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Information on EC 2.4.3.7 - alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide 6-alpha-sialyltransferase
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EC Tree
2.4.3.7 alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide 6-alpha-sialyltransferaseIUBMB Comments
Attaches N-acetylneuraminic acid in alpha-2,6-linkage to N-acetylgalactosamine only when present in the structure of alpha-N-acetylneuraminyl-(2->3)-beta-galactosyl-(1->3)-N-acetylgalactosaminyl-R, where R may be protein or p-nitrophenol. Not identical with EC 2.4.3.3 alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
st6galnac, st6galnac iii, st6galnac vi, st6galnac iv, st6galnac v, st6galnac-iv, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl-galactosaminide 6-alpha-sialyltransferase
-
-
-
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alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase
-
-
-
-
CMP-N-acetylneuraminate:(alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3)-N-acetyl-D-galactosaminide alpha-2,6-N-acetylneuraminyl-transferase
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-
-
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cytidine monophosphoacetylneuraminate-(alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide-alpha-2,6-sialyltransferase
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-
-
-
EC 2.4.99.7
-
-
formerly
-
NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc-alpha-2,6-sialyltransferase
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-
-
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sialyltransferase
-
-
-
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sialyltransferase 3C
-
-
-
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sialyltransferase 7D
-
-
-
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sialyltransferase, cytidine monophosphoacetylneuraminate-(alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide-alpha-2,6-sialyltransferase
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-
-
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SIAT7
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-
-
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ST6GALNAC
-
-
-
-
ST6GalNAc III
ST6GalNAc IV
ST6GalNAc V
ST6GalNAc VI
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CMP-N-acetylneuraminate + N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosaminyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-[N-acetyl-alpha-neuraminyl-(2->6)]-N-acetyl-D-galactosaminyl-R
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
CMP-N-acetylneuraminate:N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)- N-acetyl-D-galactosaminide galactosamine-6-alpha-N-acetylneuraminyltransferase
Attaches N-acetylneuraminic acid in alpha-2,6-linkage to N-acetylgalactosamine only when present in the structure of alpha-N-acetylneuraminyl-(2->3)-beta-galactosyl-(1->3)-N-acetylgalactosaminyl-R, where R may be protein or p-nitrophenol. Not identical with EC 2.4.3.3 alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
129924-24-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CMP-N-acetyl-beta-neuraminate + Neu5Acalpha2-3Galbeta1-3GalNacalpha-O-benzyl
?
-
-
-
?
CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
CMP-N-acetylneuraminate + alpha1-acid glycoprotein
?
acceptor structur: Neu5Acalpha2-6Galbeta1-4GlcNac-R, 8.7% of activity with fetuin
-
-
?
CMP-N-acetylneuraminate + fetuin
?
acceptor structures: Neu5Acalpha2-3Galbeta1-3GalNacalpha1-O-Ser/Thr, Neu5Acalpha2-3Galbeta1-3[Neu5Acalpha2-6]GalNacalpha1-O-Ser/Thr and Neu5Acalpha2-6(3)Galbeta1-4GlcNac-R
-
-
?
CMP-N-acetylneuraminate + GlcNac-alpha1-O-benzyl
?
7.6% of activity with fetuin
-
-
?
CMP-N-acetylneuraminate + monosialylgalactosylgloboside
CMP + disialylgalactosylgloboside
isoforms ST6GalNAc III and ST6GalNAc VI generate disialylgalactosylgloboside from monosialylgalactosylgloboside with Vmax/Km values of 1.91 and 4.16 respectively
-
-
?
CMP-N-acetylneuraminate + N-alpha-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
CMP-N-acetylneuraminate + Neu5Acalpha2-3Galbeta1-3GalNac
?
60.3% of activity with fetuin
-
-
?
CMP-N-acetylneuraminate + Neu5Acalpha2-3Galbeta1-4GlcNac-alpha1-O-benzyl
?
224% of activity with fetuin
-
-
?
CMP-N-acetylneuraminate + sialyl lactoetraosylceramide
CMP + ?
-
-
product are disialyl Lewis a structures
-
?
CMP-Neu5Ac + fetuin
?
-
ST6GalNAc III also shows activity with O-glycans, but not N-glycans, in fetuin
-
-
?
CMP-Neu5Ac + GM1b
?
-
i.e. NeuAcalpha2,3Galbeta1,3GalNAcbeta1,4Galbeta1,4Glcbeta1-Cer, best substrate
-
-
?
CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
-
pathway in glycoprotein biosynthesis
-
-
?
CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
-
pathway in glycoprotein biosynthesis
-
-
?
CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
-
pathway in glycoprotein biosynthesis
-
-
?
CMP-N-acetylneuraminate + N-alpha-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
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no substrates are beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R or N-acetylgalactosylaminyl-R
-
?
CMP-N-acetylneuraminate + N-alpha-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
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attaches sialic acid in alpha-2,6-linkage to N-acetylgalactosamine only when present in the structure of alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminyl-R
-
?
CMP-N-acetylneuraminate + N-alpha-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
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R can be a protein or p-nitrophenol
-
?
CMP-N-acetylneuraminate + N-alpha-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
-
substrates are sialylated antifreeze glycoprotein as well as N-acetyl-D-galactosamine or beta-galactosyl-1,3-N-acetyl-D-galactosamine side chains from ovine submaxillary asialomucin or porcine submaxillary asialo/afucomucin respectively
-
?
CMP-N-acetylneuraminate + N-alpha-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
-
-
-
?
CMP-N-acetylneuraminate + N-alpha-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
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attaches sialic acid in alpha-2,6-linkage to N-acetylgalactosamine only when present in the structure of alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminyl-R
-
?
CMP-N-acetylneuraminate + N-alpha-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
-
-
-
?
CMP-NAC + monosialylgalactosylgloboside
CMP + disialylgalactosylgloboside
-
-
-
?
CMP-NAC + monosialylgalactosylgloboside
CMP + disialylgalactosylgloboside
the enzyme is responsible for the synthesis of disialylgalactosylgloboside from monosialylgalactosylgloboside in normal and malignant kidney cells, the reaction suppressed during the malignant transformation of the proximal tubules as a maturation arrest of glycosylation, overview
-
-
?
additional information
?
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enzyme is responsible for synthesis of disialyl Lewis a structures in colon tissues, but not for synthesis of alpha-series gangliosides, model of pathway for synthesis of disialyl lactoetraosylceramides and disialyl Lewis a structures
-
-
?
additional information
?
-
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substrate specificity, no activity with GA1, GA2, GM1, GM2, GD3, GT1b, GQ1b, and Lc4, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
CMP-NAC + monosialylgalactosylgloboside
CMP + disialylgalactosylgloboside
the enzyme is responsible for the synthesis of disialylgalactosylgloboside from monosialylgalactosylgloboside in normal and malignant kidney cells, the reaction suppressed during the malignant transformation of the proximal tubules as a maturation arrest of glycosylation, overview
-
-
?
additional information
?
-
-
enzyme is responsible for synthesis of disialyl Lewis a structures in colon tissues, but not for synthesis of alpha-series gangliosides, model of pathway for synthesis of disialyl lactoetraosylceramides and disialyl Lewis a structures
-
-
?
CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
-
pathway in glycoprotein biosynthesis
-
-
?
CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
-
pathway in glycoprotein biosynthesis
-
-
?
CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-(N-acetylneuraminyl-2,6)-N-acetyl-D-galactosaminyl-R
-
pathway in glycoprotein biosynthesis
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis-(2-nitrobenzoic acid)
-
0.01 mM, 50% inhibition, 0.1 mM, 97% inhibition
N-ethylmaleimide
-
0.014 mM, 50% non-competitive inhibition, almost complete protection with 0.05 mM CMP-N-acetylneuraminate
p-chloromercuribenzoic acid
-
0.036 mM, 50% inhibition, 0.1 mM, 97% inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.028
6,6'-dithiodinicotinic acid carboxypyridine disulfide
Rattus norvegicus
-
IC50: 0.028 mM
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
renal cancer cell line, expression of ST6GalNAc VI
brenda
additional information
in proximal tubule epithelial cells, expression of ST6GalNAc III
brenda
in proximal tubule epithelial cells, expression of ST6GalNAc VI
brenda
isoform ST6GalNAc-VI and disialylgalactosylgloboside are found in proximal tubule epithelial cells in normal kidney tissues
brenda
renal cancer cell line, expression of ST6GalNAc VI
brenda
renal cancer cell line, expression of ST6GalNAc VI
brenda
renal cancer cell line, expression of ST6GalNAc VI
brenda
renal cancer cell line, expression of ST6GalNAc VI
brenda
renal cancer cell line, expression of ST6GalNAc VI
brenda
renal cancer cell line, expression of ST6GalNAc VI
brenda
renal cancer cell line, expression of ST6GalNAc VI
brenda
renal cancer cell line, expression of ST6GalNAc VI
brenda
renal cancer cell line, expression of ST6GalNAc VI
brenda
renal cancer cell line, expression of ST6GalNAc VI
brenda
additional information
-
ST6GalNAc III tissue expression pattern, in situ hybridization, overview
brenda
additional information
ST6GalNAc III tissue expression pattern, in situ hybridization, overview
brenda
additional information
ST6GalNAc III tissue expression pattern, in situ hybridization, overview
brenda
additional information
-
ST6GalNAc VI tissue expression pattern, ST6GalNAc VI is downregulated in renal cancer cell lines and cancer tissues, in situ hybridization, overview
brenda
additional information
ST6GalNAc VI tissue expression pattern, ST6GalNAc VI is downregulated in renal cancer cell lines and cancer tissues, in situ hybridization, overview
brenda
additional information
ST6GalNAc VI tissue expression pattern, ST6GalNAc VI is downregulated in renal cancer cell lines and cancer tissues, in situ hybridization, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
the enzyme is a Golgi type II transmembrane glycosyltransferase
brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SIA7C_HUMAN
305
1
35395
Swiss-Prot
Secretory Pathway (Reliability: 1)
SIA7C_MOUSE
305
1
35414
Swiss-Prot
Secretory Pathway (Reliability: 1)
SIA7C_RAT
305
1
35150
Swiss-Prot
Secretory Pathway (Reliability: 1)
SIA7D_HUMAN
302
1
34201
Swiss-Prot
Secretory Pathway (Reliability: 1)
SIA7D_MOUSE
360
2
40773
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q5NDG1_DANRE
291
1
33529
TrEMBL
Secretory Pathway (Reliability: 1)
Q5K025_ORYLA
345
1
40002
TrEMBL
Secretory Pathway (Reliability: 4)
Q704X3_PIG
302
1
34227
TrEMBL
Secretory Pathway (Reliability: 1)
B7PL99_IXOSC
155
0
16612
TrEMBL
other Location (Reliability: 5)
B7PL99_IXOSC
155
0
16612
TrEMBL
other Location (Reliability: 5)
D2U4U1_DANRE
285
0
32498
TrEMBL
other Location (Reliability: 2)
Q0V9X0_XENTR
288
0
32773
TrEMBL
Secretory Pathway (Reliability: 1)
Q704S4_DANRE
306
1
35242
TrEMBL
Secretory Pathway (Reliability: 1)
Q704X4_BOVIN
323
1
36765
TrEMBL
Secretory Pathway (Reliability: 1)
Q704X2_CHICK
289
1
32780
TrEMBL
Secretory Pathway (Reliability: 1)
B5X2G4_SALSA
295
1
34431
TrEMBL
Secretory Pathway (Reliability: 1)
Q5K024_ORYLA
301
0
34460
TrEMBL
Secretory Pathway (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
two transmembrane isozymes, short and long enzyme form of 305 and 240 amino acids, respectively, the long form shows a short cytoplasmic transmembrane domain of sixteen amino acids and a catalytic domain of 280 amino acids, both isozymes contain the sialyl motif L and sialyl motif S, overview
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of ST6GalNAc VI and ST6GalNAc III with disialylgalactosylgloboside in Caki-1 cells
phylogenetic analysis, sequence comparison and sialylmotif regions analysis, overview
short and long enzyme form of 305 and 240 amino acids, respectively, DNA and amino acid sequence determination and analysis, alternative usage of the second exon seems to generate these two transcripts, expression analysis, sequence comparisons, overview, expression of soluble fusion enzyme, a truncated form of ST6GalNAc III lacking 21 amino acids from the NH2 terminus
-
phylogenetic analysis, sequence comparison and sialylmotif regions analysis, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the expression profiles of isoform ST6GalNAc VI among 20 renal cancer cell lines correlates clearly with those of disialylgalactosylgloboside, suggesting that the sialyltransferase involved in the synthesis of disialylgalactosylgloboside in the kidney is ST6GalNAc-VI. ST6GalNAc-VI and disialylgalactosylgloboside are found in proximal tubule epithelial cells in normal kidney tissues, while they are downregulated in renal cancer cell lines and cancer tissues
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bergh, M.L.E.; van den Eijnden, D.H.
Aglycon specificity of fetal calf liver and ovine and porcine submaxillary gland alpha-N-acetylgalactosaminide alpha 2 leads to 6 sialyltransferase
Eur. J. Biochem.
136
113-118
1983
Bos taurus
brenda
Higgins, E.A.; Siminovitch, K.A.; Zhuang, D.; Brockhausen, I.; Dennis, J.W.
Aberrant O-linked oligosaccharide biosynthesis in lymphocytes and platelets from patients with the Wiskott-Aldrich syndrome
J. Biol. Chem.
266
6280-6290
1991
Homo sapiens
brenda
Bergh, M.L.E.; Hooghwinkel, G.J.M.; Van den Eijnden, D.H.
Biosynthesis of the O-glycosidically linked oligosaccharide chains of fetuin. Indications for an alpha-N-acetylgalactosaminide alpha 2 leads to 6 sialyltransferase with a narrow acceptor specificity in fetal calf liver
J. Biol. Chem.
258
7430-7436
1983
Bos taurus, Ovis aries
brenda
Baubichon-Cortay, H.; Broquet, P.; George, P.; Louisot, P.
Different reactivity of two brain sialyltransferases towards sulfhydryl reagents. Evidence for a thiol group involved in the nucleotide-sugar binding site of the NeuAc alpha 2-3Gal beta 1-3GalNAc alpha(2-6)sialyltransferase
Glycoconjugate J.
6
115-127
1989
Rattus norvegicus
brenda
Dall'olio, F.
Sialyltransferases of developing rat brain
Glycoconjugate J.
7
301-310
1990
Rattus norvegicus
brenda
Takashima, S.; Kurosawa, N.; Tachida, Y.; Inoue, M.; Tsuji, S.
Comparative analysis of the genomic structures and promoter activities of mouse Siaa2,3Galb1,3GalNAc GalNAca2,6-sialyltransferase genes (ST6GalNAc III and IV): characterization of their Sp1 binding sites
J. Biochem.
127
399-409
2000
Mus musculus
brenda
Harduin-Lepers, A.; Stokes, D.C.; Steelant, W.F.A.; Samyn-Petit, B.; Krzewinski-Recchi, M.A.; Vallejo-Ruiz, V.; Zanetta, J.P.; Auge, C.; Delannoy, P.
Cloning, expression and gene organization of a human Neu5Aca2-3Galb1-3GalNAc a2,6-sialyltransferase: hST6GalNAc IV
Biochem. J.
352
37-48
2000
Homo sapiens (Q9H4F1), Homo sapiens
brenda
Tsuchida, A.; Okajima, T.; Furukawa, K.; Ando, T.; Ishida, H.; Yoshida, A.; Nakamura, Y.; Kannagi, R.; Kiso, M.
Synthesis of disialyl Lewis a (Le(a)) structure in colon cancer cell lines by a sialyltransferase, ST6GalNAc VI, responsible for the synthesis of alpha-series gangliosides
J. Biol. Chem.
278
22787-22794
2003
Homo sapiens
brenda
Senda, M.; Ito, A.; Tsuchida, A.; Hagiwara, T.; Kaneda, T.; Nakamura, Y.; Kasama, K.; Kiso, M.; Yoshikawa, K.; Katagiri, Y.; Ono, Y.; Ogiso, M.; Urano, T.; Furukawa, K.; Oshima, S.; Furukawa, K.
Identification and expression of a sialyltransferase responsible for the synthesis of disialylgalactosylgloboside in normal and malignant kidney cells: downregulation of ST6GalNAc VI in renal cancers
Biochem. J.
402
459-470
2007
Homo sapiens, Homo sapiens (Q8NDV1), Homo sapiens (Q969X2)
brenda
Harduin-Lepers, A.; Mollicone, R.; Delannoy, P.; Oriol, R.
The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach
Glycobiology
15
21G
2005
Danio rerio (Q5NDG1), Danio rerio (Q6ZXX8), Danio rerio (Q6ZXY7), Danio rerio (Q704S4), Homo sapiens (Q8NDV1), Homo sapiens (Q969X2), Homo sapiens (Q9BVH7), Homo sapiens (Q9H4F1)
-
brenda
Tsuchida, A.; Ogiso, M.; Nakamura, Y.; Kiso, M.; Furukawa, K.; Furukawa, K.
Molecular cloning and expression of human ST6GalNAc III: restricted tissue distribution and substrate specificity
J. Biochem.
138
237-243
2005
Homo sapiens
brenda
Wang, L.; Liu, Y.; Wu, L.; Sun, X.L.
Sialyltransferase inhibition and recent advances
Biochim. Biophys. Acta
1864
143-153
2016
Homo sapiens
brenda
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