2.4.1.38: beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
This is an abbreviated version!
For detailed information about beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.38
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2.4.1.38
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galts
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galactosylate
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synthesis
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alpha-lactalbumin
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p34cdc2-related
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beta4galts
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drug development
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pharmacology
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medicine
- 2.4.1.38
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galts
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galactosylate
- synthesis
- alpha-lactalbumin
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p34cdc2-related
- beta4galts
- drug development
- pharmacology
- medicine
Reaction
Synonyms
(alpha4Gal-T1), 4betaGalT, acetyllactosamine synthetase, alpha-1,4-galactosyltransferase I, B4GALT1, beta 1, 4-GalT-I, beta 1,4-galactosyltransferase 1, beta 1,4-GalT-I, beta 1,4GalT V, beta(1,4)-galactosyltransferase, beta(1,4)-GalT, beta(1,4)-GT, beta-1,4 galactosyltransferase I, beta-1,4 galactosyltransferase V, beta-1,4-galactosyltransferase, beta-1,4-galactosyltransferase 1, beta-1,4-galactosyltransferase I, beta-1,4-galactosyltransferase IV, beta-1,4-galactosyltransferase-I, beta-1,4-GalT, beta-1,4-GalT I, beta-1,4-GalT V, beta-1,4-GalT-I, beta-1,4-GalT5, beta-1,4-GalT6, beta-1,4-GalT7, beta-1,4-GT-IV, beta-N-acetyl-beta1-4-galactosyltransferase, beta-N-acetylglucosaminide beta1-4-galactosyltransferase, beta1,4-Gal-transferase T1, beta1,4-galactosyltransferase, beta1,4-galactosyltransferase 1, beta1,4-galactosyltransferase 7, beta1,4-galactosyltransferase I, beta1,4-galactosyltransferase II, beta1,4-galactosyltransferase V, beta1,4-galactosyltransferase-1, beta1,4-galactosyltransferase-I, beta1,4-galactosyltransferase1, beta1,4-GalT1, beta1,4-GalT7, beta1,4-GT, beta1,4-GT 1, beta1,4GalT II, beta1,4GT1, beta1-4-galactosyltransferase, beta1-4GalT, beta1-4GalT1, beta4 Gal-transferase, beta4-GalT-I, beta4-GalT-II, beta4-GalT-III, beta4-GalT-IV, beta4-GalT-V, beta4Gal-T1, beta4GalT, beta4GalT-II, beta4GalT1, beta4GalT7, betaGalT, betaGalT-1, betaGALT1, betaGT, EC 2.4.1.98, Gal-T, Gal-T1, galactosyltransferase 7, galactosyltransferase, uridine diphosphogalactose-acetylglucosamine, GalNAcT2, GALT, GalT I, GalT V, GalT1, GalTase, GalTI, glycoprotein 4-beta-galactosyl-transferase, glycoprotein beta-galactosyltransferase, HP0826, lactosamine synthase, lactosamine synthetase, lactose synthetase A protein, LgtB, LgtB-A, LgtB-B, LgtH, More, N-acetylglucosamine beta1,4 galactosyltransferase, N-acetyllactosamine synthetase, NAL synthetase, thyroid galactosyltransferase, thyroid glycoprotein beta-galactosyltransferase, UDP-beta-1,4-galactosyltransferase, UDP-Gal:betaGlcNAc beta-1,4-galactosyltransferase, polypeptide 1, UDP-Gal:N-acetylglucosamine beta1-4-galactosyltransferase, UDP-galactose N-acetylglucosamine beta-4-galactosyltransferase, UDP-galactose-acetylglucosamine galactosyltransferase, UDP-galactose-N-acetylglucosamine beta-1,4-galactosyltransferase, UDP-galactose-N-acetylglucosamine galactosyltransferase, UDP-galactose:N-acetylglucosaminide beta1-4-galactosyltransferase, UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase 2, UDPgalactose-glycoprotein galactosyltransferase, UDPgalactose-N-acetylglucosamine beta-D-galactosyltransferase, UDPgalactose:N-acetyl-beta-D-glucosaminylglycopeptide beta-1,4-galactosyltransferase, UDPgalactose:N-acetylglucosaminyl(beta1-4)galactosyltransferase, uridine diphosphogalactose-acetylglucosamine galactosyltransferase, uridine diphosphogalactose-glycoprotein galactosyltransferase
ECTree
2.4.1.38 beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.1.38 - beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D320A
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when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme
D320E
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when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme
D320N
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when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme
E317A
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when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme
E317D
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when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme
E317Q
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when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme
H347D
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in presence of Mn2+ retains 0.02% of wild-type enzyme activity, in presence of Co2+ retains 0.085% of wild-type enzyme activity
H347E
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in presence of Mn2+ retains 0.1% of wild-type enzyme activity, in presence of Co2+ retains 0.4% of wild-type enzyme activity
H347N
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in presence of Mn2+ retains 0.07% of wild-type enzyme activity, in presence of Co2+ retains 0.36% of wild-type enzyme activity
H347Q
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in presence of Mn2+ retains 0.28% of wild-type enzyme activity, in presence of Co2+ retains 1.21% of wild-type enzyme activity
M344A
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in presence of Mn2+ retains 54.5% of wild-type enzyme activity, in presence of Co2+ retains 6.15% of wild-type enzyme activity
M344H
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site-directed mutagenesis, substrate binding structure in comparison to the wild-type enzyme, overview
M344Q
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in presence of Mn2+ retains 15.37% of wild-type enzyme activity, in presence of Co2+ retains 31.08% of wild-type enzyme activity
R228K
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mutant enzyme shows 16% of the wild-type galactosyltransferase activity, mutation results in a 15fold higher glucosyltransferase activity, which is further enhanced by alpha-lactalbumin to nearly 25% of the galactosyltransferase activity of the wild type. The main effect of the mutation is on the kcat of glucosyltransferase, which increases 3-4fold, both in the absence and in the presence of alpha-lactalbumin simultaneously, the kcat for the galactosyltransferase reaction is reduced 30fold
Y289I
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mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type
Y289L
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mutation enhances GalNAc-transferase activity. Km for GlcNAc is incereased compared to the wild type
Y289N
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mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type
I289Y
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mutation of the Drosophila beta4GalNAc-T1 converts the enzyme to a beta-1,4-galactosyltransferase-1, beta4Gal-T1, by reducing its beta4GalNAc-T1 activity by nearly 1000fold while enhancing its beta4Gal-T1 activity by 80fold
M340H
site-directed mutagenesis, substrate binding structure in comparison to the wild-type enzyme, overview
M344H
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in the presence of Mg2+ the mutant exhibits 25% of the catalytic activity compared to the wild type enzyme in the presence of Mn2+. Although the mutant has higher Km in the presence of Mg2+ for the substrates compared to the wild type enzyme in the presence of Mn2+, the catalytic efficiency with respect to donor and acceptor has decreased by an order of about 13 and 6, respectively. The turnover number of the mutant is only reduced to 60%
R228K
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the mutation enhances the glucosyltransferase activity of beta4GalNAc-T1, which is low for the wild-type enzyme, by steric alterations, overview
W312C/P401C
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site-directed mutagenesis, the mutations facilitate invitro folding of the recombinantly expressed enzyme
W312C/P401C/M340H
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site-directed mutagenesis, substrate binding structure in comparison to the wild-type enzyme, overview
Y268G
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site-directed mutagenesis, the mutant enzyme is less active compared to the wild-type enzyme
Y268G/Y294G
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site-directed mutagenesis, the mutant enzyme is less active compared to the wild-type enzyme
Y285I
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site-directed mutagenesis, the mutation converts the betaGALT1 enzyme into an equally efficient beta4GalNAc-T1, EC 2.4.1.90
Y285L
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site-directed mutagenesis, the mutation converts the betaGALT1enzyme into an equally efficient beta4GalNAc-T1, EC 2.4.1.90
Y289I
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the mutation makes the enzyme equally as efficient as Gal- or GalNAc-transferase
Y289L
Y289L/C342T
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site-directed mutagenesis, the mutant is able to transfer GalNAc from the sugar donor UDP-GalNAc to the acceptor, GlcNAc, with efficiency as good as that of galactose from UDP-Gal, in contrast to the wild-type enzyme, mutant substrate specificity with different donor substrate and oligosaccharides as acceptor substrates, mass spectrometry product analysis, overview, the C342T mutation does not alter enzyme activity, but increases the enzyme stability at room temperature
Y289N
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the mutation makes the enzyme equally as efficient as Gal- or GalNAc-transferase
Y294G
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site-directed mutagenesis, the mutant enzyme is less active compared to the wild-type enzyme
additional information
Y289L
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mutation of the beta4GalNAc-T1 converts the enzyme to a beta-1,4-galactosyltransferase-1, beta4Gal-T1. Substituting Tyr289 for Leu removes this restriction and the Tyr289Leu mutant can now transfer GalNAc or other Gal C2-analogues from their respective UDPderivatives, not normally substrates of the enzyme, to the acceptor GlcNAc with the same efficiency with which the wild-type enzyme transfers Gal from UDP-Gal, phenotype, overview
Y289L
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the mutation makes the enzyme equally as efficient as Gal- or GalNAc-transferase
additional information
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N-terminal truncated forms of the enzyme between residues 1-129, do not show any significant difference in the apparent Km-values towards N-acetylglucosamine or linear oligosaccharide acceptors, e.g. for chitobiose and chitotriose, or for the nucleotide donor UDPgalactose. The binding behaviour of N-terminal and C-terminal fragments of the enzyme towards the N-acetylglucosamine-agarose and UDP-agarose columns differ, the former binds preferentially to the N-acetylglucosamine-columns, while the latter binds to UDP-agarose columns via Mn2+
additional information
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covalent immobilization of the enzyme in the absence of alpha-lactalbumin for use as biocatalyst, method evaluation, overview
additional information
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knockdown of zebrafish beta-4GalT1 by two independent morpholino oligonucleotides results in embryos with a truncated anterior-posterior axis, as well as elongated somites and moderate defects in the patterning of the head mesenchyme, phenotype with the axial mesoderm of epiboly stage embryos being abnormally widened in beta-4GalT1 morphants, indicative of abnormal convergent extension, laminin isolated from beta-4GalT1 morphant embryos is poorly galactosylated, activity is restored by injection of wild-type enzyme mRNA, overview
additional information
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autophosphorylation of epidermal growth factor receptor, EGFR, and phosphorylation of protein kinase B, PKB/Akt, and extracellular signalregulated protein kinase1/2,ERK1/2, which are downstream molecules of EGFR, are reduced in cell surface beta1,4GT1-overexpressing SMMC-7721 cells, phenotype, overview, knockdown of beta1,4GT1 by siRNA increases the autophosphorylation of EGFR at Tyr1068
additional information
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RNAi-mediated knockdown of beta1,4-GT 1 inhibits CDK11(p58)-mediated apoptosis induced by cycloheximide, while ectopically expressed beta1,4-GT 1 increases CDK11p58-mediated apoptosis, enzyme knockout also inhibits the release of cytochrome c from mitochondria and caspase-3 processing, mechanism of beta1,4-GT 1 in CHX-induced apoptosis of CDK11p58-overexpressing cells, overview
additional information
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beta 1,4GalT V antisense constructs interfere with beta 1,4GalT V leading to promotion of As2O3-induced glioma cell apoptosis, while overexpression of beta 1,4GalT V inhibits it, overview
additional information
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introduction of human betaGalT into suspension cultured tobacco cells results in the production of recombinant proteins with galactose-extended glycans and decreased contents of beta(1,2)-xylose and alpha(1,3)-fucose
additional information
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expression vectors bearing the luminal domains of beta4GalT-II and glucuronyltransferase show in GST-pulldown assays that the Golgi luminal domains are sufficient for the complex to form
