY hide
71124-50-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CMP-N-acetylneuraminate + glycano-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein
CMP + glycano-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
show the reaction diagram
hST6GalNAc-I catalyzes the key step in the biosynthesis of Sialyl-Tn antigen, Neu5Acalpha(2-6)GalNAcalpha1-O-Ser/Thr
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CMP-N-acetylneuraminate + GTTPSPVPT[GalNAc]TSTTSAP
CMP + GTTPSPVPT[Neu5Acalpha(2-6)GalNAc]TSTTSAP
show the reaction diagram
hexadecaglycopeptide acceptor, corresponding to the MUC5AC tandem repeat sequence substituted by a GalNAc residue on Thr-9, hST6GalNAc-I
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?
CMP-N-acetylneuraminate + R-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein
CMP + R-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
show the reaction diagram
hST6GalNAc-I transfers a sialic acid residue in alpha2,6-linkage to GalNAc-O-Ser/Thr, substrate specificity of hST6GalNAc-I and -II
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?
CMP-N-acetylneuraminate + asialo-fetuin
CMP + fetuin
show the reaction diagram
CMP-N-acetylneuraminate + asialo-orosomucoid
CMP + orosomucoid
show the reaction diagram
-
-
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?
CMP-N-acetylneuraminate + Galbeta(1-3)GalNAc-R
CMP + Galbeta(1-3)(NeuAcalpha(2-6))GalNAc-R
show the reaction diagram
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R: protein, formation of TF Sia6Core-1, Galbeta(1-3)(NeuAcalpha(2,6))GalNAc-R, or of TF DiSiaCore-1, NeuAcalpha(2-3)Galbeta(1-3)(NeuAcalpha(2,6))GalNAc-R, by the sialyltransferase ST6GalNAc-II
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?
CMP-N-acetylneuraminate + GalNAc-R
CMP + NeuAcalpha(2-6)GalNAc-R
show the reaction diagram
CMP-N-acetylneuraminate + glycano-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein
CMP + glycano-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
show the reaction diagram
CMP-N-acetylneuraminate + native fetuin
?
show the reaction diagram
STM, i.e. hST6GalNAc-II, 83% as effective as asialo-fetuin
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-
?
CMP-N-acetylneuraminate + NeuAcalpha(2-3)Galbeta(1-3)GalNAc-R
CMP + NeuAcalpha(2-3)Galbeta(1-3)(NeuAcalpha(2-6))GalNAc-R
show the reaction diagram
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R: protein, formation of TF Sia6Core-1, Galbeta(1-3)(NeuAcalpha(2,6))GalNAc-R, or of TF DiSiaCore-1, NeuAcalpha(2-3)Galbeta(1-3)(NeuAcalpha(2,6))GalNAc-R, by the sialyltransferase ST6GalNAc-II
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?
CMP-N-acetylneuraminate + p-nitrophenyl-beta-D-galactoside
CMP + alpha-sialosyl-(2-6)-p-nitrophenyl-beta-D-galactoside
show the reaction diagram
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?
CMP-N-acetylneuraminate + protein MUC1-MFP6
?
show the reaction diagram
CMP-N-acetylneuraminate + R-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein
CMP + R-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
show the reaction diagram
CMP-N-acetylneuraminate + VPSTPPTPSPSTPPTPSPSCCHPR-GalNAc
CMP + ?
show the reaction diagram
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?
CMP-Neu5Ac + asialofetuin
CMP + ?
show the reaction diagram
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?
CMP-Neu5Ac + fetuin
CMP + ?
show the reaction diagram
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isoform ST6GalNAc-I, 84% of reactivity with asialofetuin, isoform ST6GalNAc-II, 88% of reactivity with asialofetuin
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?
CMP-Neu5Ac + HIV 120gp (17-mer)
CMP + ?
show the reaction diagram
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isoform ST6GalNAc-I, 34% of reactivity with asialofetuin, isoform ST6GalNAc-II, 38% of reactivity with asialofetuin
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?
CMP-Neu5Ac + HIV 120gp (21-mer)
CMP + ?
show the reaction diagram
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isoform ST6GalNAc-I, 62% of reactivity with asialofetuin, isoform ST6GalNAc-II, 58% of reactivity with asialofetuin
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?
CMP-sialic acid-PEG4-biotin + desialyated bovine serum albumin
?
show the reaction diagram
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bacterially produced ST6 is active and capable of catalyzing the transfer of sialic acid onto a desialylated O-glycoprotein, bovine submaxillary mucin
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CMP-N-acetylneuraminate + glycano-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein
CMP + glycano-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
show the reaction diagram
Q9NSC7
hST6GalNAc-I catalyzes the key step in the biosynthesis of Sialyl-Tn antigen, Neu5Acalpha(2-6)GalNAcalpha1-O-Ser/Thr
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CMP-N-acetylneuraminate + glycano-1,3-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein
CMP + glycano-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein
show the reaction diagram
CMP-N-acetylneuraminate + protein MUC1-MFP6
?
show the reaction diagram
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recombinant protein substrate expressed in MDA-MB-231 breast cancer cells, glycoprofiling, overview
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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activity decreases with increasing divalent cation concentration
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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dithioerythritol
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8.5
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about half-maximal activity at pH 6.2 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
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about half-maximal activity at 20C and 40C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
hST6GalNAc-I
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
colon cancer cells, hST6GalNAc-I
Manually annotated by BRENDA team
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malignant hematopoietic cell. Sialylated histo-blood group carbohydrate CD175 is present in all hematopoietic cell lines and native lymphocytes examined. CD175 and sialylated CD175 are preferentially expressed on erythroblastic leukemia cell lines. Presence of sialylated CD175 is consistent with the expression of the gene encoding alpha2,6-sialyltransferase ST6GalNAc-1
Manually annotated by BRENDA team
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hematopoietic cell line, high ST6GalNAc-I expression
Manually annotated by BRENDA team
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human colon cancer cell line, recombinant ST6GalNAc-II
Manually annotated by BRENDA team
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sialylated histo-blood group carbohydrate CD175 is present in all hematopoietic cell lines and native lymphocytes examined. CD175 and sialylated CD175 are preferentially expressed on erythroblastic leukemia cell lines. Presence of sialylated CD175 is consistent with the expression of the gene encoding alpha2,6-sialyltransferase ST6GalNAc-1
Manually annotated by BRENDA team
normal human mammary epithelial cell strains 70N, 76N and 81N, STM RNA expression is highest in 76N, followed by 81N and 70N
Manually annotated by BRENDA team
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human colon carcinoma cells, recombinant ST6GalNAc-II
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
SIA7A_HUMAN
600
1
68564
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
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x * 65000, isoform ST6GalNAc-I, x * 39000, isoform ST6GalNAc-II, SDS-PAGE
42000
x * 42000, predicted from the amino acid sequence
54000
x * 54000, SDS-PAGE
65000
104000
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maltose-binding protein-ST6, Western blotting
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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t1/2: about 60 min
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
recombinant ST6GalNAc-II, immobilized metal-affinity chromatography
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cDNA encoding the full-length hST6GalNAc-I from HT-29-MTX cells is cloned, stable transfection of MDA-MB-231 breast cancer cells expressing enzyme induces the expression of sialyl-Tn antigen at the cell surface associated with morphological changes, decreased growth and increased migration of the cells
a codon-optimized gene encoding the catalytic domain of ST6 (amino acids Lys36-end) cloned into pTrc99a downstream from the tac promoter, FLAG tag and an octahistidine tag fused at the N- and C-termini, respectively. Catalytic domain of ST6 cloned into the high-copy number plasmid pCWin2MBP, which expresses an N-terminal fusion of ST6 with the Escherichia coli maltose-binding protein under the control of a dual tac promoter. Expression of soluble ST6 in a variety of Escherichia coli strains with oxidizing cytoplasm. Fusion of the ST6 enzyme to maltose-binding protein expressed in Origami 2 cells
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expressed in HEK-293 cells
expressed in Sf9 insect cells or HEK-293T cells
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overexpression in baculovirus system
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SIATL1 gene encoding STM is mapped to the long arm of chromosome 17 at q23-qter, full-length cDNA from normal human mammary epithelial cell strain 76N is cloned, sequenced and encodes a protein of 374 amino acids, expression in COS-7 cells
ST6GalNAc-II cDNA is cloned, LS147T and SW-480 human colorectal carcinoma cells are transfected with human ST6GalNAc-II cDNA leading to an increased cell surface expression of Thomsen-Friedenreich-related blood group antigen TF, which depends in SW-480 cells on the ratio of core 2 beta-1,6-N-acetylglucosaminyltransferase and ST6GalNAc-II
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stable transfection of the breast cancer cell line MDA-MB-231 with ST6GalNAc I cDNA induces sialyl-Tn antigen expression, modifications of the O-glycosylation pattern of a MUC1-related recombinant protein secreted by MDA-MB-231 sialyl-Tn positive cells occurs, sialyl-Tn expression and concomitant changes in the overall O-glycan profiles induce a decrease of adhesion and an increase of migration of MDA-MB-231, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
while wild-type Escherichia coli strain DHB4 produces very small amounts of soluble ST6, engineered strains of Escherichia coli (strains SMG96, FA113, MJF277.2, and DR611), which possess certain types of oxidative cytoplasm or which co-express specific molecular chaperones (DnaK/DnaJ, GroEL/GroES, and Skp), can result in significant yields of ST6. DR611 cells are able to produce dramatically increased amounts of soluble ST6. Fusion of the ST6 enzyme to maltose-binding protein results in a marked increase in the amount of soluble ST6 in Origami 2 cells, as well as in the DR611 strain
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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Escherichia coli system may be used as a starting point for the evolution of sialyltransferases with better expression characteristics or altered donor/acceptor specificities
medicine
synthesis
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use of glycan microarrays for high-throughput acceptor specificity screening of recombinant sialyltransferases. Donor substrate is cytidine 5'-monophospho-N-acteylneuraminate, which has been biotinylated at position 9. human alpha2,6sialyltransferase-I also sialylates chitobiose structures including N-glycans
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bauvois, B.; Cacan, R.; Fournet, B.; Caen, J.; Montreuil, J.; Verbert, A.
Discrimination between activity of (alpha 2-3)-sialyltransferase and (alpha 2-6)-sialyltransferase in human platelets using p-nitrophenyl-beta-D-galactoside as acceptor
Eur. J. Biochem.
121
567-572
1982
Homo sapiens
Manually annotated by BRENDA team
Schneider, F.; Kemmner, W.; Haensch, W.; Franke, G.; Gretschel, S.; Karsten, U.; Schlag, P.M.
Overexpression of sialyltransferase CMP-sialic acid:Galbeta1,3GalNAc-R alpha6-sialyltransferase is related to poor patient survival in human colorectal carcinomas
Cancer Res.
61
4605-4611
2001
Homo sapiens
Manually annotated by BRENDA team
Sotiropoulou, G.; Kono, M.; Anisowicz, A.; Stenman, G.; Tsuji, S.; Sager, R.
Identification and functional characterization of a human GalNAc alpha2,6-sialyltransferase with altered expression in breast cancer
Mol. Med.
8
42-55
2002
Homo sapiens, Homo sapiens (Q9UJ37)
Manually annotated by BRENDA team
Julien, S.; Krzewinski-Recchi, M.A.; Harduin-Lepers, A.; Gouyer, V.; Huet, G.; Le Bourhis, X.; Delannoy, P.
Expression of sialyl-Tn antigen in breast cancer cells transfected with the human CMP-Neu5Ac:GalNAc alpha2,6-sialyltransferase (ST6GalNac I) cDNA
Glycoconjugate J.
18
883-893
2001
Homo sapiens (Q9NSC7)
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Manually annotated by BRENDA team
Marcos, N.T.; Cruz, A.; Silva, F.; Almeida, R.; David, L.; Mandel, U.; Clausen, H.; von Mensdorff-Pouilly, S.; Reis, C.A.
Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I expression in gastric carcinoma cell lines
J. Histochem. Cytochem.
51
761-771
2003
Homo sapiens
Manually annotated by BRENDA team
Marcos, N.T.; Pinho, S.; Grandela, C.; Cruz, A.; Samyn-Petit, B.; Harduin-Lepers, A.; Almeida, R.; Silva, F.; Morais, V.; Costa, J.; Kihlberg, J.; Clausen, H.; Reis, C.A.
Role of the human ST6GalNAc-I and ST6GalNAc-II in the synthesis of the cancer-associated sialyl-Tn antigen
Cancer Res.
64
7050-7057
2004
Homo sapiens
Manually annotated by BRENDA team
Julien, S.; Adriaenssens, E.; Ottenberg, K.; Furlan, A.; Courtand, G.; Vercoutter-Edouart, A.S.; Hanisch, F.G.; Delannoy, P.; Le Bourhis, X.
ST6GalNAc I expression in MDA-MB-231 breast cancer cells greatly modifies their O-glycosylation pattern and enhances their tumourigenicity
Glycobiology
16
54-64
2006
Homo sapiens
Manually annotated by BRENDA team
Blixt, O.; Allin, K.; Bohorov, O.; Liu, X.; Andersson-Sand, H.; Hoffmann, J.; Razi, N.
Glycan microarrays for screening sialyltransferase specificities
Glycoconj. J.
25
59-68
2008
Homo sapiens
Manually annotated by BRENDA team
Cao, Y.; Merling, A.; Karsten, U.; Goletz, S.; Punzel, M.; Kraft, R.; Butschak, G.; Schwartz-Albiez, R.
Expression of CD175 (Tn), CD175s (sialosyl-Tn) and CD176 (Thomsen-Friedenreich antigen) on malignant human hematopoietic cells
Int. J. Cancer
123
89-99
2008
Homo sapiens
Manually annotated by BRENDA team
Suzuki, H.; Moldoveanu, Z.; Hall, S.; Brown, R.; Vu, H.L.; Novak, L.; Julian, B.A.; Tomana, M.; Wyatt, R.J.; Edberg, J.C.; Alarcon, G.S.; Kimberly, R.P.; Tomino, Y.; Mestecky, J.; Novak, J.
IgA1-secreting cell lines from patients with IgA nephropathy produce aberrantly glycosylated IgA1
J. Clin. Invest.
118
629-639
2008
Homo sapiens
Manually annotated by BRENDA team
Skretas, G.; Carroll, S.; DeFrees, S.; Schwartz, M.F.; Johnson, K.F.; Georgiou, G.
Expression of active human sialyltransferase ST6GalNAcI in Escherichia coli
Microb. Cell Fact.
8
50
2009
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Stuchlova Horynova, M.; Vrablikova, A.; Stewart, T.J.; Takahashi, K.; Czernekova, L.; Yamada, K.; Suzuki, H.; Julian, B.A.; Renfrow, M.B.; Novak, J.; Raska, M.
N-acetylgalactosaminide alpha2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy
Nephrol. Dial. Transplant.
30
234-238
2015
Homo sapiens (A0A024R8M1), Homo sapiens
Manually annotated by BRENDA team
Takahashi, K.; Raska, M.; Horynova, M.; Hall, S.; Poulsen, K.; Kilian, M.; Hiki, Y.; Yuzawa, Y.; Moldoveanu, Z.; Julian, B.; Renfrow, M.; Novak, J.
Enzymatic sialylation of IgA1 O-glycans: Implications for studies of IgA nephropathy
PLoS ONE
9
e99026
2014
Homo sapiens
Manually annotated by BRENDA team
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