Information on EC 2.4.1.41 - polypeptide N-acetylgalactosaminyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.4.1.41
-
RECOMMENDED NAME
GeneOntology No.
polypeptide N-acetylgalactosaminyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
hexosyl group transfer
-
-
hexosyl group transfer
-
-
hexosyl group transfer
Q07537
-
hexosyl group transfer
Q10473
-
hexosyl group transfer
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
mucin core 1 and core 2 O-glycosylation
-
-
mucin core 3 and core 4 O-glycosylation
-
-
Mucin type O-Glycan biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyl-transferase
Requires both Mn2+ and Ca2+. The glycosyl residue is transferred to threonine or serine hydroxy groups on the polypeptide core of submaxillary mucin, kappa-casein, apofetuin and some other acceptors of high molecular mass.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(UDP)-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
Q10471, Q10472, Q8N4A0, Q8NCW6
-
acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-glycoprotein
-
-
-
-
dGalNAc-T3
-
-
Eg-ppGalNAc-T1
-
-
GalNAc transferase
Q10471, Q10472, Q8N4A0, Q8NCW6
-
GalNAc transferase
Q10473
-
GalNAc-T
Q10471, Q10472
-
GalNAc-T
Q14435
-
GalNAc-T
Q8N4A0
-
GalNAc-T
Q8NCL4
-
GalNAc-T
Q8NCW6
-
GalNAc-T
Q96FL9
-
GalNAc-T
Q10473
-
GalNAc-T1
-
-
GalNAc-T1
Q10472
-
GalNAc-T1
Q10472
data suggest that the purified human GalNAc-transferase is a novel member of a family of polypeptide GalNAc-transferases, and a nomenclature GalNAc-T1 and GalNAc-T2 is introduced to distinguish the members
GalNAc-T11
-
-
GalNAc-T14
Q96FL9
-
GalNAc-T2
-
-
GalNAc-T2
Q10471
-
GalNAc-T2
Q10471
data suggest that the purified human GalNAc-transferase is a novel member of a family of polypeptide GalNAc-transferases, and a nomenclature GalNAc-T1 and GalNAc-T2 is introduced to distinguish the members
GalNAc-T3
-
-
GalNAc-T3
Q8N4A0
-
GalNAc-T4
-
-
GalNAc-T4
Q8N4A0
-
GalNAc-T6
-
-
GalNAc-T6
Q8NCL4
-
GalNAc-transferase
-
-
-
-
GalNAc-transferase
-
-
GalNAc-transferase
Q10471
-
GalNAc-transferase
Q10472
-
GalNAc-transferase
Q8N4A0
-
GalNAc-transferase T1
-
-
GalNAc-transferase T1
Q10472
-
GALNT12
Q8IXK2
-
glycopeptide-preferring polypeptide GalNAc transferase 10
-
-
N-acetylgalactosaminyltransferase-like 1
-
-
PGANT
Q6WV17, Q6WV19
-
polypeptide GalNAc transferase
-
-
polypeptide GalNAc transferase 2
-
-
polypeptide GalNAc-transferase
-
-
polypeptide GalNAc-transferase 2
-
-
polypeptide GalNAcT
-
-
polypeptide N-acetylgalactosaminyltransferase
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
-
polypeptide N-acetylgalactosaminyltransferase
Q96FL9
-
polypeptide N-acetylgalactosaminyltransferase
-
-
polypeptide N-acetylgalactosaminyltransferase 12
Q8IXK2
-
polypeptide N-acetylgalactosaminyltransferase 14
Q96FL9
-
polypeptide N-acetylgalactosaminyltransferase 2
-
-
polypeptide N-acetylgalactosaminyltransferase 6
-
-
polypeptide N-acetylgalactosaminyltransferase-1
-
-
polypeptide-N-acetylgalactosamine transferase
-
-
-
-
pp-GalNAc-T13
Q8IUC8
-
pp-GalNAc-T15
Q7Z4T8
-
pp-GalNAc-T2
Q10471
-
pp-GaNTases
-
-
ppGalNAc T1
-
-
ppGalNAc T10
-
-
ppGalNAc T2
-
-
ppGalNAc-T
-
-
-
-
ppGalNAc-T
-
-
ppGalNAc-T
Q10471
-
ppGalNAc-T
Q10472
-
ppGalNAc-T
Q14435, Q8N4A0, Q8NCL4
-
ppGalNAc-T1
-
-
ppGalNAc-T10
-
-
ppGalNAc-T12
Q8IXK2
-
ppGalNAc-T2
-
-
ppGalNAc-T2
Q6YK77
-
ppGalNAc-T3
Q6YBY0
-
ppGalNAc-T4
Q6TBR4
-
ppGalNAc-T5
Q6TBR3
-
ppGalNAc-T6
-
-
ppGalNAcT
Q8MVS5
-
ppGalNAcT
Q10471
-
ppGalNAcT
-
-
ppGalNAcT or hT
-
-
ppGaNTase
-
-
-
-
ppGaNTase
Q8MVS5
-
ppGaNTase-T1
Q07537
-
ppGaNTase-T1
-
-
ppGaNTase-T1
-
-
ppGaNTase-T1
Q10473
-
ppGaNTase-T1
Q29121
-
ppGaNTase-T11
Q8NCW6
-
ppGaNTase-T12
Q8IXK2
-
ppGaNTase-T3
Q14435
-
ppGaNTase-T3
P70419
-
ppGaNTase-T3
-
-
ppGaNTase-T4
-
-
ppGaNTase-T4
-
-
ppGaNTase-T5
O88422
-
ppGaNTase-T6
Q8NCL4
-
ppGaNTases
-
-
protein-UDP acetylgalactosaminyltransferase
-
-
-
-
UDP GalNAc:polypeptide N-acetylgalactosaminyltransferase
Q10471, Q10472, Q8N4A0, Q8NCW6
-
UDP-acetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
-
-
-
-
UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase
-
-
-
-
UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase
-
-
UDP-GalNAc polypeptides:N-acetyl-alpha-galactosaminyltransferase
Q10471
-
UDP-GalNAc transferase
Q10471, Q7Z4T8
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase
Q07537
abbreviated as ppGalNAc T
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase
Q6WV17, Q6WV19
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase
-
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase
Q10471
abbreviated as ppGalNAc T
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2
-
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1
-
-
UDP-GalNAc:polypeptide alphaN-acetylgalactosaminyltransferase
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
-
-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
Q29121
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
Q07537
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
Q8MVS5
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
Q9HCQ5
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
O88422
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
Q10473
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
Q6TBR3, Q6TBR4, Q6YBY0, Q6YK77
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 18
Q58A54
member of Y subfamily (together with UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8, 9 and 17)
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3
P70419
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
Q10471, Q10472
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
Q8N4A0
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13V1
-
splice variant 1 of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13, a 198 bp intron between exons 10 and 11 is not spliced out resulting in alteration of the lectin domain
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 16
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 17
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 18
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 19
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 20
-
-
UDP-N-acetyl-alpha-D-galactosaminyltransferase
Q14435
-
UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-6
-
-
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1
-
-
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T10
-
-
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3
Q6YBY0
-
UDP-N-acetylgalactosamine-glycoprotein N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine-protein N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:kappa-casein polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:polypeptide N-acetyl-alpha-galactosaminyltransferase
Q10471
-
UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase
Q10471
-
UDP-N-acetylgalactosamine:protein N-acetylgalactosaminyl transferase
-
-
-
-
UDP-N-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
-
uridine diphosphate-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
-
-
uridine diphosphoacetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
-
-
-
-
xGaltnl-1
-
-
glycoprotein acetylgalactosaminyltransferase
-
-
-
-
additional information
-
the enzyme belongs to the large family of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases, ppGalNAc Ts
additional information
-
the enzyme belongs to the family of UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferases, i.e. ppGalNAcTs
CAS REGISTRY NUMBER
COMMENTARY
9075-15-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme ppGalNAc T1
-
-
Manually annotated by BRENDA team
isozyme T1
-
-
Manually annotated by BRENDA team
lactating cow
-
-
Manually annotated by BRENDA team
ppGalNAc T1
SwissProt
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
enzyme form PGANT1
SwissProt
Manually annotated by BRENDA team
enzyme form PGANT3
SwissProt
Manually annotated by BRENDA team
enzyme form PGANT4
SwissProt
Manually annotated by BRENDA team
enzyme form PGANT6
SwissProt
Manually annotated by BRENDA team
enzyme form PGANT7
SwissProt
Manually annotated by BRENDA team
enzyme form PGANT8
-
-
Manually annotated by BRENDA team
PGANT2; PGANT2 is the orthologue of mammalian ppGalNAc T2
SwissProt
Manually annotated by BRENDA team
PGANT35A; PGANT35A is an orthologue of mammalian ppGalNTase -T11
UniProt
Manually annotated by BRENDA team
PGANT5; PGANT5 is the orthologue of mammalian ppGalNAc T1
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
; GalNAc-T14
UniProt
Manually annotated by BRENDA team
enzyme form pp-GalNAc-T15
SwissProt
Manually annotated by BRENDA team
enzyme form pp-GalNAc-T2
SwissProt
Manually annotated by BRENDA team
GalNAc-T1
UniProt
Manually annotated by BRENDA team
GalNAc-T1, -T2 and -T3
-
-
Manually annotated by BRENDA team
GalNAc-T11
SwissProt
Manually annotated by BRENDA team
GalNAc-T2
SwissProt
Manually annotated by BRENDA team
GalNAc-T4
SwissProt
Manually annotated by BRENDA team
GalNAc-T7
Uniprot
Manually annotated by BRENDA team
GalNAc-T9
-
-
Manually annotated by BRENDA team
isoforms ppGalNAcT-2 (hT2) and ppGalNAcT-10 (hT10)
-
-
Manually annotated by BRENDA team
isozyme T1-T4
-
-
Manually annotated by BRENDA team
isozymes ppGalNAc T2 and ppGalNAc T10
-
-
Manually annotated by BRENDA team
pp-GalNAc-T1, -T2, -T3 and -T4
-
-
Manually annotated by BRENDA team
ppGalNAc T2
SwissProt
Manually annotated by BRENDA team
ppGalNAc-T1
UniProt
Manually annotated by BRENDA team
ppGalNAc-T13, -T1 and -T9
-
-
Manually annotated by BRENDA team
ppGalNAc-T14 and -T2
-
-
Manually annotated by BRENDA team
ppGalNAc-T2
SwissProt
Manually annotated by BRENDA team
ppGalNAc-T3
SwissProt
Manually annotated by BRENDA team
ppGalNAc-T4
SwissProt
Manually annotated by BRENDA team
ppGalNAc-T6
SwissProt
Manually annotated by BRENDA team
ppGalNAcT-2
SwissProt
Manually annotated by BRENDA team
recombinant GalNAc-T2 and -T4
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
BALB/c mouse, ppGaNTase-T6, -T1 and -T4
-
-
Manually annotated by BRENDA team
C57BL/6 wild-type, isozyme ppGalNAcT-1, encoded by gene Galnt1, and isozymes ppGalNAcT-2, and ppGalNAcT-3
-
-
Manually annotated by BRENDA team
isoenzymes ppGaNTase-T4 and -T1
-
-
Manually annotated by BRENDA team
isoform ppGalNAcT-1
-
-
Manually annotated by BRENDA team
ppGalNAc-T13, subsequently termed ppGalNAc-T8
-
-
Manually annotated by BRENDA team
female albino rats
-
-
Manually annotated by BRENDA team
GalNAc-T1
-
-
Manually annotated by BRENDA team
GalNAc-T1
SwissProt
Manually annotated by BRENDA team
male rats
-
-
Manually annotated by BRENDA team
ppGaNTase-T9
Uniprot
Manually annotated by BRENDA team
Wistar rats, ppGaNTase-T6, -T1 and -T4
Uniprot
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
isozymes xGalnt1, -4, -6, -7
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
aberrant mucin O-glycosylation is often observed in cancer and is characterized by the expression of immature simple mucin-type carbohydrate antigens. Altered expression of ppGalNAc-Ts can be one of the mechanisms that explain the changes in mucin O-glycosylation during malignant transformation
malfunction
-
mutation of the enzyme might be involved in development of cancer
malfunction
-
Overexpression of polypeptide N-acetylgalactosaminyltransferase 6 induces epithelial-to-mesenchymal transition-like morphologic alterations
metabolism
-
GalNAc-type protein O-glycosylation is important in modulating protein processing, O-linked glycans have important biological functions
physiological function
-
ppGalNAc-T6 is one of the enzymes responsible for the initial step in mucin O-glycosylation
physiological function
-
the GALNT enzyme plays a role in initiating mucin type O-linked protein glycosylation
physiological function
-
UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferases regulate the mucin-type O-glycan biosynthesis
physiological function
-
site-specific O-glycosylation inhibits proprotein activation of the lipase inhibitor ANGPTL3 in HepG2 cells
physiological function
-
the lectin domain strictly recognizes GalNAc on the substrate and this specificity controls the glycosylation pathway
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
erythropoietin T + UDP-Gal
erythropoietin T-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
erythropoietin T + UDP-Gal
erythropoietin T-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
also catalysed by mutants GalTNAc-T2-D458H and GalTNAc-T2-D541A
-
-
?
hCG-beta + UDP-Gal
hCG-beta-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
IgA hinge + UDP-Gal
IgA hinge-nGal + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
IgA hinge + UDP-GalNAc
IgA hinge-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
IgA hinge + UDP-GalNAc
IgA hinge-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
GalTNAc-T11 incorporates only two GalNAc residues into IgA hinge peptide
-
-
?
IgA hinge + UDP-GalNAc
IgA hinge-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
mutant GalNAc-T2-D458H incorporates 1-2 fewer GalNAc residues than wild-type
-
-
?
MUC1 + UDP-GalNAc
MUC1-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
MUC1 + UDP-GalNAc
MUC1-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-T4 lectin domain does not exhibit selective specificities for peptide sequences, or the density or pattern of GalNAc glycosylation, GalNAc-T4 lectin domain mediates GalNAc-glycopeptide substrate specificity
-
-
?
MUC1 + UDP-GalNAc
MUC1-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
mutant GalNAc-T2-D458H incorporates 1-2 fewer GalNAc residues than wild-type, GalNAc-T2 lectin domain does not exhibit selective specificities for peptide sequences, or the density or pattern of GalNAc glycosylation
-
-
?
MUC1-2GalNAc + UDP-GalNAc
MUC1-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
MUC1a' + UDP-GalNAc
MUC1a'-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
MUC1b' + UDP-GalNAc
MUC1b'-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
MUC2 + UDP-GalNAc
MUC2-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
MUC2-6GalNAc + UDP-GalNAc
MUC2-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
MUC5AC + UDP-GalNAc
GalNAc-Thr9-MUC5AC + UDP
show the reaction diagram
-
hT2CD, hT2: glycosylation site selection driven by and substrate binding through its catalytic domain, hT10: not catalysed by hT10 because hT10 does not recognize naked peptides
preferred site for glycosylation by hT2 and hT2CD compared to Thr-3, Thr-10 and Thr-13
-
?
MUC5AC glycopeptides + UDP-GalNAc
GalNAc-MUC5AC + UDP
show the reaction diagram
-
hT2: site preference of glycosylation depends on location of pre-existing GalNAc and is mediated by its lectin domain which directs glycosylation 10 residues N- or C-terminal to an extant GalNAc residue and aids site selection only when potential site is N-terminal to an extant GalNAc residue not C-terminal, Thr-9 is no preferred site of glycosylation, hT10: must recognize existing GalNAc residues via its catalytic domain which directs selection to the glycosylation site immediately N-terminal to the present GalNAc,
-
-
?
MUC5AC-13 + UDP-GalNAc
GalNAc-Thr12-MUC5AC-13 + UDP
show the reaction diagram
-
hT10, hT10CD, hT10CD-hT2LD
-
-
?
MUC5AC-13 + UDP-GalNAc
GalNAc-Thr3-MUC5AC-13 + UDP
show the reaction diagram
-
hT2: substrate binding through its catalytic domain, hT10: transfer of only single GalNAc residues
predominant product of hT2 and hT10
-
?
MUC5AC-13 + UDP-GalNAc
GalNAc-Thr9-MUC5AC-13 + UDP
show the reaction diagram
-
hT2, hT2CD: no initial burst phase during catalysis
not preferred by hT2, preferred by hT2CD
-
?
MUC5AC-3 + UDP-GalNAc
GalNAc-Thr13-MUC5AC-3 + UDP
show the reaction diagram
-
hT2: no initial burst phase during catalysis, substrate binding through its catalytic domain, hT10: transfer of only single GalNAc residues
hT2: preferred site for glycosylation, mediated by enhanced product release through lectin domain, hT10: predominant product
-
?
MUC5AC-3 + UDP-GalNAc
GalNAc-Thr2-MUC5AC + UDP
show the reaction diagram
-
hT10CD, hT10CD-hT2LD, hT10: catalysis faster than for MUCAC-9
-
-
?
MUC5AC-3 + UDP-GalNAc
GalNAc-Thr9-MUC5AC-3 + UDP
show the reaction diagram
-
hT2, hT2CD
not preferred by hT2, hT2CD: preferred site for glycosylation, lack of lectin domain in hT2CD results in rate-limiting product release
-
?
MUC5AC-3,13 + UDP-GalNAc
GalNAc-Ser-5-MUC5AC-3,13 + UDP
show the reaction diagram
-
hT2, not catalysed by hT2CD and hT2CD-hT10LD
preferred site by hT2
-
?
MUC5AC-3,13 + UDP-GalNAc
GalNAc-Thr2,12-MUC5AC-3,13 + UDP
show the reaction diagram
-
hT10, hT10CD, hT10CD-hT2LD
-
-
?
MUC5AC-9 + UDP-GalNAc
GalNAc-Thr2-MUC5AC-9 + UDP
show the reaction diagram
-
not catalysed by hT10CD and hT10CD-hT2LD, hT10: catalysis slower than for MUC5AC-3
preferred site of glycosylation by hT10
-
?
MUC7 + UDP-GalNAc
MUC7-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
OSM fragment + UDP-Gal
OSM fragment-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
UDP-alpha-GalNAc + polypeptide
GalNAc-alpha-polypeptide + UDP
show the reaction diagram
Q8MVS5
-
major mucin-type O-glycan in embryonic tracheal system along the apical region and luman of the tracheal tubes O-glycan, detectable by lectins Jacalin, soybean agglutinin and Vicia villosa agglutinin
-
?
UDP-galactose + Muc1 peptide
UDP + galactosyl-Muc1 peptide
show the reaction diagram
-
synthetic substrate, 2 of 3 threonine residues on the Muc1 tandem repeat peptides, none of the serine residues, maximum is 2 Mol of GalNAc linked to each 20-residue repeat unit
-
?
UDP-galactose + Muc2 peptide
UDP + galactosyl-Muc2 peptide
show the reaction diagram
-
peptides derived of Muc2 mucin
-
-
?
UDP-galactose + Muc2 peptide
UDP + galactosyl-Muc2 peptide
show the reaction diagram
-
only GalNAc-T2, only with the Muc2 acceptor peptide
-
-
?
UDP-galactose + Muc2 peptide
UDP + galactosyl-Muc2 peptide
show the reaction diagram
-
investigation of preferences for distinct threonine residues in the peptide sequences
-
-
?
UDP-galactose + PTTTPITTTTK
UDP + galactosyl-PTTTPITTTTK
show the reaction diagram
-
Muc2 peptide, investigation of preferences for distinct threonine residues in the peptide sequences of isozyme T1 to T4, linked to FITC
-
-
?
UDP-GalNAc + Ac-TPPA
UDP + Ac-(GalNAcalpha1-)TPPA
show the reaction diagram
-
pH 7.5, 37C
-
-
?
UDP-GalNAc + apomucin
UDP + GalNAc-mucin
show the reaction diagram
Q10473
apomucin is a deglycosylated bovine submaxillary mucin, mutants W328Y, W328F, W328A, W316H and W316A are inactive, mutants W316Y and W316F show 40% and 20% activity, respectively, relative to wild-type
-
-
?
UDP-GalNAc + AQPTPPP
UDP + AQP-(GalNAcalpha1-)TPPP
show the reaction diagram
-
pH 7.5, 37C, 0.2 mM, 100% activity
-
-
?
UDP-GalNAc + EA2
GalNAc-EA2 + UDP
show the reaction diagram
-
-
-
-
?
UDP-GalNAc + EA2
GalNAc-EA2 + UDP
show the reaction diagram
Q10471
ternary complex of ppGalNAcT-2 in crystal structure PDB: 2FFU, UDP-GalNAc binding results in the closed confirmation of loop B which stabilises loop A by binding of loop A (N102) to loop B (R362), EA2 peptide binds in an extended confirmation
binary complex of UDP and ppGalNAcT-2 in crystal structure PDB: 2FFV
-
?
UDP-GalNAc + GAGA(X)3T(X)3AGAGK
GAGA(X)3(GalNAc)T(X)3AGAGK + UDP
show the reaction diagram
Q6WV17, Q6WV19
-
-
-
?
UDP-GalNAc + GAGA(X)3T(X)3AGAGK
UDP + GAGA(X)3(GalNAc)T(X)3AGAGK
show the reaction diagram
Q07537
-
-
-
?
UDP-GalNAc + GAGA(X)3T(X)3AGAGK
UDP + GAGA(X)3(GalNAc)T(X)3AGAGK
show the reaction diagram
Q10471
-
-
-
?
UDP-GalNAc + GAGA(X)5T(X)5AGAGK
GAGA(X)5(GalNAc)T(X)5AGAGK + UDP
show the reaction diagram
Q6WV17, Q6WV19
transferase activity relatively insensitive to the nature of amino acids 4 and 5 residues away from site of glycosylation, high correlation between peptide preferences of PGANT5 and mammalian orthologue ppGalNAc T1 with r(square) = 0.67, the hydrophobic residue proline is preferred at the -1, +1, and +3 positions, the hydrophobic residues valine and tyrosin are moderately preferred at the -1 and +3 positions, the hydrophobic residue methionine is disfavoured at the -1 position, low hydrophilic preference at the -1 position, strong glutamate/aspartate preference at the +1 position, higher preference of glutamate at +1 and +2 positions than mammalian orthologue ppGalNAc T1
-
-
?
UDP-GalNAc + GAGA(X)5T(X)5AGAGK
GAGA(X)5(GalNAc)T(X)5AGAGK + UDP
show the reaction diagram
Q6WV17, Q6WV19
transferase activity relatively insensitive to the nature of amino acids 4 and 5 residues away from site of glycosylation, very high correlation between peptide preferences of PGANT2 and mammalian orthologue ppGalNAc T2 with r(square) = 0.92
-
-
?
UDP-GalNAc + GAGA(X)5T(X)5AGAGK
UDP + GAGA(X)5(GalNAc)T(X)5AGAGK
show the reaction diagram
Q10471
very high correlation between peptide preferences of ppGalNAc T2 and fly orthologue PGANT2 with r(square) = 0.92
-
-
?
UDP-GalNAc + GAGA(X)5T(X)5AGAGK
UDP + GAGA(X)5(GalNAc)T(X)5AGAGK
show the reaction diagram
Q07537
very high correlation between peptide preferences of ppGalNAc T2 and fly orthologue PGANT2 with r(square) = 0.92, the hydrophobic residue proline is preferred at the -1, +1, and +3 positions, the hydrophobic residues valine and tyrosin are moderately preferred at the -1 and +3 positions, the hydrophobic residue methionine is disfavoured at the -1 position, low hydrophilic preference at the -1 position, strong glutamate/aspartate preference at the +1 position, lower preference of glutamate at +1 and +2 positions than fly orthologue PGANT5
-
-
?
UDP-GalNAc + GAGA(X)nT(X)nAGAGK
GAGA(X)n(GalNAc)T(X)nAGAGK + UDP
show the reaction diagram
Q6WV17, Q6WV19
library of unmodified peptides, with randomized residue at position X and n=3 or n=5
-
-
?
UDP-GalNAc + GAGA(X)nT(X)nAGAGK
GAGA(X)n(GalNAc)T(X)nAGAGK + UDP
show the reaction diagram
Q07537
library of unmodified peptides, with randomized residue at position X and n=3 or n=5, random peptide preferences are not significantly altered by increased peptide substrate length n=5 compared to n=3 or the proximity of flanking Gly and Ala residues to the site of glycosylation, major peptide substrate preference determinants are the 2 to 3 residues flanking the site of glycosylation
-
-
?
UDP-GalNAc + GAGA(X)nT(X)nAGAGK
GAGA(X)n(GalNAc)T(X)nAGAGK + UDP
show the reaction diagram
Q10471
library of unmodified peptides, with randomized residue at position X and n=3 or n=5, random peptide preferences are not significantly altered by increased peptide substrate length n=5 compared to n=3 or the proximity of flanking Gly and Ala residues to the site of glycosylation, major peptide substrate preference determinants are the 2 to 3 residues flanking the site of glycosylation
-
-
?
UDP-GalNAc + GVVPTVVPG
UDP + GVVP(GalNAc)TVVPG
show the reaction diagram
Q10473
GVVPTVVPG is a synthetic peptide with threonine as acceptor site, weaker acceptor substrate for wild-type and truncated version P-T1/delta42 as PPDAATAAPL
-
-
?
UDP-GalNAc + HGVTSAPDTRPAPGSTAPPA
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-GalNAc + N-acetyl-4-benzoyl-L-Phe-L-Pro-L-Tyr-L-Pro-L-Pro-L-Pro-NH2
UDP + N-acetyl-4-benzoyl-L-Phe-L-Pro-L-(GalNAcalpha1-)Tyr-L-Pro-L-Pro-L-Pro-NH2
show the reaction diagram
-
pH 7.5, 37C
-
-
?
UDP-GalNAc + polypeptide
GalNAc-alpha-polypeptide + UDP
show the reaction diagram
-
-
glycosylation at Thr or Ser
-
?
UDP-GalNAc + PPDAATAAPL
UDP + PPDAA(GalNAc)TAAPL
show the reaction diagram
Q10473
PPDAATAAPL is a synthetic peptide with threonine as acceptor site, efficient acceptor substrate for wild-type and truncated version P-T1/delta42
-
-
?
UDP-GalNAc + PRFODSSSKAPPPLPSPSRLPG
GalNAc-PRFODSSSKAPPPLPSPSRLPG + UDP
show the reaction diagram
-
-
-
-
?
UDP-GalNAc + PTTTPISTTTMVTPTPTPTC
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-GalNAc + PTTTPITTTG
UDP + P-(GalNAcalpha1-)TTTPITTTG + P-(GalNAcalpha1-)TTTPI-(GalNAcalpha1-)TTTG
show the reaction diagram
-
pH 7.5, 37C, 0.2 mM, 26% activity relative to AQPTPPP
-
-
?
UDP-GalNAc + selectin
GalNAc-selectin + UDP
show the reaction diagram
-
-
reduced expression of cell surface E- and P-selectins (fourfold and fivefold) and L-selectins on immune cells of ppGalNAcT-1 deficient mice
-
?
UDP-GalNAc + TPTGTQTPTG
UDP + TPTG-(GalNAcalpha1-)TQTPTG
show the reaction diagram
-
pH 7.5, 37C, 0.2 mM, 8% activity relative to AQPTPPP
-
-
?
UDP-GalNAc + TTTVTPTPTG
UDP + TTTV-(GalNAcalpha1-)TPTPTG + T-(GalNAcalpha1-)TTV-(GalNAcalpha1-)TPTPTG + T-(GalNAcalpha1-)T-(GalNAcalpha1-)TV-(GalNAcalpha1-)TP-(GalNAcalpha1-)TPTG + T-(GalNAcalpha1-)TTV-(GalNAcalpha1-)TP-(GalNAcalpha1-)TP-(GalNAcalpha1-)TG + TT-(GalNAcalpha1-)TV-(GalNAcalpha1-)TPTPTG + ?
show the reaction diagram
-
pH 7.5, 37C, 0.2 mM, 109% activity relative to AQPTPPP
monoglycosylated product appears after 30 min, higher glycosylated products appear with increasing time of incubation
-
?
UDP-GalNAc + TVTPTPTPTG
UDP + TVTP-(GalNAcalpha1-)TPTPTG
show the reaction diagram
-
pH 7.5, 37C, 0.2 mM, 145% activity relative to AQPTPPP
-
-
?
UDP-GalNAc + VLTTTATTPTA
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + (glycosylated GTTPSPVPTTSTTSAP)
UDP + ?
show the reaction diagram
-
natural-type (alpha-GalNAc-O-Thr) and unnatural-type (beta-GalNAc-O-Thr, alpha-Fuc-O-Thr and beta-GlcNAc-O-Thr) glycosylated
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Ac-CIRIQRGPGRAFVTIGKIGNMR
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Ac-QATEYEYLDYDFLPETEPPEM
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + AHGVTSAPDTR
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GAGAEAPTPAPAGAGK
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTAKPTTLKPTE
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + GT[GalNAc]TPSPVPTTSTTSAP
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
show the reaction diagram
-
-
glycosylation at Thr-3 and Thr-13
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + GT[GalNAc]TP[GalNAc]SPVPTTSTTSAP
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTST[GalNAc]TSAP
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTST[GalNAc]TSAP
UDP + GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTST[GalNAc]TSAP
UDP + GT[GalNAc]TP[GalNAc]SPVPTTST[GalNAc]TSAP
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GT[GalNAc]TPSPVPTTSTTSAP
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GT[GalNAc]TPSPVPTTSTTSAP
UDP + GT[GalNAc]TPSPVPTTS[GalNAc]T[GalNAc]TSAP
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GT[GalNAc]TPSPVPTTSTTSAP
UDP + G[GalNAc]T[GalNAc]TPSPVPTTST[GalNAc]TSAP
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
UDP + GT[GalNAc]TPSPVPTTS[GalNAc]T[GalNAc]TSAP
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + PDTRPAPGSTAPPAC
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + PSTPPTPSPSTPPTPSPS
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + SPTTSTPISSTPQPTS
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + A1 protein
UDP + N-acetyl-D-galactosaminyl-A1 protein
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-CIRIQRGPGRAFVTIGKIGNMR
UDP + N-acetyl-D-galactosaminylated Ac-CIRIQRGPGRAFVTIGKIGNMR
show the reaction diagram
Q10471, Q10472, Q8N4A0
-
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-PFVTHPGYD
UDP + N-acetyl-D-galactosaminylated Ac-PFVTHPGYD
show the reaction diagram
Q10471, Q10472, Q8N4A0
-
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-QATEYEYLDYDFLPETEPPEM
UDP + N-acetyl-D-galactosaminylated Ac-QATEYEYLDYDFLPETEPPEM
show the reaction diagram
Q10471, Q10472, Q8N4A0
-
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-QATEYEYLDYDFLPETEPPEM
UDP + N-acetyl-D-galactosaminylated Ac-QATEYEYLDYDFLPETEPPEM
show the reaction diagram
Q10471, Q10472, Q8N4A0
acceptor substrate
-
-
?
UDP-N-acetyl-D-galactosamine + AcTPPP
UDP + N-acetyl-D-galactosaminyl-AcTPPP
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + AHGVTSAPDTR
UDP + N-acetyl-D-galactosaminylated AHGVTSAPDTR
show the reaction diagram
Q10471, Q10472, Q8N4A0
-
-
-
?
UDP-N-acetyl-D-galactosamine + AHGVVTSAPDTR
UDP + ?
show the reaction diagram
Q10471, Q7Z4T8
i.e. Muc1, 3% of the activity with Muc5AC as substrate, enzyme form pp-GalNAc-T2
-
-
?
UDP-N-acetyl-D-galactosamine + AHGVVTSAPDTR
UDP + ?
show the reaction diagram
Q10471, Q7Z4T8
i.e. Muc1a, enzyme form pp-GalNAc-T15
-
-
?
UDP-N-acetyl-D-galactosamine + ANTPSFPTATSPAPPI
UDP + ?
show the reaction diagram
Q10471, Q7Z4T8
i.e. Muc13, about 25% of the activity with Muc5AC as substrate, enzyme form pp-GalNAc-T2
-
-
?
UDP-N-acetyl-D-galactosamine + ANTPSFPTATSPAPPI
UDP + ?
show the reaction diagram
Q10471, Q7Z4T8
i.e. Muc13, about 50% of the activity with Muc1a, enzyme form pp-GalNAc-T15
-
-
?
UDP-N-acetyl-D-galactosamine + apoantifreeze glycoproteins
UDP + N-acetyl-D-galactosaminyl-apoantifreeze glycoproteins
show the reaction diagram
-
apoantifreeze glycoprotein of high molecular weight accepts GalNAc much faster than apoantifreeze glycoprotein 8
-
-
?
UDP-N-acetyl-D-galactosamine + apofetuin
UDP + N-acetyl-D-galactosaminyl-apofetuin
show the reaction diagram
-
lowest rate of transfer
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
bovine apomucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
enzymatically prepared apomucin accepts GalNAc much faster than chemically prepared apomucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
deglycosylated bovine submaxillary mucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
deglycosylated bovine submaxillary mucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
deglycosylated bovine submaxillary mucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
porcine apomucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
GalNAc-T1
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
acceptor: apomucin motif encoded by the MUC5AC gene
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
ovine apomucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
best substrate, poorer substrates: asialo mucin, native mucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
show the reaction diagram
-
deglycosylated Cowper's gland, swine and human trachea mucins
-
?
UDP-N-acetyl-D-galactosamine + AWIPTPPPIPG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + bone sialoprotein
UDP + UDP-N-acetyl-D-galactosaminyl-bone sialoprotein
show the reaction diagram
-
preferred substrate of isozyme ppGalNAcT-1, glycosylation of Thr101, Ser131, Thr199, and Ser214, glycosylation pattern, overview
-
-
?
UDP-N-acetyl-D-galactosamine + CPPTPSATTPAPPSSSAPPETTAA
UDP + N-acetyl-D-galactosaminylated CPPTPSATTPAPPSSSAPPETTAA
show the reaction diagram
Q10471, Q10472, Q8N4A0
mucin derived substrate
-
-
?
UDP-N-acetyl-D-galactosamine + CPPTPSATTPAPPSSSAPPETTAA
UDP + N-acetyl-D-galactosaminylated CPPTPSATTPAPPSSSAPPETTAA
show the reaction diagram
Q10471, Q10472, Q8N4A0
mucin derived substrate, acceptor substrate
-
-
?
UDP-N-acetyl-D-galactosamine + deglycosylated ovine submaxillary mucin
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + DSTTPAPTTK
UDP + N-acetyl-D-galactosaminylated DSTTPAPTTK
show the reaction diagram
Q10471, Q10472, Q8N4A0
mucin derived substrate
-
-
?
UDP-N-acetyl-D-galactosamine + DSTTPAPTTK
UDP + N-acetyl-D-galactosaminylated DSTTPAPTTK
show the reaction diagram
Q10471, Q10472, Q8N4A0
mucin derived substrate, acceptor substrate
-
-
?
UDP-N-acetyl-D-galactosamine + DSTTPAPTTK
UDP + N-acetyl-D-galactosaminylated-DSTTPAPTTK
show the reaction diagram
Q10471, Q10472, Q8N4A0
mucin derived substrate, acceptor substrate
-
-
?
UDP-N-acetyl-D-galactosamine + fibronectin
UDP + N-acetyl-D-galactosaminyl-fibronectin
show the reaction diagram
-
fibronectin is a physiological substrate for GalNAc-T3
-
-
?
UDP-N-acetyl-D-galactosamine + GAGAPGPTPGPAGAGK
UDP + GAGAPGP-(N-acetyl-D-galactosaminylT)-PGPAGAGK
show the reaction diagram
-
optimal isozyme ppGalNAc T2 peptide substrate
-
-
?
UDP-N-acetyl-D-galactosamine + GAGPGTXASSVGVTGAPGSG
UDP + ?
show the reaction diagram
-
low activity
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
show the reaction diagram
Q925R7
ppGaNTase-T9: acceptors are di- and triglycosylated MUC5AC and mono-glycosylated EA2, obtained by prior action of ppGaNTase-T1, but not the unmodified peptides, formation of a tetra-glycopeptide species from MUC5AC triglycopeptide substrate, ppGaNTase-T7 forms a hexa-glycopeptide species
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
show the reaction diagram
Q8MVS5
acceptor: MUC5AC-13 glycopeptide
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
show the reaction diagram
Q86SF2
GalNAc-T7: exclusive specificity for partially GalNAc-glycosylated acceptor substrates, GalNAc-glycosylated peptide substrates derived from the tandem repeats of human Muc2 and rat submandibular gland mucin, specificity of GalNAc-T4
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
show the reaction diagram
-
rGalNAc-T4 is dependent on the presence of GalNAc on acceptor peptides, activity is triggered by a lectin-like interaction of enzyme with the glycopeptide directed by the putative lectin domain found in the C-terminal region, rGalNAc-T2 activity is enhanced on glycosylated acceptor peptides
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
show the reaction diagram
-
GalNAc-T1 may also specifically recognize and glycosylate partially glycosylated acceptors
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
show the reaction diagram
Q9R0C5
ppGaNTase-T6 requires at least 2 intact GalNAc residues in the substrate, acceptor: MUC5AC-glycopeptide, obtained by the action of ppGaNTase-T1
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
show the reaction diagram
-
ppGalNAc-T14 can utilize GalNAc transferred peptides as substrates
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
show the reaction diagram
-
ppGalNAc-T4 and -T7 prefer peptides having GalNAc residues as acceptor substrates
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
show the reaction diagram
-
acceptors: partially glycosylated versions of a peptide derived from mucin2, pp-GalNAc-T1, -T2, -T3 and -T4 exhibit distinct specificities toward glycopeptides, pathway of incorporation of the second and third GalNAc, isoenzymes may recognize directly GalNAc residues in the vicinity
-
-
?
UDP-N-acetyl-D-galactosamine + GKPRPYSPRPTSHPRPIRV
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. drosocin, low activity, enzyme form PGANT8
-
-
-
UDP-N-acetyl-D-galactosamine + GSPAGDVGAPAVDSGASQAAG
UDP + ?
show the reaction diagram
-
low activity
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTS-(O-GalNAc)T-SAP
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTS-(O-GalNAc)T-SAP
UDP + ?
show the reaction diagram
Q6YBY0
-
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTS-(O-GalNAc)T-SAP
UDP + ?
show the reaction diagram
-
23% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSA
UDP + N-acetyl-D-galactosaminyl-[GTTPSPVPTTSTTSA]
show the reaction diagram
-
i.e. Muc5Ac peptide
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAk
UDP + ?
show the reaction diagram
Q10471, Q7Z4T8
i.e. Muc5AC, about 55% of the activity with Muc1a, pp-GalNAc-T15 shows significantly less catalytic activity than pp-GalNAc-T2,T15 transferrs up to seven GalNAcs to the Muc5AC peptide, while T2 transferrs up to five GalNAcs, enzyme form pp-GalNAc-T15
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAk
UDP + ?
show the reaction diagram
Q10471, Q7Z4T8
i.e. Muc5AC, pp-GalNAc-T15 shows significantly less catalytic activity than pp-GalNAc-T2,T15 transferrs up to seven GalNAcs to the Muc5AC peptide, while T2 transferrs up to five GalNAcs
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + ?
show the reaction diagram
Q6YBY0
0.3% of the activity with GTTPSPVPTTS-(O-GalNAc)T-TSAP
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + ?
show the reaction diagram
-
73% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. MUC5AC
-
-
-
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. MUC5AC, enzyme form PGANT4
-
-
-
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. MUC5AC, low activity enzyme form PGANT6
-
-
-
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. MUC5AC, low activity, enzyme form PGANT8
-
-
-
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. MUC5AC, very low activity, enzyme form PGANT3
-
-
-
UDP-N-acetyl-D-galactosamine + HGVTSAPDTRP
UDP + ?
show the reaction diagram
-
i.e. Muc1
-
-
?
UDP-N-acetyl-D-galactosamine + HIV-V3 peptide
UDP + N-acetyl-D-galactosaminyl-HIV-V3 peptide
show the reaction diagram
-
submaxillary gland enzyme, low activity
-
-
?
UDP-N-acetyl-D-galactosamine + HIV-V3 peptide
UDP + N-acetyl-D-galactosaminyl-HIV-V3 peptide
show the reaction diagram
-
HIVIIIBgp120, only GalNAc-T3
-
-
?
UDP-N-acetyl-D-galactosamine + HIV-V3 peptide
UDP + N-acetyl-D-galactosaminyl-HIV-V3 peptide
show the reaction diagram
-
placenta, but not liver enzyme
-
-
?
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
show the reaction diagram
-
placenta enzyme, only Ser acceptor sites, with a very low activity
-
-
?
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
show the reaction diagram
-
only Ser acceptor sites, with a very low activity
-
-
?
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
show the reaction diagram
-
only GalNAc-T2
-
-
?
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
show the reaction diagram
-
submaxillary gland enzyme
-
-
?
UDP-N-acetyl-D-galactosamine + immunoglobulin A1
UDP + N-acetyl-D-galactosaminyl-immunoglobulin A1
show the reaction diagram
-
O-linked glycosylation of the human IgA1 hinge region by ppGalNAc-T2, synthetic IgA hinge peptide: ppGalNAc-T2 shows strongest activity and is able to transfer GalNAc to almost all possible glycosylation sites, other ppGalNAc-Ts show extremely weak activities
-
-
?
UDP-N-acetyl-D-galactosamine + ITTTTTPLPTG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + kappa-casein
UDP + N-acetyl-D-galactosaminyl-kappa-casein
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + kappa-casein
UDP + N-acetyl-D-galactosaminyl-kappa-casein
show the reaction diagram
-
kappa-subcomponent 1, the nonglycosylated kappa-casein, is the best substrate among kappa-casein subcomponents, asialo kappa-casein, agalacto kappa-casein and nature kappa-casein, glycosylation of kappa-casein occurs after casein micelle formation triggered by the accumulation of Ca2+ in vivo
-
-
?
UDP-N-acetyl-D-galactosamine + LGEPLGLAPSSSP
UDP + ?
show the reaction diagram
-
low activity
-
-
?
UDP-N-acetyl-D-galactosamine + LPPVTTTPAPG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + MPTAGTPPPIG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC4AC-13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT2
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT2
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT4
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT6
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT7
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT8
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
high activity, enzyme form PGANT5
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
PGANT1
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
very low activity, enzyme form PGANT3
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3/13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT8
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3/13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
high activity, enzyme form PGANT4
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3/13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
high activity, enzyme form PGANT5
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3/13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
high activity, enzyme form PGANT7
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3/13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
low activity, enzyme form PGANT2
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AC-3/13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
preferred substrate, enzyme form PGANT4
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AX-13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT4
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AX-13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT6
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AX-13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT8
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AX-13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
high activity, enzyme form PGANT5
-
-
?
UDP-N-acetyl-D-galactosamine + mucin MUC5AX-13
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
low activity, enzyme form PGANT7
-
-
?
UDP-N-acetyl-D-galactosamine + myelin basic protein
UDP + N-acetyl-D-galactosaminyl-myelin basic protein
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + myelin basic protein
UDP + N-acetyl-D-galactosaminyl-myelin basic protein
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + osteopontin
UDP + N-acetyl-D-galactosaminyl-osteopontin
show the reaction diagram
-
preferred substrate of isozyme ppGalNAcT-1, glycosylation pattern, overview
-
-
?
UDP-N-acetyl-D-galactosamine + osteopontin
UDP + N-acetyl-D-galactosaminyl-osteopontin
show the reaction diagram
-
isozyme ppGalNAc T10 prefers previously glycosylated peptides as substrates, ppGalNAc T10 exhibits a single large preference for Ser/Thr-O-GalNAc at the +1, C-terminal, position relative to the Ser or Thr acceptor site
-
-
?
UDP-N-acetyl-D-galactosamine + P-(O-GalNAc)T-TDSTTPAPTTK
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + P-(O-GalNAc)T-TDSTTPAPTTK
UDP + ?
show the reaction diagram
Q6YBY0
0.3% of the activity with GTTPSPVPTTS-(O-GalNAc)T-TSAP
-
-
?
UDP-N-acetyl-D-galactosamine + PADVTTAAPGG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PDTRPAPGSTAPPAC
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. MUC1b
-
-
?
UDP-N-acetyl-D-galactosamine + PDTRPAPGSTAPPAC
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. MUC1b, enzyme form PGANT4
-
-
?
UDP-N-acetyl-D-galactosamine + PDTRPAPGSTAPPAC
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. MUC1b, low activity, enzyme form PGANT2
-
-
?
UDP-N-acetyl-D-galactosamine + PDTRPAPGSTAPPAC
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. MUC1b, low activity, enzyme form PGANT6
-
-
?
UDP-N-acetyl-D-galactosamine + PDTRPAPGSTAPPAC
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. MUC1b, low activity, enzyme form PGANT8
-
-
?
UDP-N-acetyl-D-galactosamine + PGGDSSSYQPG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PGLPPTTPAVTTTATP
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PHMAQVTVGPGL
UDP + N-acetyl-D-galactosaminyl-PHMAQVTVGPGL
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PITTTTTVTPG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q86SF2
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q8MM26
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q96FL9
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
ppGalNAc-T14: acceptors are mucin-derived peptides such as Muc2, Muc5AC, Muc7, Muc13
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptors: synthetic glycopeptides and peptides most of which contain sequences derived from the tandem repeat region of MUC2 mucin
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptor: asialo mucin, subcomponents of kappa-casein, asialo kappa-casein, agalacto kappa-casein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptor: deglycosylated bovine submaxillary mucin
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q8IUC8
ppGalNAc-T13: acceptors are mucin peptides, such as Muc1a', Muc5Ac and Muc7, forms a triplet Tn epitope, 3 consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, different substrate specificities of ppGalNAc-T1 and -T13
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
ppGaNTase-T1: EA2 peptide acceptor, interdependence of binding of UDP-GalNAc and acceptor substrate, enzyme undergoes a conformational change upon sugar binding, equilibrium between open and closed states may be used as a regulation mechanism of activity
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
GalNAc-T1: Asp-144 is the most important site for GalNAc recognition, primarily recognizes the UDP portion of UDP-GalNAc
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
substrate specificities of recombinant ppGalNAc-T1, -T2, -T3, -T4, -T6 and T9
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
octapeptide Val-Thr-Pro-Arg-Thr-Pro-Pro-Pro is the best substrate, threonine cannot be glycosylated without a carboxyl triprolyl sequence, the alpha-amino acid group of the threonine must be blocked, the nature of the group NH2-terminal to the threonine affects the kinetics of the reaction, one residue can be between the threonine and the triprolyl sequence
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
site-specific O-glycosylation by rGalNAc-T2 and -T4 is controlled by the primary sequence context and the position and structure of previously introduced O-glycans, acceptors: synthetic mucin-type peptides and glycopeptides derived from tandem repeat regions of MUC1, MUC2 and MUC4, minimum peptide length is required, which is larger for glycosylated substrates, concerted and sequential action of rGalNAc-T2 and -T4 fully glycosylates MUC1, but only partially MUC2 and MUC4 tandem repeat peptides
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptor specificity
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
rate of incorporation of GalNAc into Thr is significantly greater than into Ser residues, presence of 1-2 GalNAc-Thr moieties in the subtrate reduces enzyme activity, especially when Galbeta1-3GalNAc is present, O-glycosylation depends on both amino acid sequence and prior glycosylation of substrates, enzyme is selective in glycosylating peptides with the Pro-Thr-Thr-Thr-Pro-Ile-Ser-Thr sequence in that the preferred primary site is the third Thr from the N-terminal end
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
L-threonine specifically O-glycosylated in alpha-configuration, Thr-Pro-Pro-Pro-sequence requires a peptide length of five or more for significant acceptor activity
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
broad specificity, acceptors: unglycosylated protein acceptors, synthetic peptides, O-glycosylates threonine about 35times faster than serine, specificity is determined by the amino acids in the acceptor peptide segment and its accessibility, enzymatic active site interacts with an 8-amino acid long segment of the substrate, spanning 3 amino acids preceding and 4 amino acids following the reactive Thr or Ser
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
only UDP-GalNAc serves as sugar donor
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
only UDP-GalNAc serves as sugar donor
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
only UDP-GalNAc serves as sugar donor
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
only UDP-GalNAc serves as sugar donor
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptors: synthetic peptides
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptors: synthetic polypeptides with sequences identical or similar to those found in porcine mucin or human erythropoietin, acceptor substrate specificity is dependent on the amino acid sequence adjacent to serine and threonine residues, but it is more sensitive to the sequence adjacent to serine than to threonine
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptors: bovine submaxillary mucin core protein, myelin basic protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
O-glycosylation of the polypeptide, acceptor: porcine stomach mucin
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
GalNAc-T1 and -T3: strict specificity for UDP-GalNAc, GalNAc-T2: utilizes UDP-GalNAc and UDP-Gal
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptors: apomucin, kappa-casein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptors: apomucin, kappa-casein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptors: ovine and porcine apomucin, porcine mucin-like synthetic peptides
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptors: A1 protein, apofetuin, apoantifreeze glycoproteins, frequent glycosylation of the abundant serine plus threonine residues of mucins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q8MVS5
acceptors: substantial activity only with EA2 peptide, less active with IgAh peptide
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
O-glycosylating enzyme, acceptors: synthetic peptides in which the Thr-Pro-Pro-Pro sequence is varied
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
O-glycosylating enzyme, acceptors: synthetic peptides in which the Thr-Pro-Pro-Pro sequence is varied
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptor: SIV3 peptide
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptor: mucin2 derived fluorescein-conjugated peptide Pro-Thr-Thr-Thr-Pro-Leu-Lys, preferential sites of O-glycosylation by pp-GalNAc-T1, -T2, -T3 and -T4, of which each has a unique specificity
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q9R0C5
ppGaNTase-T1: acceptor is MUC5AC peptide, di-glycopeptide contains GalNAc at Thr-3 and -13, tri-glycopeptide an additional one at Ser-5
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptor: human MUC5AC peptide Thr-Thr-Ser-Ala-Pro-Thr-Thr-Ser
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q8MVS5
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q925R7
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptors: deglycosylated Cowper's gland, swine and human trachea mucins, tryptic peptides prepared from them, best substrates are fragments of incompletely deglycosylated mucin polypeptide chains
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
specifically transfers N-acetylgalactosamine from UDP-GalNAc to the hydroxyl group of threonine, no transferase activity towards serine-containing peptides, amino acid sequence adjacent to glycosylated Thr residues may influence the rate of glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
acceptors: human mucin Muc1 and Muc2 peptides, human chorionic gonadotropin-beta peptide, HIV-V3 peptides
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
3 GalNAc-transferases: GalNAc-T1, -T2 and -T3 with distinct but partly overlapping specificities, dependent on the primary sequence of the acceptor substrate, acceptors: peptides based on Muc1 tandem repeat, TAP24, Muc2, Muc5AC, erythropoietin, hCG-beta, HIVIIIBgp120, ovine submaxillary mucin fragment, peptide derived from fibronectin, GalNAc-T1, -T2 and -T3 react at different rates with individual sites in the Muc1 repeat
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q925R7
diversely regulated ppGaNTase family may play a role in the various processes governing development
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q8IUC8
ppGalNAc-T13: synthesis of O-glycan, specifically the Tn antigen in neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
key role in O-linked glycosylation, catalyzes first step in the assembly
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
GalNAc-T1 glycosylates unmodified polypeptides in vivo
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q86SF2
GalNAc-T7: functions as a follow-up enzyme in the initiation step of O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q86SF2
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q925R7
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q9R0C5
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
different enzyme activities are involved in the initiation of GalNAc O-glycosylation and these are differentially expressed in cells and organs
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
ppGalNAc-T14 may be involved in O-glycosylation in kidney, catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
GalNAc-T9 catalyzes O-glycosylation in brain
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
first step in biosynthesis of O-linked oligosaccharides in submaxillary gland
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
catalyzes in vivo glycosylation of both threonine and serine
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
initial step of mucin-type O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q9R0C5
O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
post-translational, initial reaction in O-linked oligosaccharide biosynthesis
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
post-translational, initial reaction in O-linked oligosaccharide biosynthesis
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
key role in overall control of O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
ppGalNAc-T2: initiation of O-glycosylation in the IgA1 hinge region
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
primary step in the production of mucin-type O-linked oligosaccharide groups in glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
primary step in the production of mucin-type O-linked oligosaccharide groups in glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
can participate in the biosynthesis of O-glycosylated parasite proteins exposed at the interface between Echinococcus granulosus and its hosts
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
O08912
initiates the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-alpha-1-O-Ser/Thr)
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
the enzyme is involved in the normal development of the brain through O-glycosylation of proteins in the neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q9HCQ5
the enzyme is involved in the normal development of the brain through O-glycosylation of proteins in the neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
glycosylates peptides containing a sequence of XTPXP or TTAAP most efficiently
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
transfers GalNAc to a broad range of substrate peptides, derived from human mucins and O-glycosylated parasite proteins, including acceptors containing only serine or only threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q07537
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q10473
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q10471
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q6WV17, Q6WV19
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q96FL9
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q8MVS5
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
usage of random peptide substrates, overview. Isozyme substrate specificities, amino acid residue enhancement factors for ppGalNAc T isozymes are obtained from random peptide substrates, detailed overview
product analysis by NMR and mass spectrometry
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
usage of random peptide substrates, overview. Isozyme substrate specificity, amino acid residue enhancement factors for the ppGalNAc T isozyme are obtained from random peptide substrates, detailed overview
product analysis by NMR and mass spectrometry
-
?
UDP-N-acetyl-D-galactosamine + PPAHGVTSAPG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PPDAATAAPLR
UDP + N-acetyl-D-galactosaminyl-PPDAATAAPLR
show the reaction diagram
-
i.e. EPO-T peptide
-
-
?
UDP-N-acetyl-D-galactosamine + PPETTAAPPTG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PPVVPFTPLPG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PRFQDSSSSKAPPPSLPSPSRL
UDP + N-actetyl-D-galactosaminylated PRFQDSSSSKAPPPSLPSPSRL
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PRFQDSSSSKAPPPSLPSPSRLPG
UDP + N-acetyl-D-galactosaminylated PRFQDSSSSKAPPPSLPSPSRLPG
show the reaction diagram
Q10471, Q10472, Q8N4A0
-
-
-
?
UDP-N-acetyl-D-galactosamine + PSPPITTTTTG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PSTPPTPSPSTPPTPSPS
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. IgAh
-
-
-
UDP-N-acetyl-D-galactosamine + PSTPPTPSPSTPPTPSPS
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. IgAh, low activity, enzyme form PGANT2
-
-
-
UDP-N-acetyl-D-galactosamine + PSTPPTPSPSTPPTPSPS
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. IgAh, low activity, enzyme form PGANT8
-
-
-
UDP-N-acetyl-D-galactosamine + PSTPPTPSPSTPPTPSPS
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. IgAh, very low activity, enzyme form PGANT3
-
-
-
UDP-N-acetyl-D-galactosamine + PTTDS-(O-GalNAc)T-TPAPTTK
UDP + ?
show the reaction diagram
-
38.7% of the activity with GTTPSPVPTTS-(O-GalNAc)T-TSAP
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDS-(O-GalNAc)T-TPAPTTK
UDP + ?
show the reaction diagram
-
4.5% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDS-(O-GalNAc)T-TPAPTTK
UDP + ?
show the reaction diagram
Q6YBY0
59.6% of the activity with GTTPSPVPTTS-(O-GalNAc)T-TSAP
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTT
UDP + ?
show the reaction diagram
Q10471, Q7Z4T8
i.e. EA2, about 25% of the activity with Muc1a, enzyme form pp-GalNAc-T15
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTT
UDP + ?
show the reaction diagram
Q10471, Q7Z4T8
i.e. EA2, about 35% of the activity with Muc5AC as substrate, enzyme form pp-GalNAc-T2
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
Q6YBY0
0.3% of the activity with GTTPSPVPTTS-(O-GalNAc)T-TSAP
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
-
74% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT2
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
enzyme form PGANT3
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
O88422
enzyme form ppGaNTase-T1, enzyme form ppGaNTase-T3, enzyme form ppGaNTase-T4, enzyme form ppGaNTase-T5
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. EA2, enzyme form PGANT4
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. EA2, enzyme form PGANT6
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. EA2, enzyme form PGANT8
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. EA2, glycosylation at threonines 7, 11, and 12, enzyme form PGANT1
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. EA2, high activity, glycosylation at threonines 7, 11, and 12, enzyme form PGANT1
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPISTTMVTPTPTPTC
UDP + N-actetyl-D-galactosaminylated PTTTPISTTMVTPTPTPTC
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPISTTTMVTPTPTPTC
UDP + N-acetyl-D-galactosaminylated PTTTPISTTTMVTPTPTPTC
show the reaction diagram
Q10471, Q10472, Q8N4A0
mucin derived substrate
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPITTTTTV
UDP + ?
show the reaction diagram
-
i.e. Muc2
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPITTTTTVTPTPTPTGTQT
UDP + ?
show the reaction diagram
Q10471, Q7Z4T8
i.e. Muc2, about 35% of the activity with Muc1a, enzyme form pp-GalNAc-T15
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPITTTTTVTPTPTPTGTQT
UDP + ?
show the reaction diagram
Q10471, Q7Z4T8
i.e. Muc2, about 95% of the activity with Muc5AC as substrate, enzyme form pp-GalNAc-T2
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPSPPITG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + QATEYEYLDYDFLPEC
UDP + N-acetyl-D-galactosaminylated QATEYEYLDYDFLPEC
show the reaction diagram
Q10471, Q10472, Q8N4A0
-
-
-
?
UDP-N-acetyl-D-galactosamine + rhodanese
UDP + N-acetyl-D-galactosaminyl-rhodanese
show the reaction diagram
-
reduced and carboxylmethylated bovine rhodanese, at a lower rate than with myelin basic protein
-
-
?
UDP-N-acetyl-D-galactosamine + RPAPGSTAPPA
UDP + N-acetyl-D-galactosaminylated RPAPGSTAPPA
show the reaction diagram
Q10471, Q10472, Q8N4A0
-
-
-
?
UDP-N-acetyl-D-galactosamine + SATTPAPPSSG
UDP + ?
show the reaction diagram
-
preferred substrate
-
-
?
UDP-N-acetyl-D-galactosamine + SDAESSGPVPG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + SEVTTTLVPAG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + SPTTSTPISSTPQPTS
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. rMUC-2, enzyme form PGANT2
-
-
-
UDP-N-acetyl-D-galactosamine + SPTTSTPISSTPQPTS
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. rMUC-2, enzyme form PGANT4
-
-
-
UDP-N-acetyl-D-galactosamine + SPTTSTPISSTPQPTS
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. rMUC-2, high activity
-
-
-
UDP-N-acetyl-D-galactosamine + SPTTSTPISSTPQPTS
UDP + ?
show the reaction diagram
Q6WV16, Q6WV17, Q6WV19, Q6WV20, Q8IA42, Q8MW48, Q9Y117
i.e. rMUC-2, low activity. enzyme form PGANT6
-
-
-
UDP-N-acetyl-D-galactosamine + STPSTPSTPSTPSTP
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + subtilisin
UDP + N-acetyl-D-galactosaminyl-subtilisin
show the reaction diagram
-
reduced and carboxylmethylated bacterial subtilisin, at a lower rate than with myelin basic protein or bovine rhodanese
-
-
?
UDP-N-acetyl-D-galactosamine + SVLVLTTVSVPPSPASAGPSV
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + syndecan-3
UDP + N-acetyl-D-galactosaminyl-syndecan-3
show the reaction diagram
Q8IUC8
syndecan-3 may be a natural substrate for GalNAc-T13
-
-
?
UDP-N-acetyl-D-galactosamine + TAPPAHGVTSAPDTRPAPGSTAPP
UDP + N-acetyl-D-galactosaminylated TAPPAHGVTSAPDTRPAPGSTAPP
show the reaction diagram
Q10471, Q10472, Q8N4A0
-
-
-
?
UDP-N-acetyl-D-galactosamine + TAPPAHGVTSAPDTRPAPGSTAPP
UDP + N-acetyl-D-galactosaminylated TAPPAHGVTSAPDTRPAPGSTAPP
show the reaction diagram
Q10471, Q10472, Q8N4A0
acceptor substrate
-
-
?
UDP-N-acetyl-D-galactosamine + TSAPGTTPSPG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + TTAAPPTPSAG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + TTPLPTTTPSG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + TTSTTSAPGTG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + TTTTTTPKPTG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + TTTVTPTPTPG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + TVPVTGPTAPALVQSVTPPT
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + VESDRSTTTTQAP
UDP + ?
show the reaction diagram
Q6YBY0
0.3% of the activity with GTTPSPVPTTS-(O-GalNAc)T-TSAP
-
-
?
UDP-N-acetyl-D-galactosamine + VESDRSTTTTQAP
UDP + ?
show the reaction diagram
-
34% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
-
-
?
UDP-N-acetyl-D-galactosamine + VLTTTATTPTA
UDP + ?
show the reaction diagram
-
i.e. Muc5B
-
-
?
UDP-N-acetyl-D-galactosamine + VPETASSKTATGDSFS
UDP + ?
show the reaction diagram
-
-
-
-
?
IgA hinge-4GalNAc + UDP-GalNAc
IgA hinge-nGalNAc + UDP
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
Q86SF2
GalNAc-T7: no activity with non-glycosylated peptides and GalNAc-glycosylated Muc1 substrate
-
-
-
additional information
?
-
-
not: lacto-N-fucopentaose I, ceramide dihexosides, ceramide trihexosides, globoside
-
-
-
additional information
?
-
-
contains a lectin-like repeat sequence at the C-terminus, role of GalNAc-T1 lectin domain, which is involved in glycosylation of substrates with multiple acceptor sites
-
-
-
additional information
?
-
-
different substrate specificities before and after Muc2 affinity chromatography of enzyme
-
-
-
additional information
?
-
Q8MVS5
519-amino acid putative catalytic region
-
-
-
additional information
?
-
-
multiple enzyme isoforms
-
-
-
additional information
?
-
Q86SF2
multiple enzyme isoforms
-
-
-
additional information
?
-
-
multiple enzyme isoforms
-
-
-
additional information
?
-
Q8IUC8
multiple enzyme isoforms
-
-
-
additional information
?
-
-
multiple enzyme isoforms
-
-
-
additional information
?
-
Q925R7
multiple enzyme isoforms
-
-
-
additional information
?
-
Q9R0C5
multiple enzyme isoforms
-
-
-
additional information
?
-
-
not: UDP-glucuronate, UDP-xylose, GDP-mannose, GDP-fucose, intact mucins, desialylated mucins, glycolipid acceptors, including globoside and ceramide hexosides, no transfer of GalNAc to terminal sugar residues in oligosaccharide chains
-
-
-
additional information
?
-
-
14 distinct isoforms different with regard to their expression and specificity, but overlaps also occur, ppGalNAc-T14 forms together with ppGalNAc-T2 a subfamily of ppGalNAc-T gene family
-
-
-
additional information
?
-
Q9R0C5
ppGaNTase-T6: no activity with unglycosylated peptides
-
-
-
additional information
?
-
-
all known rGalNAc-Ts are characterized by a putative lectin domain in their C-terminal regions
-
-
-
additional information
?
-
Q925R7
9 isoforms, ppGaNTase-T9 contains a 480-amino acid conserved region and shows no activity with non-glycosylated peptides
-
-
-
additional information
?
-
-
not: UDP-Glc
-
-
-
additional information
?
-
-
not: bovine cytochrome c
-
-
-
additional information
?
-
-
GalNAc-T9 contains a 485-amino acid putative catalytic region, GalNAc-T1, -T2, -T4 and -T8 belongs to the housekeeping enzymes with ubiquitous expression, GalNAc-T3, -T5, -T6, -T7 and -T9 belongs to the tissue-specific enzymes
-
-
-
additional information
?
-
-
existence of multiple enzyme activities, differentially expressed in different organs, at least 2 distinct enzyme specificities
-
-
-
additional information
?
-
-
enzyme structure, GT1 motif, DXD motif, Gal/GalNAc-T motif
-
-
-
additional information
?
-
-
at least 11 human ppGalNAc-Ts
-
-
-
additional information
?
-
-
not: UDP-GlcNAc
-
-
-
additional information
?
-
-
not: UDP-GlcNAc
-
-
-
additional information
?
-
-
not: UDP-GlcNAc
-
-
-
additional information
?
-
-
not: UDP-Gal
-
-
-
additional information
?
-
-
not: UDP-Gal
-
-
-
additional information
?
-
-
not: alphaS1-casein, alphaS2-casein, beta-casein, alpha-lactalbumin, beta-lactoglobulin, bovine serum albumin
-
-
-
additional information
?
-
Q86SF2
amino acid sequences of seven GalNAc-transferases
-
-
-
additional information
?
-
-
amino acid sequences of seven GalNAc-transferases
-
-
-
additional information
?
-
Q8MVS5
involved in development, necessary for viability
-
-
-
additional information
?
-
Q8IUC8
pp-GalNAc-T13 is specifically expressed in neurons and synthesizes Tn antigen
-
-
-
additional information
?
-
Q10471, Q10472, Q8N4A0, Q8NCW6
MUC1-2GalNAc, MUC2-6GalNAc, OSM fragments, hCG-beta are not substrates for GalNAc-T11
-
-
-
additional information
?
-
Q10471, Q10472, Q8N4A0, Q8NCW6
MUC1b' and hCG-beta are no substrates for GalNAc-T1
-
-
-
additional information
?
-
-
UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase catalyzes the first step in the mucin-type O-glycan biosynthesis pathway by transferring GalNAc to Ser or Thr residues in a protein from the sugar donor UDP-GalNAc
-
-
-
additional information
?
-
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases transfer GalNAc from UDP-GalNAc to the Ser and Thr residues of polypeptide acceptors, and initiate and regulate mucin-type O-glycosylation
-
-
-
additional information
?
-
-
most active with partially glycosylated MUC5AC (by a combination of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 and UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2), no activity observed with substrate peptides of other UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases
-
-
-
additional information
?
-
Q58A54
no activity toward classical substrates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-galactosamine + bone sialoprotein
UDP + UDP-N-acetyl-D-galactosaminyl-bone sialoprotein
show the reaction diagram
-
preferred substrate of isozyme ppGalNAcT-1, glycosylation of Thr101, Ser131, Thr199, and Ser214, glycosylation pattern, overview
-
-
?
UDP-N-acetyl-D-galactosamine + fibronectin
UDP + N-acetyl-D-galactosaminyl-fibronectin
show the reaction diagram
-
fibronectin is a physiological substrate for GalNAc-T3
-
-
?
UDP-N-acetyl-D-galactosamine + kappa-casein
UDP + N-acetyl-D-galactosaminyl-kappa-casein
show the reaction diagram
-
glycosylation of kappa-casein occurs after casein micelle formation triggered by the accumulation of Ca2+ in vivo
-
-
?
UDP-N-acetyl-D-galactosamine + osteopontin
UDP + N-acetyl-D-galactosaminyl-osteopontin
show the reaction diagram
-
preferred substrate of isozyme ppGalNAcT-1, glycosylation pattern, overview
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q925R7
diversely regulated ppGaNTase family may play a role in the various processes governing development
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q8IUC8
ppGalNAc-T13: synthesis of O-glycan, specifically the Tn antigen in neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
key role in O-linked glycosylation, catalyzes first step in the assembly
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
GalNAc-T1 glycosylates unmodified polypeptides in vivo
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q86SF2
GalNAc-T7: functions as a follow-up enzyme in the initiation step of O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q86SF2
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q925R7
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q9R0C5
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
different enzyme activities are involved in the initiation of GalNAc O-glycosylation and these are differentially expressed in cells and organs
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
ppGalNAc-T14 may be involved in O-glycosylation in kidney, catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
GalNAc-T9 catalyzes O-glycosylation in brain
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
first step in biosynthesis of O-linked oligosaccharides in submaxillary gland
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
catalyzes in vivo glycosylation of both threonine and serine
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
initial step of mucin-type O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q9R0C5
O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
post-translational, initial reaction in O-linked oligosaccharide biosynthesis
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
post-translational, initial reaction in O-linked oligosaccharide biosynthesis
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
key role in overall control of O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
ppGalNAc-T2: initiation of O-glycosylation in the IgA1 hinge region
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
primary step in the production of mucin-type O-linked oligosaccharide groups in glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
primary step in the production of mucin-type O-linked oligosaccharide groups in glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
can participate in the biosynthesis of O-glycosylated parasite proteins exposed at the interface between Echinococcus granulosus and its hosts
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
O08912
initiates the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-alpha-1-O-Ser/Thr)
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
the enzyme is involved in the normal development of the brain through O-glycosylation of proteins in the neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q9HCQ5
the enzyme is involved in the normal development of the brain through O-glycosylation of proteins in the neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
-
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q07537
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q10473
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q10471, Q10472, Q8N4A0, Q8NCW6
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q10471
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q6WV17, Q6WV19
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q96FL9
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
Q8MVS5
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + syndecan-3
UDP + N-acetyl-D-galactosaminyl-syndecan-3
show the reaction diagram
Q8IUC8
syndecan-3 may be a natural substrate for GalNAc-T13
-
-
?
additional information
?
-
Q8MVS5
involved in development, necessary for viability
-
-
-
additional information
?
-
Q8IUC8
pp-GalNAc-T13 is specifically expressed in neurons and synthesizes Tn antigen
-
-
-
additional information
?
-
-
UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase catalyzes the first step in the mucin-type O-glycan biosynthesis pathway by transferring GalNAc to Ser or Thr residues in a protein from the sugar donor UDP-GalNAc
-
-
-
additional information
?
-
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases transfer GalNAc from UDP-GalNAc to the Ser and Thr residues of polypeptide acceptors, and initiate and regulate mucin-type O-glycosylation
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
stimulates to a smaller extent than Mn2+
Ca2+
-
stimulates to a smaller extent than Mn2+
Ca2+
-
10 mM, 5.4fold activation
Cd2+
-
less stimulation than by Mn2+
Cd2+
-
partially restores activity after EDTA treatment
Co2+
-
less stimulation than by Mn2+
Co2+
-
less stimulation than by Mn2+
Co2+
-
almost as effective as Mn2+, restores activity after EDTA treatment
Co2+
-
10 mM, 5.9fold activation
Co2+
-
enhances activity with 60% of the activation observed with Mn2+
Cu2+
-
less stimulation than by Mn2+
Cu2+
-
less stimulation than by Mn2+
Cu2+
-
10 mM, 11.4fold activation, recombinant protein lacking the trans-membrane domain shows maximal activity in presence of Cu2+
Mg2+
-
stimulates to a smaller extent than Mn2+
Mg2+
-
10 mM, 6.4fold activation
Mn2+
-
most effective cation; requirement
Mn2+
-
requirement; strong stimulation, maximal activity at 4-10 mM
Mn2+
-
metal-free enzyme is inactive, Mn2+ is the best activator, maximal activity at 5 mM, half-maximal activity at 0.4 mM MnCl2, 20 and 100 mM result in 10% and 80% inhibition
Mn2+
-
requirement
Mn2+
-
maximal activity at 2.5 mM, restores activity after EDTA treatment; most effective cation; requirement
Mn2+
-
maximal activity at 10 mM; requirement
Mn2+
-
maximal activity at 5-7.5 mM, higher concentrations are inhibitory; requirement
Mn2+
-
Mn2+ cannot be replaced by Mg2+ or Ca2+; requirement
Mn2+
-
requirement
Mn2+
-
essential for donor substrate binding
Mn2+
-
10 mM, 7fold activation
Mn2+
-
most efficiently enhances activity among divalent cations tested
Mn2+
O08912
ion complexed by invariant D209 and H211 of the DXH motif and by invariant H344
Mn2+
-
in coordination both with the phosphates of UDP and the DXH motif of the enzyme
Mn2+
Q6WV17, Q6WV19
10 mM MnCl2; 10 mM MnCl2
Mn2+
Q10471
hydrated by a single water molecule in the presence of UDP-GalNAc or UDP-GalNAc and peptide
Ni2+
-
less stimulation than by Mn2+
Ni2+
-
partially restores activity after EDTA treatment
Ni2+
-
10 mM, 6.1fold activation
Ni2+
-
enhances activity with 20% of the activation observed with Mn2+
Zn2+
-
stimulates to a smaller extent than Mn2+
Zn2+
-
10 mM, 5.7fold activation
Mn2+
-
-
additional information
-
no reactivation of metal-free enzyme by Mg2+, Zn2+ and Ca2+
additional information
-
not activated by Mg2+ or Ca2+
additional information
-
metal-dependent enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
weak
alphaS1-casein
-
strong inhibition of GalNAc transfer to kappa-casein, reversed by Ca2+
-
AMP
-
-
ATP
-
weak
benzyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
;
benzyl-N-acetyl-alpha-D-galactosaminide
-
benzyl-GalNAc, 2 mM over night in Hek293T cell culture, abolishes activity of transiently transfected xGalntl-1 in Hek293T cells like inhibition of Smad2 phosphorylation by ActR-IIB and induction of a migration shift of ActR-IIB and Alk-3
CDP
-
-
CMP
-
-
CTP
-
-
D-galactose
Q10471, Q10472, Q8N4A0, Q8NCW6
-
diethyldicarbonate
-
binds to His; hydroxylamine partiallly protects, UDP-GalNAc protects
EDTA
-
10 mM, complete inhibition
EDTA
-
0.5 mM, complete inhibition
EDTA
-
Na2EDTA, 7.5 mM, complete inhibition
EDTA
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-T4 enzyme and lectin domain; inhibition of GalNAc-T2 enzyme and lectin domain
fully GalNAc-substituted MUC1 repeat peptide
-
inhibits activity of rGalNAc-T4 and -T2
-
GalNAc
-
inhibition of GalNAc-T1 by free GalNAc: follow-up O-glycosylation of apomucin is sensitive, O-glycosylation of synthetic peptides containing a single glycosylation site is resistant
GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
inhibition for GalNAc-T2 lectin domain to bind GalNAc-MUC1; inhibition for GalNAc-T4 lectin domain to bind GalNAc-MUC1
GDP
-
weak
GMP
-
-
GTP
-
-
Helix pomatia lectin
-
-
-
HIV-V3
-
competitive inhibition of Muc2 glycosylation
-
methyl-alpha-Gal
Q10471, Q10472, Q8N4A0, Q8NCW6
-
methyl-beta-Gal
Q10471, Q10472, Q8N4A0, Q8NCW6
-
Mn2+
-
Mn2+ is the best activator, maximal activity at 5 mM, 20 and 100 mM result in 10% and 80% inhibition
Muc2
-
competitive inhibition of HIV-V3 peptide glycosylation
-
o-nitrophenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
;
o-nitrophenyl-beta-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
;
p-Chloromercuriphenylsulfonic acid
-
irreversible
p-nitrophenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
;
p-nitrophenyl-beta-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
;
phenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
;
Soybean lectin
-
-
-
UDP
-
competitive
UDP
-
strong
UDP
-
competitive
UDP
-
competitive
UDP-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
;
UMP
-
uncompetitive
UMP
-
-
UMP
-
uncompetitive
UMP-1-hexadecanesulfonic anhydride
-
50% inhibition at 0.16 mM, competitive
UMP-1-octanesulfonic anhydride
-
-
UMP-butanesulfonic anhydride
-
-
UTP
-
competitive
UTP
-
-
Mn2+
-
at higher concentrations, 30 mM: 50% inhibition
additional information
-
not inhibited by ATP, CDP, GDP
-
additional information
-
not inhibited by wheat germ lectin
-
additional information
-
not inhibited by UTP
-
additional information
-
elongation of GalNAc by beta3-galactosylation inhibits rGalNAc-T4 activity completely and rGalNAc-T2 activity with respect to the acceptor site GSTA, not inhibited by GlcNAc
-
additional information
-
GalNAc-T1: follow-up glycosylation is inhibited by addition of beta1,3Gal to GalNAc, apomucin glycosylation is not inhibited by galactose, glucose, N-acetylglucosamine, mannose and fucose
-
additional information
-
-
-
additional information
Q10471, Q10472, Q8N4A0, Q8NCW6
benzyl or phenyl alpha and beta-GalNAc compounds show higher inhibition for GalNAc-T2 to bind GalNAc-MUC1 than for isoform GalNAc-T4. No inhibition of GalNAc-T2 enzyme and lectin domain by glucose, GlcNAc or mannose; benzyl or phenyl alpha and beta-GalNAc compounds show weaker inhibition for GalNAc-T4 to bind GalNAc-MUC1 than for isoform GalNAc-T2. No inhibition of GalNAc-T4 enzyme and lectin domain by glucose, GlcNAc or mannose
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
-
required for maximal activity
Triton X-100
-
required for maximal activity
Triton X-100
-
0.1% w/v; required for maximal activity
DTT
-
activates, especially after storage
additional information
Q86SF2
GalNAc-T7: selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human Muc2 and rat submaxillary gland mucin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
Ac-Asn-Leu-Thr-Pro-Pro-Pro
-
-
1.3
Ac-Pro-Thr-Thr-Thr
-
derived from the bovine myelin basic protein sequence
-
1.3
Ac-Pro-Thr-Thr-Thr-Pro-Ile-Ser-Thr-NH2
-
derived from the MUC2 repeat sequence
-
1.33
Ac-Thr-Pro-Pro-Pro
-
-
3.7
Ac-TPPA
-
-
0.45
AHGVVTSAPDTR
Q10471, Q7Z4T8
pH 7.4, 37C, enzyme form pp-GalNAc-T2
0.24
AQPTPPP
-
-
0.4
Arg-Thr-Pro-Pro-Pro
-
-
3.3
Arg-Thr-Pro-Pro-Pro
-
derived from the major acceptor sequence in myelin basic protein
14.9
Asp-Ala-Ala-Ser-Ala-Ala-Pro-Leu
-
-
0.01
CPPTPSATTPAPPSSSAPPETTAA
Q8N4A0
-
0.015
CPPTPSATTPAPPSSSAPPETTAA
Q8N4A0
-
0.04
CPPTPSATTPAPPSSSAPPETTAA
Q8N4A0
-
0.48
CPPTPSATTPAPPSSSAPPETTAA
Q8N4A0
-
0.0175
deglycosylated human trachea mucin
-
-
-
0.0141
deglycosylated swine trachea mucin
-
-
-
0.07
DSTTPAPTTK
Q8N4A0
-
0.46
DSTTPAPTTK
Q8N4A0
-
0.85
DSTTPAPTTK
Q8N4A0
-
2.19
DSTTPAPTTK
Q8N4A0
-
0.595
EA2 peptide
Q8MVS5
-
-
39.5
Gln-Ala-Ala-Gly-Thr-Ser-Gly-Ala-Gly-Pro-Gly
-
-
0.8
Gly-Val-Val-Pro-Thr-Val-Val-Pro-Gly
-
GalNAc-T1
0.0209
GTTPSPVPTTS-(O-GalNAc)T-SAP
-
pH 7.0, 37C
0.0721
GTTPSPVPTTS-(O-GalNAc)T-SAP
-
pH 7.0, 37C
0.0259
GTTPSPVPTTSTTSAP
-
pH 7.0, 37C
0.067
GTTPSPVPTTSTTSAP
-
pH not specified in the publication, 37C
0.111
GTTPSPVPTTSTTSAP
-
pH not specified in the publication, 37C
0.171
GTTPSPVPTTSTTSAP
-
pH not specified in the publication, 37C
0.344
GTTPSPVPTTSTTSAP
-
pH not specified in the publication, 37C
0.115
GTTPSPVPTTST[GalNAc]TSAP
-
pH not specified in the publication, 37C
0.13
GTTPSPVPTTST[GalNAc]TSAP
-
pH not specified in the publication, 37C
0.353
GTTPSPVPTTST[GalNAc]TSAP
-
pH not specified in the publication, 37C
0.46
GTTPSPVPTTST[GalNAc]TSAP
-
pH not specified in the publication, 37C
0.035
GT[GalNAc]TPSPVPTTSTTSAP
-
pH not specified in the publication, 37C
-
0.263
GT[GalNAc]TPSPVPTTSTTSAP
-
pH not specified in the publication, 37C
-
0.299
GT[GalNAc]TPSPVPTTSTTSAP
-
pH not specified in the publication, 37C
-
0.206
GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
-
pH not specified in the publication, 37C
1.74
GVVPTVVPG
Q10473
+/-0.3 mM, truncated wild-type P-T1/delta42
16
GVVPTVVPG
Q10473
+/-0.3 mM, mutant W316Y, 9.2 times higher than wild-type
17.6
GVVPTVVPG
Q10473
+/-0.5 mM, mutant W316F, 10.1 times higher than wild-type
0.5
HIV-V3 peptide
-
-
-
0.23
human mucin Muc2 peptide
-
-
-
0.01
IgA hinge
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.01 mM, mutant GalNAc-T2-D541A, pH7.4
-
0.015
IgA hinge
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.002 mM, pH7.4
-
0.02
IgA hinge
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.005 mM, mutant GalNAc-T2-D458H, pH7.4
-
0.12
IgA hinge-4GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.01 mM, pH7.4
-
0.32
IgA hinge-4GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.09 mM, mutant GalNAc-T2-D541A, pH7.4
-
0.15
MUC1
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.03 mM, mutant GalNAc-T2-D541A, pH7.4
-
0.26
MUC1
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.16 mM, pH7.4
-
0.36
MUC1
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.19mM, mutant GalNAc-T2-D458H, pH7.4
-
0.86
MUC1-2GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.21 mM, mutant GalNAc-T2-D541A, pH7.4
0.87
MUC1-2GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.23 mM, pH7.4
0.07
Muc1a' peptide
Q8IUC8
ppGalNac-T9
-
0.11
Muc1a' peptide
Q8IUC8
ppGalNac-T13
-
0.23
Muc1a' peptide
Q8IUC8
ppGalNac-T1
-
0.01
Muc2
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.001 mM, pH7.4
-
0.018
Muc2
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.003 mM, mutant GalNAc-T2-D541A, pH7.4
-
0.25
Muc2
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.006 mM, mutant GalNAc-T2-D458H, pH7.4
-
0.062
MUC2-6GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.007 mM, pH7.4
-
0.066
MUC2-6GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.010 mM, mutant GalNAc-T2-D541A, pH7.4
-
0.018
MUC5AC
-
at site Thr-9, hT2CD
0.02
MUC5AC
-
at site Thr-9, hT2
0.018
MUC5AC-13
-
at site Thr-3, hT2
0.17
MUC5AC-13
-
at site Thr-9, hT2CD
0.53
MUC5AC-13
-
at site Thr-12, hT10
0.64
MUC5AC-13
-
at site Thr-12, hT10CD-hT2LD
0.77
MUC5AC-13
-
at site Thr-12, hT10CD
0.033
MUC5AC-3
-
at site Thr-13, hT2
0.036
MUC5AC-3
-
at site Thr-9, hT2CD
0.05
MUC5AC-3
-
at site Thr-2, hT10CD
0.096
MUC5AC-3
-
at site Thr-2, hT10
0.107
MUC5AC-3
-
at site Thr-2, hT10CD-hT2LD
0.44
MUC5AC-3,13
-
at sites Thr-2 and Thr12, hT10
0.57
MUC5AC-3,13
-
at sites Thr-2 and Thr12, hT10CD-hT2LD
1
MUC5AC-3,13
-
at sites Thr-2 and Thr12, hT10CD
2.4
MUC5AC-9
-
at site Thr-2, hT10
0.02
Muc7 peptide
Q8IUC8
ppGalNac-T9
-
0.046
Muc7 peptide
Q8IUC8
ppGalNac-T13
-
0.054
Muc7 peptide
Q8IUC8
ppGalNac-T1
-
0.4
myelin basic protein
-
-
-
0.25
N-acetyl-4-benzoyl-L-Phe-L-Pro-L-Tyr-L-Pro-L-Pro-L-Pro-NH2
-
-
0.3
N-acetyl-4-benzoyl-L-Phe-L-Pro-L-Tyr-L-Pro-L-Pro-L-Pro-NH2
-
-
0.35
PPDAATAAPL
Q10473
+/-0.05 mM, truncated wild-type P-T1/delta42
13.5
PPDAATAAPL
Q10473
+/-0.7 mM, mutant W316Y, 38.5 times higher than wild-type
15.6
PPDAATAAPL
Q10473
+/-0.6 mM, mutant W316F, 44.6 times higher than wild-type
6
Pro-Pro-Ala-Ser-Thr-Ser-Ala-Pro-Gly
-
-
-
6.5
Pro-Pro-Ala-Ser-Thr-Ser-Ala-Pro-Gly
-
-
-
3.6
Pro-Pro-Asp-Ala-Ala-Ser-Ala-Ala-Pro-Leu-Arg
-
-
4.5
Pro-Pro-Asp-Ala-Ala-Ser-Ala-Ala-Pro-Leu-Arg
-
-
0.2
Pro-Pro-Asp-Ala-Ala-Thr-Ala-Ala-Pro-Leu
-
GalNAc-T1
-
18
Pro-Pro-Asp-Ala-Ser-Ser-Ser-Ala-Pro-Leu-Arg
-
-
12.9
Pro-Pro-Asp-Val-Val-Ser-Val-Val-Pro-Leu-Arg
-
-
0.52
Pro-Thr-Ala-Pro-Pro-Pro
-
-
0.1058
PTTDS-(O-GalNAc)T-TPAPTTK
-
pH 7.0, 37C
0.182
PTTDS-(O-GalNAc)T-TPAPTTK
-
pH 7.0, 37C
0.198
PTTDS-(O-GalNAc)T-TPAPTTK
-
pH 7.0, 37C
0.042
PTTDSTTPAPTTK
O88422
enzyme form ppGaNTase-1
0.108
PTTDSTTPAPTTK
-
pH not specified in the publication, 37C
0.113
PTTDSTTPAPTTK
O88422
enzyme form ppGaNTase-T5
0.124
PTTDSTTPAPTTK
-
pH not specified in the publication, 37C
0.172
PTTDSTTPAPTTK
-
pH not specified in the publication, 37C
0.229
PTTDSTTPAPTTK
O88422
enzyme form ppGaNTase-3
1.02
PTTDSTTPAPTTK
O88422
enzyme form ppGaNTase-T4
1.33
SDC106 peptide
Q8IUC8
derived from human syndecan-3, ppGalNac-T13
-
0.63
SDC155
Q8IUC8
derived from human syndecan-3, ppGalNac-T13
-
0.38
SDC165 peptide
Q8IUC8
derived from human syndecan-3, ppGalNac-T13
-
0.07
SDC284 peptide
Q8IUC8
derived from human syndecan-3, ppGalNac-T13
-
0.19
SDC284 peptide
Q8IUC8
derived from human syndecan-3, ppGalNac-T1
-
0.96
SDC284 peptide
Q8IUC8
derived from human syndecan-3, ppGalNac-T9
-
0.2
STPSTPSTPSTPSTP
-
pH 6.5, 37C, mutant enzyme W129R
0.205
STPSTPSTPSTPSTP
-
pH 6.5, 37C, mutant enzyme W129F
0.25
STPSTPSTPSTPSTP
-
pH 6.5, 37C, wild-type enzyme
0.41
STPSTPSTPSTPSTP
-
pH 6.5, 37C, mutant enzyme N126A
0.65
STPSTPSTPSTPSTP
-
pH 6.5, 37C, mutant enzyme W129A
0.027
UDP-Gal
-
GalNAc-T2
0.03
UDP-Gal
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.002 mM, pH7.4
0.036
UDP-Gal
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.001 mM, mutant GalNAc-T2-D458H, pH7.4
0.041
UDP-Gal
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.005 mM, mutant GalNAc-T2-D541A, pH7.4
0.0017
UDP-GalNAc
-
-
0.006
UDP-GalNAc
-
ovine apomucin
0.0063
UDP-GalNAc
-
-
0.008
UDP-GalNAc
-
-
0.01
UDP-GalNAc
-
GalNAc-T2
0.01
UDP-GalNAc
Q8N4A0
-
0.011
UDP-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.002 mM, pH7.4
0.013
UDP-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.001 mM, mutant GalNAc-T2-D541A, pH7.4
0.0162
UDP-GalNAc
-
-
0.02
UDP-GalNAc
Q8MVS5
-
0.029
UDP-GalNAc
-
GalNAc-T3
0.029
UDP-GalNAc
Q8N4A0
-
0.03
UDP-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.001 mM, mutant GalNAc-T2-D458H, pH7.4
0.0417
UDP-GalNAc
-
-
0.06
UDP-GalNAc
-
-
0.062
UDP-GalNAc
-
GalNAc-T1
0.062
UDP-GalNAc
Q8N4A0
-
0.11
UDP-GalNAc
-
-
0.16
UDP-GalNAc
Q8N4A0
determination of Km for UDP-GalNAc is performed with saturating concentration of CPPTPSATTPAPPSSSAPPETTAA as substrate. No incorporation is found with UDP-Gal or UDP-GlcNAc
3.6
UDP-GalNAc
-
GalNac-T1 mutant N465A
4
UDP-GalNAc
-
GalNac-T1 mutant G455Q
4.4
UDP-GalNAc
-
GalNac-T1 triple mutant D444A/D484A/D525A
5.1
UDP-GalNAc
-
GalNac-T1 mutants D444A and P-deltaN42
5.1
UDP-GalNAc
Q10473
+/-0.8 mM, truncated wild-type P-T1/delta42
5.2
UDP-GalNAc
Q10473
+/-0.1 mM, mutant Y302L
5.4
UDP-GalNAc
-
GalNac-T1 mutant F457A
6.1
UDP-GalNAc
-
GalNac-T1 mutant Q466A
6.2
UDP-GalNAc
Q10473
+/-0.6 mM, mutant F325L, 1.2 times higher than wild-type
9
UDP-GalNAc
Q10473
+/-0.1 mM, mutant W316Y, 1.8 times higher than wild-type
9.1
UDP-GalNAc
Q10473
+/-0.7 mM, mutant W316F, 1.8 times higher than wild-type
14.2
UDP-GalNAc
Q10473
+/-1.1 mM, mutant F303L, 2.8 times higher than wild-type
16
UDP-GalNAc
Q10473
+/-0.3 mM, mutant Y309L, 3.2 times higher than wild-type
0.008
UDP-N-acetyl-D-galactosamine
-
pH 6.5, 37C, wild-type enzyme
0.0107
UDP-N-acetyl-D-galactosamine
-
pH 7.2, 25C
0.014
UDP-N-acetyl-D-galactosamine
-
pH 6.5, 37C, mutant enzyme W129F
0.0141
UDP-N-acetyl-D-galactosamine
-
pH 7.0, 37C
0.016
UDP-N-acetyl-D-galactosamine
Q10471, Q7Z4T8
pH 7.4, 37C, enzyme form pp-GalNAc-T15
0.017
UDP-N-acetyl-D-galactosamine
-
pH 6.5, 37C, mutant enzyme W129R
0.029
UDP-N-acetyl-D-galactosamine
-
pH 6.5, 37C, mutant enzyme W129A
0.044
UDP-N-acetyl-D-galactosamine
-
pH 7.0, 37C
0.044
UDP-N-acetyl-D-galactosamine
-
pH 6.5, 37C, mutant enzyme N126A
0.0788
UDP-N-acetyl-D-galactosamine
-
pH 7.0, 37C
0.081
UDP-N-acetyl-D-galactosamine
Q10471, Q7Z4T8
pH 7.4, 37C, enzyme form pp-GalNAc-T2
14
Val-Leu-Gly-Ala-Thr-Ala-Val
-
-
8.3
Val-Leu-Gly-Thr-Ala-Ala-Val
-
-
18.6
Val-Leu-Gly-Thr-Thr-Ala-Val
-
-
7.2
Val-Lys-Thr-Glu-Ala-Thr-Thr-Phe-Ile
-
-
3
Val-Thr-Pro-Arg-Thr-Pro-Pro-Pro
-
-
0.91
AHGVVTSAPDTR
Q10471, Q7Z4T8
pH 7.4, 37C, enzyme form pp-GalNAc-T15
additional information
apomucin
Q10473
13.6 +/-1.9 mg/ml, mutant F303L, 2.8 times higher than wild-type; 17.4 +/-3.6 mg/ml, mutant W316Y, 3.6 times higher than wild-type; 43.9 +/-3.8 mg/ml, mutant W316F, 9.1 times higher than wild-type; 4.7 +/-0.1 mg/ml, truncated wild-type P-T1/delta42; 5.0 +/-0.2 mg/ml, mutant Y302L; 6.7 +/-1.7 mg/ml, mutant F325L, 1.4 times higher than wild-type; 7.1 +/-0.4 mg/ml, mutant Y309L, 1.5 times higher than wild-type
-
0.332
GT[GalNAc]TPSPVPTTSTTSAP
-
pH not specified in the publication, 37C
-
additional information
GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
-
KM >2 mM
0.81
IgA hinge-4GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-0.2 mM, mutant GalNAc-T2-D458H, pH7.4
-
additional information
additional information
-
Km: 0.192 mg/ml: apomucin, 1.15 mg/ml: kappa-subcomponent 1, 5.1 mg/ml: kappa-subcomponent 7
-
additional information
additional information
-
-
-
additional information
additional information
-
Km: 1.01 mg/ml: ovine apomucin, 2.54 mg/ml: porcine apomucin
-
additional information
additional information
-
Km: 2.5 mg/ml: deglycosylated bovine submaxillary mucin
-
additional information
additional information
-
-
-
additional information
additional information
-
effect of substrate glycosylation and amino acid substitution of glycopeptides on Km-values and enzyme activity
-
additional information
additional information
-
Km: 0.83 mg/ml: deglycosylated Cowper's gland mucin, 1.12 mg/ml: deglycosylated human trachea mucin, 0.94 mg/ml: deglycosylated swine trachea mucin, values for several tryptic peptides derived from them
-
additional information
additional information
-
values for different human mucin Muc1 peptides
-
additional information
additional information
-
-
-
additional information
additional information
-
values for GalNAc-T1, -T2 and -T3 for different substrate peptides
-
additional information
additional information
-
increased values, mg/ml, for apomucin of several GalNAc-T1 mutants
-
additional information
additional information
-
-
-
additional information
additional information
Q10473
KMs obtained using Lineweaver-Burk plot; the KMs for apomucin and the synthetic peptides, PPDAATAAPL and GVVPTVVPG, were measured in presence of 7.5 M UDP-GalNAc; the KMs for UDP-GalNAc were measured in presence of 1.88 mg/ml apomucin
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
MUC5AC
-
at site Thr-9, hT2, at pre-steady state
0.05
MUC5AC
-
at site Thr-9, hT2CD
0.052
MUC5AC
-
at site Thr-9, hT2
0.053
MUC5AC
-
at site Thr-9, hT2CD, at pre-steady state
0.123
MUC5AC
-
at site Thr-9, hT2, single turnover event
0.193
MUC5AC
-
at site Thr-9, hT2CD, single turnover event
0.067
MUC5AC-13
-
at site Thr-9, hT2CD
0.075
MUC5AC-13
-
at site Thr-9, hT2CD, at pre-steady state
0.103
MUC5AC-13
-
at site Thr-3, hT2
0.108
MUC5AC-13
-
at site Thr-3, hT2, at pre-steady state
0.17
MUC5AC-13
-
at site Thr-3, hT2, single turnover event
0.29
MUC5AC-13
-
at site Thr-12, hT10CD-hT2LD
0.31
MUC5AC-13
-
at site Thr-12, hT10CD
0.4
MUC5AC-13
-
at site Thr-12, hT10
0.04
MUC5AC-3
-
at site Thr-9, hT2CD, at pre-steady state
0.058
MUC5AC-3
-
at site Thr-9, hT2CD
0.137
MUC5AC-3
-
at site Thr-9, hT2CD, single turnover event
0.15
MUC5AC-3
-
at site Thr-2, hT10CD-hT2LD
0.218
MUC5AC-3
-
at site Thr-13, hT2
0.22
MUC5AC-3
-
at site Thr-13, hT2, at pre-steady state
0.24
MUC5AC-3
-
at site Thr-2, hT10CD
0.33
MUC5AC-3
-
at site Thr-2, hT10
0.52
MUC5AC-3,13
-
at site Thr-2 and Thr-12, hT10CD-hT2LD
0.76
MUC5AC-3,13
-
at sites Thr-2 and Thr-12, hT10CD
1.4
MUC5AC-3,13
-
at site Thr-2 and Thr-12, hT10
0.127
MUC5AC-9
-
at site Thr-2, hT10
0.8
STPSTPSTPSTPSTP
-
pH 6.5, 37C, mutant enzyme W129A
2.43
STPSTPSTPSTPSTP
-
pH 6.5, 37C, mutant enzyme W129F
2.53
STPSTPSTPSTPSTP
-
pH 6.5, 37C, mutant enzyme N126A
2.79
STPSTPSTPSTPSTP
-
pH 6.5, 37C, mutant enzyme W129R
3.47
STPSTPSTPSTPSTP
-
pH 6.5, 37C, wild-type enzyme
0.8
UDP-N-acetyl-D-galactosamine
-
pH 6.5, 37C, mutant enzyme W129A
2.43
UDP-N-acetyl-D-galactosamine
-
pH 6.5, 37C, mutant enzyme W129F
2.53
UDP-N-acetyl-D-galactosamine
-
pH 6.5, 37C, mutant enzyme N126A
2.79
UDP-N-acetyl-D-galactosamine
-
pH 6.5, 37C, mutant enzyme W129R
3.47
UDP-N-acetyl-D-galactosamine
-
pH 6.5, 37C, wild-type enzyme
additional information
additional information
-
hT2 catalysed glycosylation of MUC5AC-3 follows a linear time course: rate limiting catalysis or substrate binding; hT2 catalysed glycosylation of MUC5AC and MUC5AC-13 follows a biphasic time course: fast formation of enzyme-product (initial burst phase: 1 molecule product per molecule hT2 enzyme), slow and rate-limiting product release; steady-state rates of hT2 catalysis are less than 1 reaction per second at room temperature
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
68
GalNAc
-
inhibition of GalNAc-T1 mutant P-deltaN42
0.05
p-Chloromercuriphenylsulfonic acid
-
pH 7.2, 25C
0.019
UDP
-
-
0.026
UDP
-
-
0.041
UMP
-
-
0.347
UMP
-
-
0.0835
UTP
-
-
175
GalNAc
-
inhibition of GalNAc-T1 mutant D444A
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
benzyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
5
benzyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
15
benzyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2
20
benzyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
50
D-galactose
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
1
GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
5
GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
15
GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2
37
GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
50
methyl-alpha-Gal
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
0.5
o-nitrophenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
5
o-nitrophenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
7
o-nitrophenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2
12
o-nitrophenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
1
o-nitrophenyl-beta-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
10
o-nitrophenyl-beta-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2
12
o-nitrophenyl-beta-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
8
ortho-nitrophenyl-beta-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
1
p-nitrophenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
10
p-nitrophenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2; GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
0.8
p-nitrophenyl-beta-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
8
p-nitrophenyl-beta-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
10
p-nitrophenyl-beta-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2; GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
10
para-nitrophenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
1
phenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
5
phenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2; GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
15
phenyl-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
30
UDP-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
50
UDP-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
65
UDP-alpha-GalNAc
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T2
40
methyl-beta-Gal
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
additional information
additional information
Q10471, Q10472, Q8N4A0, Q8NCW6
EDTA exhibits IC50 higher than 10 in all cases; EDTA exhibits IC50s higher than 10 in all cases; galactose and methyl-alpha/beta-Gal exhibit IC50 higher than 100 mM for GalNAc-T2 enzyme and lectin domain; galactose and methyl-alpha/beta-Gal exhibit IC50s higher than 100 mM for GalNAc-T4 lectin domain; GalNAc-T2 lectin domain exhibits no specificity for anomeric configuration of GalNAc according to simlar IC50s; GalNAc-T4 lectin domain exhibits no specificity for anomeric configuration of GalNAc according to simlar IC50s; glucose derivatives, lactose and UDP exhibit IC50 higher than 100 mM in all cases; glucose derivatives, lactose and UDP exhibit IC50s higher than 100 mM in all cases; UDP-alpha-GalNAc exhibits IC50 higher than 100 mM for GalNAc-T2 lectin domain; UDP exhibits similar inhibitory effects on GalNAc-T2 and mutant GalNAc-T2-D458H
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0025
-
tumoral colon enzyme, MUC5AC peptide
0.0031
-
normal stomach enzyme, MUC5AC peptide
0.0044
-
tumoral stomach and normal colon enzyme, MUC5AC peptide
0.00863
-
-
0.09
-
-
0.11
-
-
0.15
-
-
0.5
-
GalNAc-T2 and -T3
0.6
-
GalNAc-T1
0.75
-
purification step 5, Mono S (NaCl)
1.65
-
-
1.86
-
-
2.08
-
recombinant enzyme
2.12
-
purified enzyme
2.12
-
-
2.16
-
-
30.6
-
-
45
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-13, UDP-GalNAc by mutant GalNAc-T2-D458H, pH7.4
46
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-12, UDP-GalNAc by mutant GalNAc-T2-D541A, pH7.4
49
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-5, IgA hinge-4GalNAc by mutant GalNAc-T2-D541A, pH7.4
56
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-6, UDP-Gal, pH7.4
65
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-5, UDP-Gal by mutant GalNAc-T2-D458H, pH7.4
69
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-12, UDP-GalNAc, pH7.4
72
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-21, MUC1-2GalNAc, pH7.4
81
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-1, MUC2, pH7.4
83
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-13, IgA hinge-4GalNAc, pH7.4
85
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-5, UDP-Gal by mutant GalNAc-T2-D541A, pH7.4
94
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-5, MUC1 by mutant GalNAc-T2-D458H, pH7.4
97
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-14, MUC1, pH7.4
118
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-39, MUC1-2GalNAc by mutant GalNAc-T2-D541A, pH7.4
119
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-24, IgA hinge-4GalNAc by mutant GalNAc-T2-D458H, pH7.4
143
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-15, MUC1 by mutant GalNAc-T2-D541A, pH7.4
145
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-21, IgA hinge by mutant GalNAc-T2-D541A, pH7.4
150
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-6, MUC2 by mutant GalNAc-T2-D458H, pH7.4
236
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-1, IgA hinge by mutant GalNAc-T2-D458H, pH7.4
273
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-12, MUC2 by mutant GalNAc-T2-D541A, pH7.4
292
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-18, MUC2-6GalNAc by mutant GalNAc-T2-D541A, pH7.4
302
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-17, MUC2-6GalNAc, pH7.4
321
Q10471, Q10472, Q8N4A0, Q8NCW6
+/-18, IgA hinge, pH7.4
additional information
-
-
additional information
Q10471, Q10472, Q8N4A0, Q8NCW6
0.005 +/-0.007 micromol/min/ml, MUC1-2GalNaC by mutant GalNAc-T2-D458H, pH7.4; 0.018 +/-0.003 micromol/min/ml, MUC7, pH7.4; 0.018 +/-0.004 micromol/min/ml, MUC1-b, pH7.4; 0.025 +/-0.008 micromol/min/ml, MUC1-2GalNAC, pH7.4; 0.028 +/-0.011 micromol/min/ml, MUC1-a' by mutant GalNAc-T2-D541A, pH7.4; 0.029 +/-0.007 micromol/min/ml, MUC1-a' by mutant GalNAc-T2-D458H, pH7.4; 0.029 +/-0.008 micromol/min/ml, MUC7, pH7.4; 0.031 +/-0.003 micromol/min/ml, MUC1-a', pH7.4; 0.036 +/-0.003 micromol/min/ml, MUC7, pH7.4; 0.039 +/-0.010 micromol/min/ml, erythropoitin T, pH7.4; 0.046 +/-0.005 micromol/min/ml, MUC7 by mutant GalNAc-T2-D541A, pH7.4; 0.046 +/-0.006 micromol/min/ml, MUC1-2GalNAC, pH7.4; 0.046 +/-0.009 micromol/min/ml, MUC2-6GalNAc by mutant GalNAc-T2-D541A, pH7.4; 0.047 +/-0.011 micromol/min/ml, erythropoitin T by mutant GalNAc-T2-D458H, pH7.4; 0.051 +/-0.006 micromol/min/ml, hCG-beta, pH7.4; 0.053 +/-0.010 micromol/min/ml, MUC7 by mutant GalNAc-T2-D458H, pH7.4; 0.054 +/-0.001 micromol/min/ml, hCG-beta by mutant GalNAc-T2-D458H, pH7.4; 0.055 +/-0.008 micromol/min/ml, MUC1-2GalNaC by mutant GalNAc-T2-D541A, pH7.4; 0.062 +/-0.010 micromol/min/ml, MUC2-6GalNAc, pH7.4; 0.065 +/-0.007 micromol/min/ml, hCG-beta by mutant GalNAc-T2-D541A, pH7.4; 0.066 +/-0.008 micromol/min/ml, erythropoitin T by mutant GalNAc-T2-D541A, pH7.4; 0.074 +/-0.005 micromol/min/ml, erythropoitin T, pH7.4; 0.076 +/-0.003 micromol/min/ml, erythropoitin T, pH7.4; 0.085 +/-0.003 micromol/min/ml, MUC1-a, pH7.4; 0.086 +/-0.007 micromol/min/ml, MUC1-a, pH7.4; 0.087 +/-0.006 micromol/min/ml, MUC1-b', pH7.4; 0.094 +/-0.008 micromol/min/ml, MUC1-b' by mutant GalNAc-T2-D458H, pH7.4; 0.097 +/-0.002 micromol/min/ml, MUC1, pH7.4; 0.108 +/-0.002 micromol/min/ml, OSM fragment, pH7.4; 0.121 +/-0.013 micromol/min/ml, MUC1 by mutant GalNAc-T2-D458H, pH7.4; 0.122 +/-0.007 micromol/min/ml, MUC1, pH7.4; 0.125 +/-0.003 micromol/min/ml, MUC2, pH7.4; 0.142 +/-0.005 micromol/min/ml, IgA hinge by mutant GalNAc-T2-D541A, pH7.4; 0.151 +/-0.012 micromol/min/ml, MUC1 by mutant GalNAc-T2-D541A, pH7.4; 0.158 +/-0.010 micromol/min/ml, MUC1, pH7.4; 0.161 +/-0.005 micromol/min/ml, IgA hinge, pH7.4; 0.164 +/-0.007 micromol/min/ml, MUC2 by mutant GalNAc-T2-D458H, pH7.4; 0.165 +/-0.013 micromol/min/ml, MUC2 by mutant GalNAc-T2-D541A, pH7.4; 0.185 +/-0.006 micromol/min/ml, IgA hinge by mutant GalNAc-T2-D458H, pH7.4; 0.224 +/-0.002 micromol/min/ml, IgA hinge, pH7.4; 0.281 +/-0.013 micromol/min/ml, IgA hinge, pH7.4; 0.283 +/-0.010 micromol/min/ml, MUC2, pH7.4; 128 +/-0.007 micromol/min/ml, MUC1-b' by mutant GalNAc-T2-D541A, pH7.4; 152 +/-0.018 micromol/min/ml, MUC2, pH7.4
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.5
-
Tris, imidazole and MES buffer, kappa-casein
6.7 - 7.8
-
broad pH-optimum between pH 6.7-7.8 with maximum at pH 7.2
6.8 - 8.2
-
-
7
-
recombinant protein lacking the trans-membrane domain
7.2 - 8.6
-
-
7.2
-
peptides Ac-Thr-Pro-Pro-Pro and Pro-Arg-Thr-Pro-Pro-Pro
7.2
-
broad pH-optimum between pH 6.7-7.8 with maximum at pH 7.2
7.4
-
assay at
7.5 - 8.5
-
-
7.5
-
-
7.5
-
assay at
7.8
-
assay at
additional information
-
pI: 6.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9.5
-
pH 4.5: no activity, pH 6.8: gradual decrease of activity below, pH 9.5: 16% of activity maximum
6 - 8
-
about 60% of maximal activity at pH 6.0 and at pH 8.0
6.7 - 8.7
-
pH 6.7: about 30% of maximal activity, pH 8.7: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
28
-
recombinant protein lacking the trans-membrane domain
29 - 33
-
-
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
Q925R7
assay at
37
-
assay at
37
Q8IUC8
assay at
37
-
assay at
37
Q9R0C5
assay at
37
-
assay at
37
-
assay at
37
Q8MVS5
assay at
37
-
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17 - 37
-
17C: about 40% of maximal activity, 37C: about 65% of maximal activity
20 - 37
-
20C: 49% of maximal activity, 37C: 48% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
expression of ppGalNAc-T1, -T2, -T3, -T4, -T6 and -T9 in B-cells and IgA-bearing B cells
Manually annotated by BRENDA team
-
isozymes ppGalNAcT-1, ppGalNAcT-2, and ppGalNAcT-3, expression patterns, overview. Expression of isozyme ppGalNAcT-1 especially in calvaria and tibia
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
low level of isozyme T4
Manually annotated by BRENDA team
-
ppGalNAc-T13 expression only in brain, exclusively in neuronal cells
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9, less amount
Manually annotated by BRENDA team
-
brain-specific expression of GalNAc-T9, mRNA is most abundant in cerebellum, lower levels in cerebral cortex, frontal lobe, temporal lobe and putamen
Manually annotated by BRENDA team
Q8IUC8
ppGalNAc-T13 is highly and restrictively expressed in brain, fetal brain, adult cerebellum and cerebral cortex, exclusively in neuronal cells
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q9HCQ5
high levels of expression in cerebellum, hippocampus, thalamus, and cerebral cortex. Expression is associated with neurons, but not with glial cells
Manually annotated by BRENDA team
Q8IUC8
pp-GalNAc-T13 is specifically expressed in neurons
Manually annotated by BRENDA team
Q96FL9
cDNA library used for cloning
Manually annotated by BRENDA team
-
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
redundancy of enzyme activity
Manually annotated by BRENDA team
-
benign cell line HMT 3522, non-metastatic cell line BT 474, metastatic cell lines ZR75-1, T-47D, MCF-7
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
ppGalNAc-T1 detection in all studied breast cancer cell lines
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
ppGalNAc-T2 detection in all studied breast cancer cell lines
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
ppGalNAc-T3 nearly undetectable in breast cancer cell line HMT-3522
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
ppGalNAc-T4 undetectable in breast cancer cell line ZR75-1 cell
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
ppGalNAc-T6 nearly undetectable in breast cancer cell line HMT-3522
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
very weak signal
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
weak signal
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
moderate signal
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
strong signal
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
very strong signal
Manually annotated by BRENDA team
-
lymphoma cells
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9
Manually annotated by BRENDA team
-
isozyme T4
Manually annotated by BRENDA team
-
ppGaNTase-T6
Manually annotated by BRENDA team
Q9R0C5
ppGaNTase-T6
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
ascending right part, low enzyme expression, decreased activity compared to normal colon, mono-glycosylates MUC5AC peptide
Manually annotated by BRENDA team
-
ascending right part, high enzyme expression, 2fold higher activity than in stomach
Manually annotated by BRENDA team
-
hydatid cyst wall
Manually annotated by BRENDA team
-
isozyme T4
Manually annotated by BRENDA team
-
embryonic day 14.5, ppGaNTase-T9 is expressed relatively abundantly compared with ppGaNTase-T7, accumulation in brain
Manually annotated by BRENDA team
Q8MVS5
cloning of the pgant35A gene from embryonic cDNA library
Manually annotated by BRENDA team
-
expression increases at later embryonal developmental stages, RT-PCR, xGalnt1, -6, -7 expression throughout early and late embryonal development
Manually annotated by BRENDA team
Q8MVS5
dorsal longitudinal tracheal trunks and tracheal transverse connectives at embryonic stages 15-17, loss of PGANT35A activity leads to tracheal defects at embryonic stages 15-17, altered intracellular trafficking, reduction in apical and luminal epithelial marker components, alterations in cell shape, polarity and zona adherens formation, mislocation and disfunction of septate junctions, disruption of paracellular diffusion barrier formation
Manually annotated by BRENDA team
-
high enzyme expression in tumoral gastric tissue displaying intestinal metaplasia, increased activity compared to normal stomach, di-glycosylates MUC5AC peptide
Manually annotated by BRENDA team
-
human diffuse gastric carcinoma cell line GP202, enzyme form GalNAc-T1, human diffuse gastric carcinoma cell line GP202, enzyme form GalNAc-T2, human diffuse gastric carcinoma cell line GP202, enzyme form GalNAc-T3, human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T1, human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T2, human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T3, human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T4
Manually annotated by BRENDA team
-
expression analysis of ppGalNAc-T6 in gastric mucosa, intestinal metaplasia, and gastric carcinomas, the isozyme shows a heterogeneous expression and staining pattern
Manually annotated by BRENDA team
-
stomach fundus, 2fold lower activity than in colon, mono-glycosylates MUC5AC peptide
Manually annotated by BRENDA team
-
RT-PCR, expression is restricted to dorsal marginal zones at embryonal stage 20, RT-PCR, xGalnt1, -6, -7 expression in both, dorsal and ventral marginal zones at embryonal stage 20
Manually annotated by BRENDA team
-
ppGalNacT-1 activity is essential for O-glycosylation in germinal center (GC) B cells within the white pulp of the spleen and lymph nodes upon immunization, increased apoptosis of IgG bearing GC B cells and reduced IgG abundance in the absence of ppGalNAcT-1
Manually annotated by BRENDA team
-
low level of isozyme T4
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9, less amount
Manually annotated by BRENDA team
-
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
ppGalNAcT-10 amplified from isolated total RNA
Manually annotated by BRENDA team
Q96FL9
expression detected by Western blot
Manually annotated by BRENDA team
-
AH-66 ascites hepatoma cells, harvested 6-7 days after the intraperitoneal transfer of ascites fluid from donor rats, activity much higher than in rat liver
Manually annotated by BRENDA team
Q8MVS5
loss of PGANT35A activity does not alter morphology or staining patterns of epithelial marker components
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
weak signal
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
moderate signal
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
very weak signal, nearly undetectable
Manually annotated by BRENDA team
-
ovarian cancer cell
Manually annotated by BRENDA team
-
enzyme form GalNAc-T1, enzyme form GalNAc-T2, enzyme form GalNAc-T3, low activity, enzyme form GalNAc-T4, low activity, enzyme form GalNAc-T6
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
enzyme form GalNAc-T1, enzyme form GalNAc-T3, human trophoblast, enzyme form GalNAc-T1, low activity, enzyme form GalNAc-T11, low activity, enzyme form GalNAc-T4
Manually annotated by BRENDA team
-
enzyme form GalNAc-T11, enzyme form GalNAc-T3, enzyme form GalNAc-T4, enzyme form GalNAc-T6, human stomach cancer, enzyme form GalNAc-T1, human stomach cancer, enzyme form GalNAc-T2
Manually annotated by BRENDA team
-
low level of isozyme T4
Manually annotated by BRENDA team
-
expresses GalNAc-T2
Manually annotated by BRENDA team
-
significantly high expression of ppGalNAc-T14
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q8NCW6
tubules, no activity in glomeruli
Manually annotated by BRENDA team
-
cloned from mouse kidney total RNA
Manually annotated by BRENDA team
-
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
subtegumental region of larval worms
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
ppGalNAcT-1 mediated O-glycosylation contributes to innate immune inflammatory response among activated endothelial cells by expression of cell surface selectin ligands on neutrophils
Manually annotated by BRENDA team
-
low level of isozyme T4
Manually annotated by BRENDA team
-
expresses significantly more GalNAc-T2 than GalNAc-T1
Manually annotated by BRENDA team
-
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
colon carcinoma cell line
Manually annotated by BRENDA team
Q58A54
lung small-cell carcinoma cell line
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9, less amount
Manually annotated by BRENDA team
-
isozyme T4
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
-
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
mostly inguinal lymph nodes, not Peyers patch tissue, ppGalNAcT-1 activity regulates L-selectin ligand level in high endothelial venules that is responsible for lymph node cellularity and B- and T-cell homing
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
very weak signal
Manually annotated by BRENDA team
Q96FL9
no expression detected by Western blot
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
strong signal
Manually annotated by BRENDA team
-
enzyme form GalNAc-T3, human colon epithelial carcinoma, enzyme form GalNAc-T1, human colon epithelial carcinoma, enzyme form GalNAc-T2, low activity, enzyme form GalNAc-T11, low activity, enzyme form GalNAc-T4
Manually annotated by BRENDA team
-
gastric cancer cell line, cDNA encoding the transferase is cloned and sequenced from a cDNA library of a human cancer cell line
Manually annotated by BRENDA team
-
gastric carcinoma cell line
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
expression of ppGalNAc-T1, -T2, -T3, -T4, -T6 and -T9 in NCI-H929 IgA myeloma cells
Manually annotated by BRENDA team
Q8IUC8
ppGalNAc-T13 is abundantly expressed in neuroblastoma cells
Manually annotated by BRENDA team
-
RT-PCR, expression at embryonal stage 13 in anterior mesoderm and neural crest
Manually annotated by BRENDA team
Q8IUC8
ppGalNAc-T13 is abundantly expressed in primary cultured neurons
Manually annotated by BRENDA team
Q8IUC8
pp-GalNAc-T13 is specifically expressed in neurons
Manually annotated by BRENDA team
-
low level of isozyme T4
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
-
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
-
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q96FL9
RCC 7860, expression detected by Western blot
Manually annotated by BRENDA team
Q8N4A0
immunohistology with a monoclonal antibody shows the expected Golgi-like localization in salivary glands
Manually annotated by BRENDA team
Q8MVS5
loss of PGANT35A activity does not alter morphology or staining patterns of epithelial marker components
Manually annotated by BRENDA team
Q58A54
lung small-cell carcinoma cell line
Manually annotated by BRENDA team
-
leukemia cell
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
-
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9, less amount
Manually annotated by BRENDA team
-
low level, ppGaNTase-T4
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9, less amount
Manually annotated by BRENDA team
-
isozyme T4
Manually annotated by BRENDA team
-
ppGaNTase-T6
Manually annotated by BRENDA team
Q9R0C5
ppGaNTase-T6
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
expression analysis of ppGalNAc-T6 in gastric mucosa, intestinal metaplasia, and gastric carcinomas
Manually annotated by BRENDA team
-
ppGaNTase-T6: highest level of mRNA
Manually annotated by BRENDA team
Q9R0C5
ppGaNTase-T6: highest level of mRNA
Manually annotated by BRENDA team
-
GalNAc-T5 is most abundant in
Manually annotated by BRENDA team
-
high enzyme concentration
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
very weak signal
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
moderate signal
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
strong signal
Manually annotated by BRENDA team
-
RT-PCR, expression at embryonal stage 27 excluded from the central area of the mediolateral spinal cord containing proliferating neuronal precursors, RT-PCR, expression at embryonal stage 27 in forebrain, RT-PCR, expression at embryonal stage 27 in neural crest cells that migrate into heart regions, branchial arches and heart anlage, RT-PCR, expression at embryonal stage 27 in notochord (highest in posterior regions), RT-PCR, expression at embryonal stage 27 in the mantle (differentiating) territory of the mediolateral spinal cord
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q8MVS5
loss of PGANT35A activity leads to diminished O-glycosylation in epithelial cells of tracheal tube as well as reduced amount of GalNAc alpha-S/T glycans at the apical cell surface
Manually annotated by BRENDA team
Q58A54
glioblastoma cell line
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9, less amount
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9, less amount
Manually annotated by BRENDA team
-
isozyme T4
Manually annotated by BRENDA team
Q10471, Q7Z4T8
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
-
a colon cancer cell line
Manually annotated by BRENDA team
-
a colon cancer cell line
Manually annotated by BRENDA team
Q8N4A0
Northern blot analysis of human tissues
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
weak signal
Manually annotated by BRENDA team
Q10471, Q10472, Q14435, Q8N4A0, Q8NCL4
very strong signal
Manually annotated by BRENDA team
Q8N4A0
gastric carcinoma cell line
Manually annotated by BRENDA team
additional information
-
quantitative and qualitative differences in different organs
Manually annotated by BRENDA team
additional information
Q8MVS5
expression of enzyme throughout embryonic, larval and pupal stages, in adult males and females, expression increases during larval development and continues through pupal and adult stages
Manually annotated by BRENDA team
additional information
-
existence of more than one form of GalNAc-Ts which are expressed differentially in the gastrointestinal tract
Manually annotated by BRENDA team
additional information
-
ppGalNAc-T14 is ubiquitously expressed
Manually annotated by BRENDA team
additional information
-
traces of ppGaNTase-T6 in the ovary, cervix and uterus, ppGaNTase-T1 is present in all tissues examined
Manually annotated by BRENDA team
additional information
Q9R0C5
traces of ppGaNTase-T6 in the ovary, cervix and uterus, ppGaNTase-T1 is present in all tissues examined
Manually annotated by BRENDA team
additional information
-
ppGalNAc-T13: not in astrocytes, tissue distribution of several ppGalNAc-transferases
Manually annotated by BRENDA team
additional information
Q8IUC8
tissue distribution of several ppGalNAc-transferases
Manually annotated by BRENDA team
additional information
Q8IUC8
ppGalNAc-T1 is ubiquitously expressed, ppGalNAc-T13: not in glioblastoma cells and primary cultured astrocytes
Manually annotated by BRENDA team
additional information
-
no activity of GalNAc-T4 in GP202 cells, no activity of GalNAc-T6 in GP202 cells and GP220 cells, no activity of GalNAc-T6 in MKN45 cells, GP202 cells, GP220 cells, and K562
Manually annotated by BRENDA team
additional information
Q10471, Q7Z4T8
pp-GalNAc-T15 transcript is ubiquitously expressed in human tissues, very low activity in bone marrow, leukocyte, heart, liver, testis, enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
additional information
Q8N4A0
Northern analysis of human organs revealed a wide expression pattern
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q8MM26
contains a 680-amino acid C-terminal lumenal domain, and a 49-amino acid N-terminal cytoplasmic domain
Manually annotated by BRENDA team
-
based on detection of microinjected HA-tagged protein in the supernatant of dissociated animal ectodermal explants
-
Manually annotated by BRENDA team
-
cis-Golgi apparatus and smooth-membraned vesicular structures in close topological relation with it
Manually annotated by BRENDA team
-
immunocytochemical detection using an isozyme-specific mouse monoclonal antibody
Manually annotated by BRENDA team
-
transient transfection of Flag-tagged version in COS-7 cells
Manually annotated by BRENDA team
-
specifically localized in
Manually annotated by BRENDA team
-
CHO ldlD-MUC1 cells in presence of GalNAc
Manually annotated by BRENDA team
Q10471, Q10472, Q8N4A0, Q8NCW6
CHO ldlD-MUC1 cells in presence of GalNAc: same pattern of biotinylated GalNAc-T2 like Tn (GalNAc-alpha-Ser/Thr)
Manually annotated by BRENDA team
Q10471, Q10472, Q8N4A0, Q8NCW6
CHO ldlD-MUC1 cells in presence of GalNAc: same pattern of biotinylated GalNAc-T4 and -T4 lectin like Tn (GalNAc-alpha-Ser/Thr)
Manually annotated by BRENDA team
-
human salivary glands
Manually annotated by BRENDA team
Q10471, Q10472, Q8N4A0, Q8NCW6
human salivary glands: same pattern of biotinylated GalNAc-T2 at Golgi-like supranuclear locations like Tn (GalNAc-alpha-Ser/Thr)
Manually annotated by BRENDA team
Q10471, Q10472, Q8N4A0, Q8NCW6
human salivary glands: same pattern of biotinylated GalNAc-T4 lectin at Golgi-like supranuclear locations like Tn (GalNAc-alpha-Ser/Thr)
Manually annotated by BRENDA team
-
membrane-bound
Manually annotated by BRENDA team
Q9R0C5
ppGaNTase-T6: type II membrane protein with a 27-amino acid hydrophobic region
Manually annotated by BRENDA team
Q86SF2
GalNAc-T7: type II transmembrane protein with a hydrophobic signal anchor sequence in residues 10-24
Manually annotated by BRENDA team
Q8MVS5
type II membrane protein containing a 23-amino acid transmembrane domain and an 8-amino acid cytoplasmic tail
Manually annotated by BRENDA team
-
type II membrane protein containing a 23-amino acid transmembrane domain and an 8-amino acid cytoplasmic tail
Manually annotated by BRENDA team
-
GalNAc-T9: type II membrane protein with a 20-amino acid transmembrane domain, a 7-amino acid cytoplasmic domain and a 91-amino acid stem region
Manually annotated by BRENDA team
Q925R7
ppGaNTase-T9: type II integral membrane protein with a 20-amino acid transmembrane domain, a 9-amino acid cytoplasmic domain and a 94-amino acid stem region
Manually annotated by BRENDA team
Q8IUC8
ppGaNTase-T13: type II membrane protein with a 20-amino acid transmembrane segment and an 8-amino acid N-terminal cytoplasmic domain
Manually annotated by BRENDA team
-
ppGalNAc-T14: type II membrane protein
Manually annotated by BRENDA team
Q8MM26
type II membrane protein, 22-amino acid transmembrane sequence
Manually annotated by BRENDA team
-
type II membrane protein
Manually annotated by BRENDA team
-
type II membrane protein
Manually annotated by BRENDA team
-
recombinant GalNAc-T1, -T2 and -T3, expressed in Sf9 cells
-
Manually annotated by BRENDA team
-
soluble, secreted enzyme is prepared by substituting the honeybee melittin leader sequence for the sequences coding for the cytoplasmic and membrane spanning domains
-
Manually annotated by BRENDA team
-
may be a proteolytic cleavage product from a membrane-bound form
-
Manually annotated by BRENDA team
-
isozyme ppGalNAc T1
-
Manually annotated by BRENDA team
additional information
-
not in rough endoplasmic reticulum, its translational elements, smooth-membraned structures related to it and the trans Golgi apparatus, mucn droplets and the plasma membrane
-
Manually annotated by BRENDA team
additional information
-
intracellular membrane-bound enzyme, localized in the secretory pathway
-
Manually annotated by BRENDA team
additional information
-
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
-
single band, SDS-PAGE. Polymerase chain reaction cloning and sequencing of the human version of the bovine transferase are presented, and 98% similarity at the amino acid level is found
687490
54000
-
gel filtration
489167
59210
-
molecular mass of the deduced amino acid sequence of the soluble transferase is 59205 Da, which is slightly higher than the experimentally determined molecular weight but within the limits of accuracy of the SDS-PAGE and gel filtration systems used
687490
61000
Q96FL9
endogenous GalNAc-T14 in HEK293T cells detected by anti-GalNAc-T14 antibody; Flag-tag fusion protein expressed in HEK293T cells detected by anti-Flag and anti-GalNAc-T14 antibody
689866
64700
-
cDNA sequence has a 571-amino acid coding region indicating a protein of 64.7 kDa with a type II domain structure
687490
69000
-
PAGE
489170
69000
-
gel filtration
489172
70000
-
gel filtration
489177
71500
-
gel filtration
489172
87000
Q96FL9
bacterially expressed GST-fusion protein (GST: 26 kDa) detected by anti-GST and anti-GalNAc-T14 antibody; SDS-PAGE
689866
100000
-
gel filtration
489178
200000
-
gel filtration
489168
additional information
-
in Western blot, slightly lower molecular weight of HA-tagged protein in the supernatant than in the cell pellet of dissociated animal ectodermal explants
686299
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 61000, SDS-PAGE
?
Q8MVS5
x * 78000, recombinant wild type and SF32 mutant enzyme, SDS-PAGE
?
-
x * 57000, recombinant isozyme ppGalNAcT-1, SDS-PAGE, x * 60000, recombinant isozyme ppGalNAcT-2, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 56000, SDS-PAGE in presence of 2-mercaptoethanol
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
contains 3 N- and 1 O-linked oligosaccharide structures per molecule, soluble enzyme contains N-acetylglucosamine, N-acetylgalactosamine, mannose, galactose and fucose, N-linked structures are likely to be of the truncated high-mannose type
glycoprotein
-
2 N-linked oligosaccharides, on most enzyme molecules both oligosaccharides are of the complex type, but some molecules contain one complex type and one high mannose type
glycoprotein
-
enzyme contains more than one N-linked oligosaccharide
proteolytic modification
-
assumed due to detection in supernatants of dissociated ectodermal cells at slightly lower molecular weight
glycoprotein
-
residues Asn-95 and Asn-552 of the recombinant enzyme are occupied by N-linked sugars in Cos7 cells
additional information
-
enzyme activity is reduced up to 95% by in vitro acetylation of residue K103, S109, K111, K363, S373, K521 and S529
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
binary complex of UDP and ppGalNAcT-2 in crystal structure PDB: 2FFV; dynamics of loop A dependent on presence of ligand and state of loop B; dynamics of loop B reduced upon UDP-GalNAc (donor) binding but not further reduced by subsequent peptide (acceptor) binding; flexibility of terminal residues of EA2 peptide in EA2-enzyme complex is reduced upon presence of a GalNAc moiety; in presence of UDP or UDP and peptide no water molecule-dependent, large conformational changes; low flexibility of EA2 peptide centre in EA2-enzyme complex; PDB: 2FFU incl. substrates versus PDB: 2FFU lacking substrates: flexibility of catalytic and lectin domain independent of each others presence or distance; PDB: 2FFV versus PDB: 2FFU: large conformational changes (13 to 24 ) in catalytic domain upon peptide binding and processing, loop A (AA89-98), loop B (AA361-377); PDB: 2FFV versus PDB: 2FFU: small conformational changes (4 to 5 ) of protein backbone upon peptide binding and processing, loop C (AA127-134), loop D (AA287-297), loop E (AA330-333); single-displacement transfer mechanism revealed by simulations on crystal structure PDB: 2FFU; water molecule-dependent rotation of W331 side chain (WGGEN motif within loop E) that triggers loop B opening in the absence of substrate UDP-GalNAc and facilitates donor access into the active site as well as product release
Q10471
hanging drop vapor diffusion at room temperature. X-ray crystal structures of the enzyme bound to the product UDP at 2.75 A resolution and to UDP and an acceptor peptide substrate EA2 (PTTDSTTPAPTTK) at 1.64 A resolution
-
crystals of mppGaNTase-T1 (without maltose-binding protein) are grown by hanging drop vapor diffusion at room temperature
O08912
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 35
-
1 h, less than 20% loss of activity
489168
30
-
24 h, GalNAc-T1 and -T3: 40% loss of activity, GalNAc-T2: 60% loss of activity
489179
37
-
8 h, 20 mM imidazole-HCl, pH 7.2, 0.1% Triton X-100, 5 mM MnCl2, 5% w/v glycerol, 40% loss of activity
489170
45
-
1 h, 50% loss of activity
489168
55
-
1 h, complete loss of activity
489168
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
23% loss of specific activity after 12h shaking at 37C
Q10471, Q10472, Q8N4A0, Q8NCW6
25% loss of specific activity after 12 h shaking at 37C
Q10471, Q10472, Q8N4A0, Q8NCW6
31% loss of specific activity after 12h shaking at 37C
Q10471, Q10472, Q8N4A0, Q8NCW6
mutant GalNAc-T2-D458H: 15% loss of specific activity after 12h shaking at 37C
Q10471, Q10472, Q8N4A0, Q8NCW6
mutant GalNAc-T2-D541A: 19% loss of specific activity after 12h shaking at 37C
Q10471, Q10472, Q8N4A0, Q8NCW6
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme loses activity upon storage
-
-20C, 3 months, stable
-
-20C, 20 mM imidazole-HCl, pH 7.2, 0.1% Triton X-100, 5 mM MnCl2, 60% w/v glycerol, 1 year, stable
-
-80C, washed mucosal membranes, no loss of activity after 1 year
-
4C, 20 mM imidazole-HCl, pH 7.2, 0.1% Triton X-100, 5 mM MnCl2, 25% w/v glycerol, 1 month, 10% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
21fold, recombinant soluble enzyme, expressed in Sf9 cells
-
517000fold
-
7500fold
-
recombinant enzyme
-
recombinant soluble His-tagged enzyme from Cos-7 cells, purification from the medium
-
recombinant enzyme, expressed in COS7 cells
Q8MVS5
recombinant enzyme
-
-
Q8N4A0
anti-FLAG m2 affinity chromatography
-
GST fusion protein purified by affinity chromatography, elution with 10 mM glutathione, pH8; GSTrap FF chromatography
Q96FL9
immobilized metal ion affinity chromatography (Ni2+)
-
ion exchange chromatography
-
partial
-
placenta enzyme, Muc2 peptide affinity chromatography separates two distinct transferase activities with overlapping specificity concerning Muc2 substrate, but which are distinguishable with respect to HIV-V3 substrate
-
ppGalNAc-T13, -T1 and -T9, expressed in Sf21 or High FiveTM insect cells
Q8IUC8
ppGalNAc-T14 and -T2, expressed in Sf21 cells
-
purification of His-tagged truncated lectin domain by IMAC, 250 mM imidazole; purification of His-tagged truncated lectin domain by IMAC, 250 mM imidazole; purification of secreted recombinant proteins from cell culture supernatant by Amberlite IRA-95 chromatography followed by SP Sepharose Fast Flow ion-exchange chromatography and concentrated by centrifugation through 10000 Da cut-off filter followed by elution from a PC3.2/3 column; purification of secreted recombinant proteins from cell culture supernatant by Amberlite IRA-95 chromatography followed by SP Sepharose Fast Flow ion-exchange chromatography and concentrated by centrifugation through 10000 Da cut-off filter followed by elution from a PC3.2/3 column; purification of secreted recombinant proteins from cell culture supernatant by Amberlite IRA-95 chromatography followed by SP Sepharose Fast Flow ion-exchange chromatography and concentrated by centrifugation through 10000 Da cut-off filter followed by elution from a PC3.2/3 column; purification of secreted recombinant proteins from cell culture supernatant by Amberlite IRA-95 chromatography followed by SP Sepharose Fast Flow ion-exchange chromatography and concentrated by centrifugation through 10000 Da cut-off filter followed by elution from a PC3.2/3 column
Q10471, Q10472, Q8N4A0, Q8NCW6
purified to apparent homogeneity using a synthetic acceptor peptide as affinity ligand; purified to apparent homogeneity using a synthetic acceptor peptide as affinity ligand
-
recombinant GalNAc-T1, -T2 and -T3, expressed in Sf9 cells
-
recombinant ppGalNAc-T1, -T2, -T3, -T4, -T6 and T9, expressed in insect cells
-
-
O08912
2500fold; partial
-
partial; recombinant ppGaNTases expressed in COS7 cells
-
recombinant His-tagged isozymes ppGalNAcT-1 and ppGalNAcT-2 from Pichia pastoris medium by nickel affinity chromatography, the tag is cleaved off by TEV protease, recombinant isozyme ppGalNAcT-3t from medium of COS-7 cells
-
submaxillary gland enzyme, 123.5fold
-
recombinant mutant GalNAc-T1, expressed in COS7 cells
-
recovery of the secreted recombinant proteins that harbour a protein A IgG-binding domain by IgG-Sepharose
Q10473
1320fold
-
affinity chromatography on deglycosylated Cowper's gland mucin bound to Sepharose, 12500fold
-
recombinant enzyme
-
submaxillary gland enzyme, 25.4fold
-
recombinant enzyme
-
recombinant from Drosophila melanogaster S2 cells
Q8MM26
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in COS7 cells as soluble His-tagged protein, secretion to the medium
-
expression in Escherichia coli
-
expression of wild-type and mutants in COS7 cells
-
full-length cDNA is cloned, a soluble enzyme construct prepared by substituting the honeybee melittin leader sequence for the sequences coding for the cytoplasmic and membrane spanning domains is expressed in insect Sf9 cells using a recombinant baculovirus, nucleotide and amino acid sequence
-
cloning and sequenceing of cDNAs encoding several isozymes, DNA sequence analysis
-
cloning, sequencing and expression of wild type and SF32 mutant recombinant pgant35A gene in COS7 cells
Q8MVS5
expression in COS7 cells as truncated version from pIMKF4 SV40; expression in COS7 cells as truncated version from pIMKF4 SV40
Q6WV17, Q6WV19
PGANT35A in pUAST plasmid for trachea-specific, Gal4-iduceable expression in transgenic flies under control of breathless promoter
Q8MVS5
expression in COS7 cells
-
expression in COS-7 cells
-
; ppGalNAc-T13, -T1 and -T9 are cloned, and expressed in Sf21 or High FiveTM insect cells in a soluble form, ppGalNAc-T13: gene is localized to chromosome 2, nucleotide sequence encodes a 556-amino acid protein, ppGalNAc-T1 is localized to chromosome 18
Q8IUC8
cloning of ppGalNAc-T1, -T2, -T3, -T4, -T6 and T9 and expression as secreted proteins fused with a FLAG peptide in insect cells
-
enzyme form pp-GalNAc-T15
Q10471, Q7Z4T8
expressed in Escherichia coli BL21(DE3) cells and HEK-293T cells; full-length GalNAc-T14 in pFlag-CMV2, expression in HEK293T cells; full-length GalNAc-T14 in pGEX-4T-1, expression in Escherichia coli BL21(DE3)
Q96FL9
expressed in Sf9 cells, expressed in a stably transfected Chinese hamster ovary cell line exhibited a unique acceptor substrate specificity, expressed in High Five cells; expressed in Sf9 cells or in a stably transfected Chinese hamster ovary cell line exhibited a unique acceptor substrate specificity; expressed in Sf9 cells or in a stably transfected Chinese hamster ovary cell line exhibited a unique acceptor substrate specificity; expressed in Sf9 cells or in a stably transfected Chinese hamster ovary cell line exhibited a unique acceptor substrate specificity
Q8N4A0
expression of GalNAc-T1, -T2 and -T3 as soluble proteins in insect Sf9 cells
-
expression of GalNAc-T1, -T2 and -T3 as soluble proteins in insect Sf9 cells; expression of secreted GalNAc-T4 in CHO cells
-
expression of secreted GalNAc-T4 in CHO cells
-
FLAG fusion protein (amino acid residue 42-607 (catalytic region and lectin domain)) expressed in HEK293T cells
Q58A54
FLAG fusion transmembrane deletion construct expressed in COS7 cells
-
GalNAc-T7 is cloned and expressed in insect Sf9 cells, open reading frame of 1974 bp, GALNT7 gene encoding GalNAc-T7 is localized on chromosome 4q31.1
Q86SF2
GalNAc-T9 is cloned and characterized encoding a 603 amino acid protein, nucleotide and amino acid sequence
-
GALNT12, DNA and amino acid sequence determination and analysis, genotyping, recombinant expression of tagged wild-type and mutant enzymes
-
His tagged truncated protein expressed in High Five cells
-
in pAcGP67-His vector for amplification as bacculovirus in Sf9 cells and subsequent infection of High Five cells; in pAcGP67-His vector for amplification as bacculovirus in Sf9 cells and subsequent infection of High Five cells; in pAcGP67-His vector for amplification as bacculovirus in Sf9 cells and subsequent infection of High Five cells; in pAcGP67-His vector for amplification as bacculovirus in Sf9 cells and subsequent infection of High Five cells
Q10471, Q10472, Q8N4A0, Q8NCW6
in pKN55-N6His-TEV for expression in Pichia pastoris strain SMD1168 and with TEV-cleavable hexa-His-tag
-
overexpressed in SGC-7901 cell
-
PCR cloning of human version of GalNAc-T1, based on the reported sequence of bovine GalNAc-T1. Polymerase chain reaction cloning and sequencing of the human version of the bovine transferase are presented, and 98% similarity at the amino acid level is found; PCR construct is expressed in insect cells using a baculovirus vector. Expression of GalNAc-T2 in Sf9 cells
-
ppGalNAc-T14 and -T2 are cloned and expressed in Sf21 cells in a secreted form, 2 alternatively spliced isoforms of the ppGalNAc-T14 transcript are sequenced, major splicing form: 552-amino acid protein, ppGalNAc-T14 gene is mapped to chromosome 2p23.2
-
recombinant human pt-GalNAc-T, which is expressed in insect cells, does not glycosylate several peptides derived from mammalian mucins
Q9HCQ5
soluble His-tagged protein (cytosolic tail and transmembrane domain removed) expressed in Sf9 cells
-
truncated protein expressed in insect cells
-
-
P70419
amino acid sequences of ppGaNTase-T3 and T4
-
isozymes ppGalNAcT-1, ppGalNAcT-2, and ppGalNAcT-3, recombinant expression of the His-tagged isozymes ppGalNAcT-1, ppGalNAcT-2 in Pichia pastoris and of isozyme ppGalNAcT-3 in COS-7 cells, secretion of the recombinant proteins
-
pIMKF3 for expression in COS7 cells
-
ppGalNAc-T13 and -T1 are localized to chromosome 2 and 18, ppGalNAc-T13 is cloned and sequenced, 556-amino acid protein
-
ppGaNTase-T1 (mppGaNTase-T1) is expressed as a fusion protein with maltose-binding protein at the N terminus and residues 42559 of mppGaNTase-T1 at the C terminus separated by a tobacco etch virus protease recognition sequence. The fusion protein is expressed in Pichia pastoris
O08912
ppGaNTase-T1 is cloned from kidney RNA, amino acid sequence, expression of ppGaNTases as secreted forms in COS7 cells
-
ppGaNTase-T4 from spleen cDNA library, transient expression in COS7 cellsas secreted soluble and functional enzyme
-
deletion mutant GalNAc-T1 cDNA is cloned and expressed in COS7 cells
-
expression in COS7 cells as truncated version from pInsProA
Q10473
gene encoding ppGaNTase-T9 from sublingual gland is cloned, characterized, sequenced and expressed transiently in COS7 cells, gene encodes a unique 603-amino acid protein
Q925R7
ppGaNTase-T6 from sublingual gland is cloned, sequenced and expressed transiently in COS7 cells as secreted form, 657-amino acid protein, amino acid sequences of ppGaNTase-T1, -T5 and -T6
Q9R0C5
-
Q29121
expression in COS7 cells with an N-terminal hexahistidine tag
-
-
Q6TBR3, Q6TBR4, Q6YK77
stable functional expression in Drosophila melanogaster S2 cells
Q8MM26
stable transfected into Drosophila melanogaster S2 cells
-
Flag-tagged xGalnt-6 in pCS2+ for eukaryotic expression; ORF of xGalntl-1, a C-terminal HA-tagged and a Flag-tagged version in pCS2+ for eukaryotic expression
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
upregulation in SGC-7901 cells inhibits proliferation in vitro
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D209A
-
inactive mutant enzyme
F124A
-
inactive mutant enzyme
H125A
-
1% of the wild-type activity
H211A
-
no detectable activity
H341A
-
6% of the wild-type activity
H344A
-
no detectable activity
L189A
-
inactive mutant enzyme
N126A
-
the turnover number for UDP-N-acetyl-D-galactosamine and STPSTPSTPSTPSTP is 1.4fold lower than the wild-type value, the KM-value for UDP-N-acetyl-D-galactosamine is 5.5fold higher than the wild-type value, the KM-value for STPSTPSTPSTPSTP is 1.6fold higher than the wild-type value
R193A
-
inactive mutant enzyme
W129A
-
the turnover number for UDP-N-acetyl-D-galactosamine and STPSTPSTPSTPSTP is 4.3fold lower than the wild-type value, the KM-value for UDP-N-acetyl-D-galactosamine is 3.5fold higher than the wild-type value, the KM-value for STPSTPSTPSTPSTP is 2.6fold higher than the wild-type value
W129F
-
the turnover number for UDP-N-acetyl-D-galactosamine and STPSTPSTPSTPSTP is 1.4fold lower than the wild-type value, the KM-value for UDP-N-acetyl-D-galactosamine is 1.8fold higher than the wild-type value, the KM-value for STPSTPSTPSTPSTP is 1.2fold lower than the wild-type value
W129R
-
the turnover number for UDP-N-acetyl-D-galactosamine and STPSTPSTPSTPSTP is 1.2fold lower than the wild-type value, the KM-value for UDP-N-acetyl-D-galactosamine is 2.1fold higher than the wild-type value, the KM-value for STPSTPSTPSTPSTP is 1.2fold lower than the wild-type value
pgant35A-3775
Q8MVS5
transgenic fly: heterozygous with pgant35A-SF32 or pgant35A-HG8 allele, germ line clone: heterozygous with pgant35A-HG8 or pgant35A-SF32 allele, nonsense mutation results in translational stop and loss of enzymatic activity
pgant35A-HG8
Q8MVS5
transgenic fly: heterozygous with pgant35A-SF32 or pgant35A-3775 phenotype, germ line clone: homozygous or with pgant35A-3775 allele , nonsense mutation results in translational stop and loss of enzymatic activity
pgant35A-SF32
Q8MVS5
transgenic fly: heterozygous with pgant35A-3775 or pgant35A-HG8 phenotype, germ line clone: homozygous or with pgant35A-3775 allele, missense mutation: Arg to Trp, results in diminished activity
Q89stop
Q8MVS5
HG8 mutant, truncated protein within the putative stem region, early pupal lethality
R227W
Q8MVS5
SF32 mutant with dramatically reduced activity, early pupal lethality
C479F
-
naturally occuring mutation
D261N
-
naturally occuring mutation, the mutant activity is slightly reduced compared to the wild-type enzyme
D303N
-
naturally occuring mutation, the mutant activity is reduced by 60% compared to the wild-type enzyme
D519H
-
inactivated lectin domain
E119V
-
naturally occuring mutation, the mutant activity is slightly increased compared to the wild-type enzyme
E341D
-
naturally occuring mutation
G272R
-
naturally occuring mutation, the mutant activity is slightly reduced compared to the wild-type enzyme
G3E
-
naturally occuring mutation, the mutant activity is slightly reduced compared to the wild-type enzyme
G46R
-
naturally occuring mutation, the mutant activity is unaltered compared to the wild-type enzyme
GalNAc-T2 lectin domain
Q10471, Q10472, Q8N4A0, Q8NCW6
amino acids 405 to 578 of GalNAc-T2, lower expression level than full-length enzyme
GalNAc-T2-D224H
Q10471, Q10472, Q8N4A0, Q8NCW6
mutation in DXH nucleotide-binding motif, inactive mutant
GalNAc-T2-D458H
Q10471, Q10472, Q8N4A0, Q8NCW6
mutation in CLD motif of alpha repeat, impaired lectin-mediated MUC1 and GalNAc-MUC1 binding, no impaired specific activity, incorporates 1-2 fewer GalNAc residues per substrate molecule in endpoint reactions, no utilization of partially GalNAc-glycosylated peptides, higher KM for IgA hinge-4GalNAc
GalNAc-T2-D541A
Q10471, Q10472, Q8N4A0, Q8NCW6
mutation in CLD motif of gamma repeat
GalNAc-T4 lectin domain
Q10471, Q10472, Q8N4A0, Q8NCW6
amino acids 432 to 571 of GalNAc-T4, lower expression level than full-length enzyme
GalNAc-T4 lectin domain-D459H
Q10471, Q10472, Q8N4A0, Q8NCW6
mutation in CLD motif of alpha repeat
GalNAc-T4-D459H
Q10471, Q10472, Q8N4A0, Q8NCW6
mutation in CLD motif of alpha repeat, impaired lectin-mediated MUC1 and GalNAc-MUC1 binding
hT10
-
GalNAc-T10, lacking transmembrane domain (AA1-70)
hT10CD
-
GalNAc-T10 catalytic domain, hT10 lacking lectin domain (AA446-603) and transmembrane domain (AA1-70), no altered preference in glycosylation site selection, loss of initial burst phase during glycosylation of MUC5AC-13 at Thr-9, gain of initial burst phase during glycosylation of MUC5AC-3 at Thr-9, GalNAc-transfer accompanied by high rate of UDP-GalNAc hydrolysis, lectin domain not required for catalysis, no glycosylation of MUC5AC-9
hT10CD-hT2LD
-
GalNAc-T10 catalytic domain-GalNAc-T2 lectin domain, hT10 lacking lectin domain (AA446-603) and transmembrane domain (AA1-70) fused to hT2 lectin domain, no glycosylation of MUC5AC-9
hT2
-
GalNAc-T2, lacking transmembrane domain (AA1-74)
hT2CD
-
GalNAc-T2 catalytic domain, hT2 lacking lectin domain (AA441-571) and transmembrane domain (AA1-74), reduced affinity for substrate MUC5AC-13 but not for MUC5AC-3, shift of preferred MUC5AC-3 glycosylation site from Thr-9 to Thr-13
R297W
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naturally occuring mutation, the mutant activity is reduced by about 95% compared to the wild-type enzyme
R373H
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naturally occuring mutation, the mutant activity is reduced by about 97% compared to the wild-type enzyme
R382H
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naturally occuring mutation, the mutant activity is almost completely inactive
R552K
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naturally occuring mutation, the mutant activity is unaltered compared to the wild-type enzyme
T491M
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naturally occuring mutation, the mutant activity is reduced by about 98% compared to the wild-type enzyme
Y395X
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naturally occuring mutation, the mutant activity is inactive
D155N
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ppGaNTase-T1 mutant with wild type level of enzyme activity, expression in COS7 cells is markedly compromised
D156Q
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ppGaNTase-T1 mutant without enzyme activity
D209A
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ppGaNTase-T1 mutant without enzyme activity
D209E
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ppGaNTase-T1 mutant with very low enzyme activity
D209N
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ppGaNTase-T1 mutant without enzyme activity
D310N
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ppGaNTase-T1 mutant with 2% of enzyme activity
D375A
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ppGaNTase-T1 mutant with little effect on enzyme activity
D375N
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ppGaNTase-T1 mutant with little effect on enzyme activity
delta/delta
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mice homozygous for ppGalNAcT-1delta allele
E127Q
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ppGaNTase-T1 mutant with less than 1% of enzyme activity
E150Q
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ppGaNTase-T1 mutant with wild type level of enzyme activity
E213Q
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ppGaNTase-T1 mutant with less than 1% of enzyme activity
E319Q
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ppGaNTase-T1 mutant without enzyme activity
E322Q
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ppGaNTase-T1 mutant with 1% of enzyme activity
E376Q
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ppGaNTase-T1 mutant with little effect on enzyme activity
H125F
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active ppGaNTase-T1 mutant, near 3fold greater activity than wild type enzyme
H125Q
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active ppGaNTase-T1 mutant
H211D
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ppGaNTase-T1 mutant without enzyme activity
H341A
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ppGaNTase-T1 mutant with little effect on enzyme activity
H341K
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ppGaNTase-T1 mutant with little effect on enzyme activity
H341L
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ppGaNTase-T1 mutant with little effect on enzyme activity
H341R
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ppGaNTase-T1 mutant with little effect on enzyme activity
N320A
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ppGaNTase-T1 mutant with little effect on enzyme activity
ppGalNAcT-1delta
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allele in transgenic mice that lacks exon 3 and enzymatic activity, crossed into C57BL/6NHsd background
wt/delta
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mice heterozygous for ppGalNAcT-1delta allele
D444A
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GalNAc-T1 mutant with severely impaired apomucin glycosylation, D444A/D484A/D525A triple mutant has significantly lower activity than D444A single mutant
F303L
Q10473
mutant of 40% activity relative to truncated wild-type using apomucin as acceptor substrate and of increased KM for both substrates
F325L
Q10473
mutant of 60% activity relative to truncated wild-type using apomucin as acceptor substrate
F468A
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GalNAc-T1 mutant with strongly reduced activity and decreased expression
P-T1-delta42
Q10473
truncated GalNAc-T1 wild-type, deletion of the coding sequence for the cytoplasmic tail and the transmembrane domain, cDNA for insulin signal sequence and protein A IgG-binding domain fused to the 5-end
W316A
Q10473
inactive mutant using apomucin as acceptor substrate
W316F
Q10473
mutant of 20% activity relative to truncated wild-type using apomucin as acceptor substrate and of increased KMs for apomucin, UDP-GalNAc, and synthetic peptides, PPDAATAAPL and GVVPTVVPG
W316L
Q10473
background level activity relative to truncated wild-type using apomucin as acceptor substrate
W316Y
Q10473
mutant of 40% activity relative to truncated wild-type using apomucin as acceptor substrate and of increased KMs for apomucin, UDP-GalNAc, and synthetic peptides, PPDAATAAPL and GVVPTVVPG
W328A
Q10473
inactive mutant using apomucin as acceptor substrate, low expression level
W328F
Q10473
inactive mutant using apomucin as acceptor substrate
W328L
Q10473
inactive mutant using apomucin as acceptor substrate
W328Y
Q10473
inactive mutant using apomucin as acceptor substrate
Y302L
Q10473
mutant of 80% activity relative to truncated wild-type using apomucin as acceptor substrate
Y309L
Q10473
mutant of 40% activity relative to truncated wild-type using apomucin as acceptor substrate and of increased KM for both substrates
AA93-563
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abbreviated as sGalntl-1, N-terminal transmembrane domain replaced by the Chordin N-terminal leader peptide followed by Flag-tag, no enhanced secretion compared to wild-type, altered activity in Xenopus embryo, no interference with binding of ActRII-B to type I TGFbeta receptor proteins
L195stop
Q8MVS5
3775 mutant, more than half of the putative catalytic region is eliminated, early pupal lethality
additional information
Q8MVS5
development of pgant35A mutant germ line clones arrests to 88% during embryogenesis, does not reach pupation, pgant35A mutant phenotype less severe and 7% rescue of lethality upon trachea-specific expression of PGANT35A wild-type, severity of phenotypes of transgenic flies correlates with molecular and biochemical characterization of the severity of the mutant allele
hT2CD-hT10LD
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GalNAc-T2 catalytic domain-GalNAc-T10 lectin domain, hT2 lacking lectin domain (AA441-571) and transmembrane domain (AA1-74) fused to hT10 lectin domain, partially restored glycosylation to Thr-3 on MUC5AC-13 but not to Thr-13 on MUC5AC-3 or Ser-5 on MUC5AC-3,13
additional information
Q8N4A0
linkage analysis of GalNAc-T4 with the base pair G1516A substitution
additional information
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identification of somatic and germ-line mutations in GALNT12 in individuals with colon cancer, each of the 8 GALNT12 mutations identified inactivates the normal function of the GALNT enzyme in initiating mucin type O-linked protein glycosylation, overview
H341V
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ppGaNTase-T1 mutant with little effect on enzyme activity
additional information
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ppGalNAc-T13 deficient mice with decrease in Tn antigen expression in the cerebellum
additional information
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mutations in the C-terminal 128-amino acid ricin-like lectin motif of ppGaNTase-T1 do not alter its catalytic properties
additional information
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generation of Galnt1 null mice, that show reduced glycosylation of bone sialoprotein and osteopontin Ser and Thr residues speficially glycosylated by isozyme ppGalNAcT-1, overview
G455Q
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GalNAc-T1 mutant with reduced reactivity towards apomucin
additional information
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site-directed mutagenesis at the C-terminus and its deletion inactivates GalNAc-T1, probably caused by conformational changes in the (QXW)3 repeats, deletion of the lectin domain results in complete loss of activity
additional information
Q10473
all point mutants are mutants of the truncated wild-type P-T1-delta42 and were generated by site-directed mutagenesis on pInsProAdelta42
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
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enzyme will be useful for the in vitro glycosylation of proteins obtained from microorganisms by gene manipulation techniques
drug development
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further studies of the substrate specificity of these and potentially additional enzymes are required, but it may be anticipated that this understanding will be significant for insight into O-glycosylation processing and of practical use, for example, for designing appropriate mammalian expression systems for recombinant glycoproteins in drug use, further studies of the substrate specificity of these and potentially additional enzymes are required, but it may be anticipated that this understanding will be significant for our insight into O-glycosylation processing and of practical use, for example, for designing appropriate mammalian expression systems for recombinant glycoproteins in drug use
medicine
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cancer cells compared to normal cells exhibit altered glycosyltransferase activities, enzyme is a new tool for the investigation of motif peptide O-glycosylation alterations in pathological situations
molecular biology
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enzyme-linked lectin assay (ELLA) as carbohydrate-binding assay
molecular biology
Q96FL9
polyclonal rabbit anti-GalNAc-T14 IgG (1: 1000 in Western blot, titer: appr. 1: 16000) for study of expression and distribution of human GalNAc-T14
molecular biology
Q10473
invariant residue Trp328 is essential for GalNAc-T enzymatic activity, residue Trp316 is important in the interaction with the acceptor polypeptide of GalNAc-T1
molecular biology
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overexpression in eukaryotic cell culture leads to inhibition of Activin/Nodal pathway activity in vivo by interference with binding of ActR-IIB to type I TGFbeta receptor proteins that can mediate BMP as well as Nodal signalling