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2.4.1.41: polypeptide N-acetylgalactosaminyltransferase

This is an abbreviated version!
For detailed information about polypeptide N-acetylgalactosaminyltransferase, go to the full flat file.

Word Map on EC 2.4.1.41

Reaction

UDP-N-acetyl-alpha-D-galactosamine
+
[protein]-L-serine
=
UDP
+
[protein]-3-O-(N-acetyl-alpha-D-galactosaminyl)-L-serine

Synonyms

(UDP)-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-glycoprotein, bgibmga008904, dGalNAc-T3, Eg-ppGalNAc-T1, GalNAc transferase, GalNAc-T, GalNAc-T1, GalNAc-T11, GalNAc-T12, GalNAc-T13, GalNAc-T14, GalNAc-T16, GalNAc-T18, GalNAc-T2, GalNAc-T3, GalNAc-T4, GalNAc-T5, GalNAc-T6, GalNAc-T7, GalNAc-transferase, GalNAc-transferase T1, GalNAc-transferase T2, GalNAcT4, GALNT1, GALNT11, GALNT12, Galnt13, GALNT14, Galnt18, GALNT2, GALNT3, Galnt4, GalNT5, glycopeptide-preferring polypeptide GalNAc transferase 10, glycoprotein acetylgalactosaminyltransferase, More, N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyl-transferase, N-acetylgalactosaminyltransferase, N-acetylgalactosaminyltransferase-like 1, NM_001079884, PGANT, PGANT1, PGANT2, PGANT3, PGANT4, PGANT5, PGANT6, PGANT7, PGANT8, polypeptide GalNAc transferase, polypeptide GalNAc transferase 2, polypeptide GalNAc-transferase, polypeptide GalNAc-transferase 2, polypeptide GalNAc-transferase-2, polypeptide GalNAcT, polypeptide N-acetylgalactosaminyl transferase-3, polypeptide N-acetylgalactosaminyltransferase, polypeptide N-acetylgalactosaminyltransferase 12, polypeptide N-acetylgalactosaminyltransferase 14, polypeptide N-acetylgalactosaminyltransferase 2, polypeptide N-acetylgalactosaminyltransferase 3, polypeptide N-acetylgalactosaminyltransferase 6, polypeptide N-acetylgalactosaminyltransferase-1, polypeptide-N-acetylgalactosamine transferase, polyppetide GalNAc transferase, pp-GalNAc-T13, pp-GalNAc-T15, pp-GalNAc-T2, pp-GaNTase, ppGalNAc T1, ppGalNAc T10, ppGalNAc T13, ppGalNAc T16, ppGalNAc T2, ppGalNAc T3, ppGalNAc T5, ppGalNAc T6, ppGalNAc-T, ppGalNAc-T1, ppGalNAc-T10, ppGalNAc-T12, ppGalNAc-T2, ppGalNAc-T3, ppGalNAc-T4, ppGalNAc-T5, ppGalNAc-T6, ppGalNAcT, ppGalNAcT or hT, ppGaNTase, ppGaNTase-T1, ppGaNTase-T11, ppGaNTase-T12, ppGaNTase-T3, ppGaNTase-T4, ppGaNTase-T5, ppGaNTase-T6, protein-UDP acetylgalactosaminyltransferase, UDP GalNAc:polypeptide N-acetylgalactosaminyltransferase, UDP N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyl transferase, UDP N-acetyl-alpha-Dgalactosamine:polypeptide N-acetylgalactosaminyl transferase, UDP-acetylgalactosamine-glycoprotein acetylgalactosaminyltransferase, UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase, UDP-GalNAc polypeptide:GalNAc transferase-T2, UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase, UDP-GalNAc polypeptides:N-acetyl-alpha-galactosaminyltransferase, UDP-GalNAc transferase, UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase, UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2, UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1, UDP-GalNAc:polypeptide alphaN-acetylgalactosaminyltransferase, UDP-GalNAc:polypeptide GalNAc transferase, UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 18, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, 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, 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, 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, UDP-N-acetylgalactosamine polypeptide: N-acetylgalactosaminyl-transferase, 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, UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase, UDP-N-acetylgalactosamine:protein N-acetylgalactosaminyl transferase, UDP-N-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase, UDP-polypeptide N-acetylgalactosaminyl transferase, uridine diphosphate-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, uridine diphosphoacetylgalactosamine-glycoprotein acetylgalactosaminyltransferase, xGaltnl-1

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.41 polypeptide N-acetylgalactosaminyltransferase

Engineering

Engineering on EC 2.4.1.41 - polypeptide N-acetylgalactosaminyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
L195stop
3775 mutant, more than half of the putative catalytic region is eliminated, early pupal lethality
pgant35A-3775
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
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
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
HG8 mutant, truncated protein within the putative stem region, early pupal lethality
R227W
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
E334Q
the mutant shows strongly reduced activity compared to the wild type enzyme
E341D
naturally occuring mutation
F361A
minimal residual activity
F361S
minimal residual activity
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
H253D
catalytically dead Mn2+ binding site mutant
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
I253A
reduced activity with substrate UDP-GalNAc
I253A/L310A
UDP-GalNAc is a poor substrate, some UDP-GalNAc analogs with longer or branched N-acyl chains are better substrates for mutant I253A/L310A than for wild-type
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
L310A
reduced activity with substrate UDP-GalNAc
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
D155N
-
ppGaNTase-T1 mutant with wild type level of enzyme activity, expression in COS7 cells is markedly compromised
D156Q
-
ppGaNTase-T1 mutant without enzyme activity
D209A
-
ppGaNTase-T1 mutant without enzyme activity
D209E
-
ppGaNTase-T1 mutant with very low enzyme activity
D209N
-
ppGaNTase-T1 mutant without enzyme activity
D310N
-
ppGaNTase-T1 mutant with 2% of enzyme activity
D375A
-
ppGaNTase-T1 mutant with little effect on enzyme activity
D375N
-
ppGaNTase-T1 mutant with little effect on enzyme activity
delta/delta
-
mice homozygous for ppGalNAcT-1delta allele
E127Q
-
ppGaNTase-T1 mutant with less than 1% of enzyme activity
E150Q
-
ppGaNTase-T1 mutant with wild type level of enzyme activity
E213Q
-
ppGaNTase-T1 mutant with less than 1% of enzyme activity
E319Q
-
ppGaNTase-T1 mutant without enzyme activity
E322Q
-
ppGaNTase-T1 mutant with 1% of enzyme activity
E376Q
-
ppGaNTase-T1 mutant with little effect on enzyme activity
H125F
-
active ppGaNTase-T1 mutant, near 3fold greater activity than wild type enzyme
H125Q
-
active ppGaNTase-T1 mutant
H211D
-
ppGaNTase-T1 mutant without enzyme activity
H341A
-
ppGaNTase-T1 mutant with little effect on enzyme activity
H341K
-
ppGaNTase-T1 mutant with little effect on enzyme activity
H341L
-
ppGaNTase-T1 mutant with little effect on enzyme activity
H341R
-
ppGaNTase-T1 mutant with little effect on enzyme activity
H341V
-
ppGaNTase-T1 mutant with little effect on enzyme activity
N320A
-
ppGaNTase-T1 mutant with little effect on enzyme activity
ppGalNAcT-1delta
-
allele in transgenic mice that lacks exon 3 and enzymatic activity, crossed into C57BL/6NHsd background
wt/delta
-
mice heterozygous for ppGalNAcT-1delta allele
D444A
-
GalNAc-T1 mutant with severely impaired apomucin glycosylation, D444A/D484A/D525A triple mutant has significantly lower activity than D444A single mutant
F303L
mutant of 40% activity relative to truncated wild-type using apomucin as acceptor substrate and of increased KM for both substrates
F325L
mutant of 60% activity relative to truncated wild-type using apomucin as acceptor substrate
F468A
-
GalNAc-T1 mutant with strongly reduced activity and decreased expression
G455Q
-
GalNAc-T1 mutant with reduced reactivity towards apomucin
P-T1-delta42
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
inactive mutant using apomucin as acceptor substrate
W316F
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
background level activity relative to truncated wild-type using apomucin as acceptor substrate
W316Y
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
inactive mutant using apomucin as acceptor substrate, low expression level
W328F
inactive mutant using apomucin as acceptor substrate
W328L
inactive mutant using apomucin as acceptor substrate
W328Y
inactive mutant using apomucin as acceptor substrate
Y302L
mutant of 80% activity relative to truncated wild-type using apomucin as acceptor substrate
Y309L
mutant of 40% activity relative to truncated wild-type using apomucin as acceptor substrate and of increased KM for both substrates
AA93-563
-
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
additional information