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Information on EC 2.4.1.41 - polypeptide N-acetylgalactosaminyltransferase and Organism(s) Bos taurus and UniProt Accession Q07537
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2.4.1.41 polypeptide N-acetylgalactosaminyltransferaseIUBMB Comments
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.
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Word Map
- 2.4.1.41
-
o-glycosylation
-
mucin-type
- mucin
- glycosyltransferase
- o-glycans
-
o-linked
- threonine
- gangliosides
- lectin
- calcinosis
- oligosaccharide
- metastasis
- calcification
-
hyperphosphatemic
- gm2
-
galactosyltransferase
- glycolipids
-
1,25-dihydroxyvitamin
-
phosphaturic
- gd1a
-
sialyltransferase
-
submaxillary
-
angptl3
-
mucin-like
- klotho
- hyperostosis
- muc5ac
-
factor-23
- apomucin
- analysis
- drug development
-
lutropin
-
asn-linked
- molecular biology
-
periarticular
- medicine
-
o-glycoproteins
- iga1
- villosa
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
=
+
+
=
+
Synonyms
galnt3, n-acetylgalactosaminyltransferase, galnt2, galnac-t3, galnac-t, galnt14, galnac-transferase, galnac transferase, galnac-t2, galnac-t1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase
abbreviated as ppGalNAc T
acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-glycoprotein
-
-
-
-
GalNAc-transferase
glycoprotein acetylgalactosaminyltransferase
-
-
-
-
polypeptide-N-acetylgalactosamine transferase
-
-
-
-
ppGalNAc T1
ppGalNAc-T
ppGaNTase
protein-UDP acetylgalactosaminyltransferase
-
-
-
-
UDP-acetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
-
-
-
-
UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase
-
-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
-
-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
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-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:protein N-acetylgalactosaminyl transferase
-
-
-
-
uridine diphosphoacetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
-
-
-
-
additional information
-
the enzyme belongs to the large family of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases, ppGalNAc Ts
GalNAc-transferase
-
-
-
-
ppGalNAc-T
-
-
-
-
ppGaNTase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-galactosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-alpha-D-galactosaminyl)-L-serine
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
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
9075-15-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-GalNAc + GAGA(X)5T(X)5AGAGK
UDP + GAGA(X)5(GalNAc)T(X)5AGAGK
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
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-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-GalNAc + AQPTPPP
UDP + AQP-(GalNAcalpha1-)TPPP
-
pH 7.5, 37°C, 0.2 mM, 100% activity
-
-
?
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
-
pH 7.5, 37°C
-
-
?
UDP-GalNAc + PTTTPITTTG
UDP + P-(GalNAcalpha1-)TTTPITTTG + P-(GalNAcalpha1-)TTTPI-(GalNAcalpha1-)TTTG
-
pH 7.5, 37°C, 0.2 mM, 26% activity relative to AQPTPPP
-
-
?
UDP-GalNAc + TPTGTQTPTG
UDP + TPTG-(GalNAcalpha1-)TQTPTG
-
pH 7.5, 37°C, 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 + ?
-
pH 7.5, 37°C, 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
-
pH 7.5, 37°C, 0.2 mM, 145% activity relative to AQPTPPP
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Ac-Pro-Thr-Thr-Thr-Pro-Ile-Ser-Thr-NH2
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPIV
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPIV
-
preferred substrate
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPV
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPV
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPV-C
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPV-C
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Pro-Pro-Ala-Ser-Thr-Ser-Ala-Pro-Gly
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Pro-Pro-Asp-Ala-Ala-Ser-Ala-Ala-Pro-Leu-Arg
?
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + AcTPPP
UDP + N-acetyl-D-galactosaminyl-AcTPPP
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + myelin basic protein
UDP + N-acetyl-D-galactosaminyl-myelin basic protein
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PHMAQVTVGPGL
UDP + N-acetyl-D-galactosaminyl-PHMAQVTVGPGL
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + PPDAATAAPLR
UDP + N-acetyl-D-galactosaminyl-PPDAATAAPLR
-
i.e. EPO-T peptide
-
-
?
UDP-N-acetyl-D-galactosamine + rhodanese
UDP + N-acetyl-D-galactosaminyl-rhodanese
-
reduced and carboxylmethylated bovine rhodanese, at a lower rate than with myelin basic protein
-
-
?
UDP-N-acetyl-D-galactosamine + subtilisin
UDP + N-acetyl-D-galactosaminyl-subtilisin
-
reduced and carboxylmethylated bacterial subtilisin, at a lower rate than with myelin basic protein or bovine rhodanese
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
bovine apomucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
deglycosylated bovine submaxillary mucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
best substrate, poorer substrates: asialo mucin, native mucin
-
-
?
UDP-N-acetyl-D-galactosamine + kappa-casein
UDP + N-acetyl-D-galactosaminyl-kappa-casein
-
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
-
-
?
UDP-N-acetyl-D-galactosamine + kappa-casein
UDP + N-acetyl-D-galactosaminyl-kappa-casein
-
glycosylation of kappa-casein occurs after casein micelle formation triggered by the accumulation of Ca2+ in vivo
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
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
-
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
-
acceptor: deglycosylated bovine submaxillary mucin
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
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
-
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
-
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
-
only UDP-GalNAc serves as sugar donor
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptors: synthetic peptides
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptors: apomucin, kappa-casein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
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
-
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
-
key role in O-linked glycosylation, catalyzes first step in the assembly
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
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
-
catalyzes in vivo glycosylation of both threonine and serine
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
initial step of mucin-type O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
post-translational, initial reaction in O-linked oligosaccharide biosynthesis
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
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
-
?
additional information
?
-
-
not: alphaS1-casein, alphaS2-casein, beta-casein, alpha-lactalbumin, beta-lactoglobulin, bovine serum albumin
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + kappa-casein
UDP + N-acetyl-D-galactosaminyl-kappa-casein
-
glycosylation of kappa-casein occurs after casein micelle formation triggered by the accumulation of Ca2+ in vivo
-
-
?
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
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
key role in O-linked glycosylation, catalyzes first step in the assembly
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
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
-
catalyzes in vivo glycosylation of both threonine and serine
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
initial step of mucin-type O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
post-translational, initial reaction in O-linked oligosaccharide biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mn2+
-
in coordination both with the phosphates of UDP and the DXH motif of the enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alphaS1-casein
-
strong inhibition of GalNAc transfer to kappa-casein, reversed by Ca2+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
Ac-Pro-Thr-Thr-Thr-Pro-Ile-Ser-Thr-NH2
-
derived from the MUC2 repeat sequence
3.3
Arg-Thr-Pro-Pro-Pro
-
derived from the major acceptor sequence in myelin basic protein
additional information
additional information
-
Km: 2.5 mg/ml: deglycosylated bovine submaxillary mucin
-
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: 0.192 mg/ml: apomucin, 1.15 mg/ml: kappa-subcomponent 1, 5.1 mg/ml: kappa-subcomponent 7
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cis-Golgi apparatus and smooth-membraned vesicular structures in close topological relation with it
additional information
-
type II membrane protein containing a 23-amino acid transmembrane domain and an 8-amino acid cytoplasmic tail
-
soluble, secreted enzyme is prepared by substituting the honeybee melittin leader sequence for the sequences coding for the cytoplasmic and membrane spanning domains
-
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
-
additional information
-
intracellular membrane-bound enzyme, localized in the secretory pathway
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GALT1_BOVIN
559
1
64192
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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
-
residues Asn-95 and Asn-552 of the recombinant enzyme are occupied by N-linked sugars in Cos7 cells
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble His-tagged enzyme from Cos-7 cells, purification from the medium
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
-
enzyme will be useful for the in vitro glycosylation of proteins obtained from microorganisms by gene manipulation techniques
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takeuchi, M.; Yoshikawa, M.; Sasaki, R.; Chiba, R.
Purification and characterization of UDP-N-acetylgalactosamine:kappa-casein polypeptide N-acetylgalactosaminyltransferase from mammary gland of lacting cow
Agric. Biol. Chem.
49
1059-1069
1985
Bos taurus
-
Elhammer, A.; Kornfeld, S.
Purification and characterization of UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells
J. Biol. Chem.
261
5249-5255
1986
Bos taurus, Mus musculus
Briand, J.P.; Andrews, S.P.; Cahill, E.; Conway, N.A.; Young, J.D.
Investigation of the requirements for O-glycosylation by bovine submaxillary gland UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosamine transferase using synthetic peptide substrates
J. Biol. Chem.
256
12205-12207
1981
Bos taurus
Homa, F.L.; Baker, C.A.; Thomsen, D.R.; Elhammer, A.P.
Conversion of a bovine UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase to a soluble, secreted enzyme, and expression in Sf9 cells
Protein Expr. Purif.
6
141-148
1995
Bos taurus
Brockhausen, I.; Toki, D.; Brockhausen, J.; Peters, S.; Bielfeldt, T.; Kleen, A.; Paulsen, H.; Meldal, M.; Hagen, F.; Tabak, L.A.
Specificity of O-glycosylation by bovine colostrum UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase using synthetic glycopeptide substrates
Glycoconj. J.
13
849-856
1996
Bos taurus
Elhammer, A.P.; Poorman, R.A.; Brown, E.; Maggiora, L.L.; Hoogerheide, J.G.; Kezdy, F.J.
The specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase as inferred from a database of in vivo substrates and from the in vitro glycosylation of proteins and peptides
J. Biol. Chem.
268
10029-10038
1993
Bos taurus
Wragg, S.; Hagen, F.K.; Tabak, L.A.
Identification of essential histidine residues in UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1
Biochem. J.
328
193-197
1997
Bos taurus
-
Wragg, S.; Hagen, F.K.; Tabak, L.A.
Kinetic analysis of a recombinant UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
J. Biol. Chem.
270
16947-16954
1995
Bos taurus
Roth, J.; Wang, Y.; Eckhardt, A.E.; Hill, R.L.
Subcellular localization of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland
Proc. Natl. Acad. Sci. USA
91
8935-8939
1994
Bos taurus, Sus scrofa
Homa, F.L.; Hollander, T.; Lehman, D.J.; Thomsen, D.R.; Elhammer, A.P.
Isolation and expression of a cDNA clone encodinh a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
J. Biol. Chem.
268
12609-12616
1993
Bos taurus (Q07537), Bos taurus
Hagen, F.K.; vanWyckhuyse, B.; Tabak, L.A.
Purification, cloning, and expression of a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
J. Biol. Chem.
268
18960-18965
1993
Bos taurus (Q07537), Bos taurus
Duclos, S.; Da Silva, P.; Vovelle, F.; Piller, F.; Piller, V.
Characterization of the UDP-N-acetylgalactosamine binding domain of bovine polypeptide alphaN-acetylgalactosaminyltransferase T1
Protein Eng. Des. Sel.
17
635-646
2004
Bos taurus
Gerken, T.A.; Hagen, K.G.; Jamison, O.
Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase orthologue pairs
Glycobiology
18
861-870
2008
Bos taurus (Q07537), Homo sapiens (Q10471), Drosophila melanogaster (Q6WV17), Drosophila melanogaster (Q6WV19)
Brockhausen, I.; Dowler, T.; Paulsen, H.
Site directed processing: role of amino acid sequences and glycosylation of acceptor glycopeptides in the assembly of extended mucin type O-glycan core 2
Biochim. Biophys. Acta
1790
1244-1257
2009
Bos taurus, Homo sapiens (Q10472)
Perrine, C.L.; Ganguli, A.; Wu, P.; Bertozzi, C.R.; Fritz, T.A.; Raman, J.; Tabak, L.A.; Gerken, T.A.
Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2
J. Biol. Chem.
284
20387-20397
2009
Bos taurus, Homo sapiens
Gerken, T.A.; Revoredo, L.; Thome, J.J.; Tabak, L.A.; Vester-Christensen, M.B.; Clausen, H.; Gahlay, G.K.; Jarvis, D.L.; Johnson, R.W.; Moniz, H.A.; Moremen, K.
The lectin domain of the polypeptide GalNAc transferase family of glycosyltransferases (ppGalNAc Ts) acts as a switch directing glycopeptide substrate glycosylation in an N- or C-terminal direction, further controlling mucin type O-glycosylation
J. Biol. Chem.
288
19900-19914
2013
Bos taurus, Homo sapiens
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