Information on EC 2.4.1.41 - polypeptide N-acetylgalactosaminyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9HCQ5

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Homo sapiens
UNIPROT: Q9HCQ5


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.41
-
RECOMMENDED NAME
GeneOntology No.
polypeptide N-acetylgalactosaminyltransferase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mucin core 3 and core 4 O-glycosylation
-
-
mucin core 1 and core 2 O-glycosylation
-
-
Mucin type O-glycan biosynthesis
-
-
Metabolic pathways
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9075-15-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
GalNAc-type protein O-glycosylation is important in modulating protein processing, O-linked glycans have important biological functions
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
?
5 UDP-N-acetyl-D-galactosamine + DSTTPAPTTK
5 UDP + N-acetyl-D-galactosaminylated DSTTPAPTTK
show the reaction diagram
erythropoietin T + UDP-Gal
erythropoietin T-nGalNAc + UDP
show the reaction diagram
hCG-beta + UDP-Gal
hCG-beta-nGalNAc + UDP
show the reaction diagram
-
-
-
?
IgA hinge + UDP-Gal
IgA hinge-nGal + UDP
show the reaction diagram
-
-
-
?
IgA hinge + UDP-GalNAc
IgA hinge-nGalNAc + UDP
show the reaction diagram
IgA hinge-4GalNAc + UDP-GalNAc
IgA hinge-nGalNAc + UDP
show the reaction diagram
-
-
-
?
MUC1 + UDP-GalNAc
MUC1-nGalNAc + UDP
show the reaction diagram
MUC1-2GalNAc + UDP-GalNAc
MUC1-nGalNAc + UDP
show the reaction diagram
-
-
-
?
MUC1a' + UDP-GalNAc
MUC1a'-nGalNAc + UDP
show the reaction diagram
-
-
-
?
MUC1b' + UDP-GalNAc
MUC1b'-nGalNAc + UDP
show the reaction diagram
-
-
-
?
MUC2 + UDP-GalNAc
MUC2-nGalNAc + UDP
show the reaction diagram
-
-
-
?
MUC2-6GalNAc + UDP-GalNAc
MUC2-nGalNAc + UDP
show the reaction diagram
-
-
-
?
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
-
-
-
?
OSM fragment + UDP-Gal
OSM fragment-nGalNAc + UDP
show the reaction diagram
-
-
-
?
UDP-galactose + Muc1 peptide
UDP + galactosyl-Muc1 peptide
show the reaction diagram
UDP-galactose + Muc2 peptide
UDP + galactosyl-Muc2 peptide
show the reaction diagram
UDP-galactose + PTTTPITTTTK
UDP + galactosyl-PTTTPITTTTK
show the reaction diagram
UDP-GalNAc + EA2
GalNAc-EA2 + UDP
show the reaction diagram
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
UDP + GAGA(X)3(GalNAc)T(X)3AGAGK
show the reaction diagram
-
-
-
?
UDP-GalNAc + GAGA(X)5T(X)5AGAGK
UDP + GAGA(X)5(GalNAc)T(X)5AGAGK
show the reaction diagram
very high correlation between peptide preferences of ppGalNAc T2 and fly orthologue PGANT2 with r(square) = 0.92
-
-
?
UDP-GalNAc + GAGA(X)nT(X)nAGAGK
GAGA(X)n(GalNAc)T(X)nAGAGK + UDP
show the reaction diagram
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 + HGVTSAPDTRPAPGSTAPPA
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-GalNAc + PTTTPISTTTMVTPTPTPTC
UDP + ?
show the reaction diagram
-
-
-
-
?
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 + polypeptide
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide angiopoietin-like 3
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide angiopoietin-like 3
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide EA2
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide EA2
show the reaction diagram
-
sequence PTTDSTTPAPTTK
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide FGF23
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide FGF23
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPIV
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPIV
show the reaction diagram
-
preferred substrate for isoforms ppGalNAc T2, T5, T13, T14, and T16
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPIV-C
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPIV-C
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPV
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPV
show the reaction diagram
-
preferred substrate for isoforms ppGalNAc T3, T5, T6, T13, and T16
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPV-C
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPV-C
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide Muc1
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide Muc1
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide MUC13
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide MUC13
show the reaction diagram
-
isoform GALNT14 contributes to the glycosylation of peptide MUC13, which is significantly higher in ovarian cancer cells compared with the normal/benign ovary tissues
-
-
?
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 + Ac-CIRIQRGPGRAFVTIGKIGNMR
UDP + N-acetyl-D-galactosaminylated Ac-CIRIQRGPGRAFVTIGKIGNMR
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-PFVTHPGYD
UDP + N-acetyl-D-galactosaminylated Ac-PFVTHPGYD
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-QATEYEYLDYDFLPETEPPEM
UDP + N-acetyl-D-galactosaminylated Ac-QATEYEYLDYDFLPETEPPEM
show the reaction diagram
UDP-N-acetyl-D-galactosamine + AHGVTSAPDTR
UDP + N-acetyl-D-galactosaminylated AHGVTSAPDTR
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-galactosamine + AHGVVTSAPDTR
UDP + ?
show the reaction diagram
UDP-N-acetyl-D-galactosamine + ANTPSFPTATSPAPPI
UDP + ?
show the reaction diagram
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 + CPPTPSATTPAPPSSSAPPETTAA
UDP + N-acetyl-D-galactosaminylated CPPTPSATTPAPPSSSAPPETTAA
show the reaction diagram
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 + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
show the reaction diagram
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
UDP-N-acetyl-D-galactosamine + HIV-V3 peptide
UDP + N-acetyl-D-galactosaminyl-HIV-V3 peptide
show the reaction diagram
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
show the reaction diagram
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 + 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 + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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
-
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTT
UDP + ?
show the reaction diagram
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
mucin derived substrate
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPITTTTTVTPTPTPTGTQT
UDP + ?
show the reaction diagram
UDP-N-acetyl-D-galactosamine + QATEYEYLDYDFLPEC
UDP + N-acetyl-D-galactosaminylated QATEYEYLDYDFLPEC
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-galactosamine + RPAPGSTAPPA
UDP + N-acetyl-D-galactosaminylated RPAPGSTAPPA
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-galactosamine + syndecan-3
UDP + N-acetyl-D-galactosaminyl-syndecan-3
show the reaction diagram
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
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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-alpha-D-galactosamine + polypeptide
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide EA2
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide EA2
show the reaction diagram
-
sequence PTTDSTTPAPTTK
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide Muc1
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide Muc1
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide MUC13
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide MUC13
show the reaction diagram
-
isoform GALNT14 contributes to the glycosylation of peptide MUC13, which is significantly higher in ovarian cancer cells compared with the normal/benign ovary tissues
-
-
?
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 + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
not activated by Mg2+ or Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzyl N-acetyl-alpha-D-galactosamine
-
-
-
benzyl-alpha-GalNAc
-
fully GalNAc-substituted MUC1 repeat peptide
-
inhibits activity of rGalNAc-T4 and -T2
-
GalNAc
HIV-V3
-
competitive inhibition of Muc2 glycosylation
-
methyl-alpha-Gal
-
methyl-beta-Gal
-
Muc2
-
competitive inhibition of HIV-V3 peptide glycosylation
-
N-acetyl-alpha-D-galactosamine
-
the acetylated enzyme is strongly inhibited by N-acetyl-alpha-D-galactosamine
o-nitrophenyl-alpha-GalNAc
-
o-nitrophenyl-beta-GalNAc
-
p-nitrophenyl-alpha-GalNAc
-
p-nitrophenyl-beta-GalNAc
-
phenyl-alpha-GalNAc
-
UDP-alpha-GalNAc
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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 hide
LITERATURE
IMAGE
0.45 - 0.91
AHGVVTSAPDTR
0.01 - 0.48
CPPTPSATTPAPPSSSAPPETTAA
0.07 - 2.19
DSTTPAPTTK
0.067 - 0.344
GTTPSPVPTTSTTSAP
0.115 - 0.46
GTTPSPVPTTST[GalNAc]TSAP
0.035 - 0.332
GT[GalNAc]TPSPVPTTSTTSAP
0.206
GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
-
pH not specified in the publication, 37°C
0.5
HIV-V3 peptide
-
-
-
0.23
human mucin Muc2 peptide
-
-
-
0.01 - 0.02
IgA hinge
-
0.12 - 0.81
IgA hinge-4GalNAc
-
0.15 - 0.36
MUC1
-
0.86 - 0.87
MUC1-2GalNAc
0.07 - 0.23
Muc1a' peptide
-
0.01 - 0.25
Muc2
-
0.062 - 0.066
MUC2-6GalNAc
-
0.018 - 0.02
MUC5AC
0.018 - 0.77
MUC5AC-13
0.033 - 0.107
MUC5AC-3
0.44 - 1
MUC5AC-3,13
2.4
MUC5AC-9
-
at site Thr-2, hT10
0.02 - 0.054
Muc7 peptide
-
0.108 - 0.172
PTTDSTTPAPTTK
1.33
SDC106 peptide
derived from human syndecan-3, ppGalNac-T13
-
0.63
SDC155
derived from human syndecan-3, ppGalNac-T13
-
0.38
SDC165 peptide
derived from human syndecan-3, ppGalNac-T13
-
0.07 - 0.96
SDC284 peptide
-
0.027 - 0.041
UDP-Gal
0.01 - 0.16
UDP-GalNAc
0.016 - 0.081
UDP-N-acetyl-D-galactosamine
additional information
GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 0.193
MUC5AC
0.067 - 0.4
MUC5AC-13
0.04 - 0.33
MUC5AC-3
0.52 - 1.4
MUC5AC-3,13
0.127
MUC5AC-9
-
at site Thr-2, hT10
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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
benzyl N-acetyl-alpha-D-galactosamine
Homo sapiens;
-
acetylated wild type enzyme, at pH 7.4 and 37°C
-
1 - 20
benzyl-alpha-GalNAc
50
D-galactose
Homo sapiens;
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
1 - 37
GalNAc
50
methyl-alpha-Gal
Homo sapiens;
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
40
methyl-beta-Gal
Homo sapiens;
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4
15 - 20
N-acetyl-alpha-D-galactosamine
0.5 - 12
o-nitrophenyl-alpha-GalNAc
1 - 12
o-nitrophenyl-beta-GalNAc
8
ortho-nitrophenyl-beta-GalNAc
Homo sapiens;
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
1 - 10
p-nitrophenyl-alpha-GalNAc
0.8 - 10
p-nitrophenyl-beta-GalNAc
10
para-nitrophenyl-alpha-GalNAc
Homo sapiens;
Q10471, Q10472, Q8N4A0, Q8NCW6
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
1 - 15
phenyl-alpha-GalNAc
30 - 65
UDP-alpha-GalNAc
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
0.5
-
GalNAc-T2 and -T3
0.6
-
GalNAc-T1
0.75
-
purification step 5, Mono S (NaCl)
45
+/-13, UDP-GalNAc by mutant GalNAc-T2-D458H, pH7.4
46
+/-12, UDP-GalNAc by mutant GalNAc-T2-D541A, pH7.4
49
+/-5, IgA hinge-4GalNAc by mutant GalNAc-T2-D541A, pH7.4
56
+/-6, UDP-Gal, pH7.4
65
+/-5, UDP-Gal by mutant GalNAc-T2-D458H, pH7.4
69
+/-12, UDP-GalNAc, pH7.4
72
+/-21, MUC1-2GalNAc, pH7.4
81
+/-1, MUC2, pH7.4
83
+/-13, IgA hinge-4GalNAc, pH7.4
85
+/-5, UDP-Gal by mutant GalNAc-T2-D541A, pH7.4
94
+/-5, MUC1 by mutant GalNAc-T2-D458H, pH7.4
97
+/-14, MUC1, pH7.4
118
+/-39, MUC1-2GalNAc by mutant GalNAc-T2-D541A, pH7.4
119
+/-24, IgA hinge-4GalNAc by mutant GalNAc-T2-D458H, pH7.4
143
+/-15, MUC1 by mutant GalNAc-T2-D541A, pH7.4
145
+/-21, IgA hinge by mutant GalNAc-T2-D541A, pH7.4
150
+/-6, MUC2 by mutant GalNAc-T2-D458H, pH7.4
236
+/-1, IgA hinge by mutant GalNAc-T2-D458H, pH7.4
273
+/-12, MUC2 by mutant GalNAc-T2-D541A, pH7.4
292
+/-18, MUC2-6GalNAc by mutant GalNAc-T2-D541A, pH7.4
302
+/-17, MUC2-6GalNAc, pH7.4
321
+/-18, IgA hinge, pH7.4
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
7.5
-
assay at
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
Northern blot analysis of human tissues
Manually annotated by BRENDA team
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
Northern blot analysis of human tissues
Manually annotated by BRENDA team
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
enzyme form pp-GalNAc-T15
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
-
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
expression detected by Western blot
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
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
Northern blot analysis of human tissues
Manually annotated by BRENDA team
-
colon carcinoma cell line
Manually annotated by BRENDA team
lung small-cell carcinoma cell line
Manually annotated by BRENDA team
Northern blot analysis of human tissues
Manually annotated by BRENDA team
enzyme form pp-GalNAc-T15
Manually annotated by BRENDA team
gastric carcinoma cell line
Manually annotated by BRENDA team
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
ppGalNAc-T13 is abundantly expressed in neuroblastoma cells
Manually annotated by BRENDA team
RCC 7860, expression detected by Western blot
Manually annotated by BRENDA team
immunohistology with a monoclonal antibody shows the expected Golgi-like localization in salivary glands
Manually annotated by BRENDA team
lung small-cell carcinoma cell line
Manually annotated by BRENDA team
-
leukemia cell
Manually annotated by BRENDA team
-
GalNAc-T5 is most abundant in
Manually annotated by BRENDA team
glioblastoma cell line
Manually annotated by BRENDA team
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
Northern blot analysis of human tissues
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
recombinant GalNAc-T1, -T2 and -T3, expressed in Sf9 cells
-
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
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
61000
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
64700
-
cDNA sequence has a 571-amino acid coding region indicating a protein of 64.7 kDa with a type II domain structure
87000
bacterially expressed GST-fusion protein (GST: 26 kDa) detected by anti-GST and anti-GalNAc-T14 antibody; SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 Å) 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 Å) 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
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
24 h, GalNAc-T1 and -T3: 40% loss of activity, GalNAc-T2: 60% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
23% loss of specific activity after 12h shaking at 37°C
25% loss of specific activity after 12 h shaking at 37°C
31% loss of specific activity after 12h shaking at 37°C
mutant GalNAc-T2-D458H: 15% loss of specific activity after 12h shaking at 37°C
mutant GalNAc-T2-D541A: 19% loss of specific activity after 12h shaking at 37°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anti-FLAG m2 affinity chromatography
Co2+-charged resin column chromatography
-
GST fusion protein purified by affinity chromatography, elution with 10 mM glutathione, pH8; GSTrap FF chromatography
immobilized metal ion affinity chromatography (Ni2+)
-
ion exchange chromatography
-
Ni-NTA-agarose column chromatography and MonoQ column 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
ppGalNAc-T14 and -T2, expressed in Sf21 cells
-
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
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
-
SP-Sepharose column chromatography and MonoQ or MonoS column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant human pt-GalNAc-T, which is expressed in insect cells, does not glycosylate several peptides derived from mammalian mucins
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
expressed in COS-7 cells
-
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)
expressed in High Five insect 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, 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 insect cells
-
expressed in Sf9 insect cells Pichia pastoris G115 cells
-
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
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
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 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-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
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
-
soluble His-tagged protein (cytosolic tail and transmembrane domain removed) expressed in Sf9 cells
-
truncated protein expressed in insect cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
extracellular signal-regulated kinase 1/2 inhibitor modulates the expression levels of isoform GALNT14
-
interleukin-8 has no remarkable effect on the expression of isoform GALNT14
-
isoform GalNAc-T3 is highly expressed in papillary carcinomas that have invaded beyond the thyroid capsule
-
isoform GALNT3 is strongly overexpressed in high-grade serous epithelial ovarian tumors as compared to normal ovarian tissue
-
upregulation in SGC-7901 cells inhibits proliferation in vitro
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
E334Q
-
the mutant shows strongly reduced activity 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
amino acids 405 to 578 of GalNAc-T2, lower expression level than full-length enzyme
GalNAc-T2-D224H
mutation in DXH nucleotide-binding motif, inactive mutant
GalNAc-T2-D458H
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
mutation in CLD motif of gamma repeat
GalNAc-T4 lectin domain
amino acids 432 to 571 of GalNAc-T4, lower expression level than full-length enzyme
GalNAc-T4 lectin domain-D459H
mutation in CLD motif of alpha repeat
GalNAc-T4-D459H
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
hT2CD-hT10LD
-
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
K521Q
-
the mutation enhances the carbohydrate specificity of lectin domain for alpha-GalNAc and results in reduced enzyme activity compared to the wild type enzyme
N335A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
N335D
-
the mutant shows strongly reduced activity compared to the wild type enzyme
N335H
-
the mutant shows strongly reduced activity compared to the wild type enzyme
N335S
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R297W
-
naturally occuring mutation, the mutant activity is reduced by about 95% compared to the wild-type enzyme
R362K
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R373H
-
naturally occuring mutation, the mutant activity is reduced by about 97% compared to the wild-type enzyme
R382H
-
naturally occuring mutation, the mutant activity is almost completely inactive
R552K
-
naturally occuring mutation, the mutant activity is unaltered compared to the wild-type enzyme
T491M
-
naturally occuring mutation, the mutant activity is reduced by about 98% compared to the wild-type enzyme
Y395X
-
naturally occuring mutation, the mutant activity is inactive
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
molecular biology