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Information on EC 2.4.1.38 - beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase and Organism(s) Bos taurus and UniProt Accession P08037
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2.4.1.38 beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferaseIUBMB Comments
Terminal N-acetyl-beta-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown towards such residues in branched-chain polysaccharides when these are linked by beta-1,6-links to galactose residues; lower activity towards residues linked to galactose by beta-1,3-links. A component of EC 2.4.1.22 (lactose synthase).
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Word Map
- 2.4.1.38
-
galts
-
galactosylate
- synthesis
- alpha-lactalbumin
-
p34cdc2-related
- beta4galts
- drug development
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
beta1,4gt1, beta4galt-ii, beta1,4-gt 1, galt v, beta1,4-galactosyltransferase 1, galti, galnact2, 4betagalt, betagalt, betagalt-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyllactosamine synthetase
-
-
-
-
beta-1,4-galactosyltransferase
beta-N-acetyl-beta1-4-galactosyltransferase
-
-
-
-
beta-N-acetylglucosaminide beta1-4-galactosyltransferase
-
-
-
-
beta1,4-GT
-
-
-
-
beta1-4-galactosyltransferase
beta1-4GalT
-
-
-
-
Gal-T
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-acetylglucosamine
-
-
-
-
GalTase
-
-
-
-
glycoprotein 4-beta-galactosyl-transferase
-
-
-
-
glycoprotein beta-galactosyltransferase
-
-
-
-
lactosamine synthase
-
-
-
-
lactosamine synthetase
-
-
-
-
lactose synthetase A protein
-
-
-
-
N-acetyllactosamine synthetase
-
-
-
-
NAL synthetase
-
-
-
-
thyroid galactosyltransferase
-
-
-
-
thyroid glycoprotein beta-galactosyltransferase
-
-
-
-
UDP-beta-1,4-galactosyltransferase
-
-
-
-
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
-
-
-
-
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
-
-
-
-
additional information
beta-1,4-galactosyltransferase
-
-
-
-
beta1-4-galactosyltransferase
-
-
-
-
additional information
-
cf. EC 2.4.1.90, the enzyme belongs to the CAZY family 7 of inverting glycosyltransferases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
mechanism
-
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
reaction mechanism and structural changes
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:N-acetyl-beta-D-glucosaminylglycopeptide 4-beta-galactosyltransferase
Terminal N-acetyl-beta-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown towards such residues in branched-chain polysaccharides when these are linked by beta-1,6-links to galactose residues; lower activity towards residues linked to galactose by beta-1,3-links. A component of EC 2.4.1.22 (lactose synthase).
CAS REGISTRY NUMBER
COMMENTARY
37237-43-7
-
9054-94-8
-
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-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide
UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
-
-
-
?
UDP-alpha-D-galactose + 4-methylumbelliferyl beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc
?
-
90-95% activity
-
-
?
UDP-alpha-D-galactose + 4-methylumbelliferyl beta-D-GlcNAc-N3(1->3)-beta-D-Gal-(1->4)-beta-D-Glc
?
-
35-40% activity
-
-
?
UDP-alpha-D-galactose + 4-methylumbelliferyl beta-D-GlcNAcPh(1->3)-beta-D-Gal-(1->4)-beta-D-Glc
?
-
20-25% activity
-
-
?
UDP-alpha-D-galactose + 4-methylumbelliferyl beta-D-GlcNTFA-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc
?
-
60-65% activity
-
-
?
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide
UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
-
-
-
-
?
UDP-galactose + 3-deoxy-3-fluoro-GlcNAcbeta-Bn
UDP + Galbeta(1-4)3-deoxy-3-fluoro-GlcNAcbeta-Bn
-
-
-
-
?
UDP-galactose + 6-deoxy-GlcNAcbeta-Bn
UDP + Galbeta(1-4)6-deoxy-GlcNAcbeta-Bn
-
low activity
-
-
?
UDP-galactose + 6-thio-GlcNAcbeta-Bn
UDP + Galbeta(1-4)6-thio-GlcNAcbeta-Bn
-
low activity
-
-
?
UDP-galactose + benzyl 2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
UDP + benzyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
-
pH 7.0, 0.5 mM, 100% activity
-
-
?
UDP-galactose + ginsenoside Rg1
UDP + beta-D-galactosyl-1,4-ginsenoside Rg1
-
-
-
-
?
UDP-galactose + methyl 2-acetamido-2-deoxy-beta-D-glucoside
UDP + beta-D-galactosyl-1,4-beta-1-O-methyl-2-deoxy-2-acetylamido-beta-D-glucopyranoside
-
76% of the activity with N-acetylglucosamine
-
-
?
UDP-galactose + methyl 2-bromo-acetamido-2-deoxy-beta-D-glucoside
UDP + beta-D-galactosyl-1,4-1-O-methyl-2-bromo-acetamido-2-deoxy-beta-D-glucoside
-
75% of the activity with N-acetylglucosamine
-
-
?
UDP-galactose + methyl 2-deoxy-2-benzamido-beta-D-glucoside
UDP + beta-D-galactosyl-1,4-1-O-methyl-2-deoxy-2-benzamido-beta-D-glucoside
-
16% of the activity with N-acetylglucosamine
-
-
?
UDP-galactose + N-4-toluenesulfonyl-GlcN
UDP + Galbeta(1-4)N-4-toluenesulfonyl-GlcN
-
-
-
-
?
UDP-galactose + N-acetyl-beta-D-glucosaminylglycopeptide
UDP + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminylglycopeptide
UDP-galactose + N-acetylglucosamine
UDP + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine
-
-
-
-
?
UDP-galactose + N-butyryl-GlcNbeta-Bn
UDP + Galbeta(1-4)N-butyryl-GlcNbeta-Bn
-
-
-
-
?
UDP-galactose + N-methanesulfonyl-GlcN
UDP + Galbeta(1-4)N-methanesulfonyl-GlcN
-
-
-
-
?
UDP-galactose + N-trifluoroacetyl-GlcN
UDP + Galbeta(1-4)N-trifluoroacetyl-GlcN
-
-
-
-
?
UDP-galactose + T-(GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TTVTPTPTG
UDP + T-(Galbeta1-4GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TTVTPTPTG
-
pH 7.0, 0.5 mM, 40% activity
-
-
?
UDP-galactose + TT-(GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TVTP(GGA)TPTG
UDP + TT-(Galbeta1-4GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TVTP(GGA)TPTG
-
pH 7.0, 0.5 mM, 25% activity
-
-
?
UDP-galactose + TT-(GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TVTPTPTG
UDP + TT-(Galbeta1-4GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TVTPTPTG
UDP-galactose + TTTVTP-(GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TPTG
UDP + TTTVTP-(Galbeta1-4GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TPTG
-
pH 7.0, 0.5 mM, 20% activity
-
-
?
UDP-glucose + N-acetylglucosamine
UDP + beta-D-glucosyl-1,4-N-acetyl-beta-D-glucosamine
-
reaction with 0.3% efficiency. R228K mutation results in a 15-fold higher glucosyltransferase activity, which is further enhanced by alpha-lactalbumin to nearly 25% of the galactosyltransferase activity of the wild type
-
-
?
UDPgalactose + 2-acetamido-N-(L-aspart-4-oyl)-1,2-dideoxy-beta-glucoside
?
-
65% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + agalacto-ovomucoid
?
-
65% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + agalactokeratan
?
-
agalactokeratan from bovine cornea and nasal septum, at 5% and 13% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + asialo-agalacto-alpha1-glycoprotein
?
-
42% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + di-acetylchitobiose
?
-
54% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + N-acetyl-beta-D-glucosaminyl-glycopeptide
UDP + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminylglycopeptide
-
glycoproteins containing terminal nonreducing N-acetylglucosaminyl units
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
UDPgalactose + N-acetylglucosaminyl-beta-1,3-(galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,6-)galactose
UDP + galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,3-(galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,6-)galactose
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl-beta-1,3-(N-acetylglucosaminyl-beta-1,6-)galactose
UDP + galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,3-(N-acetylglucosaminyl-beta-1,6-)galactose
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl-beta-1,3-galactose
UDP + galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,3-galactose
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl-beta-1,6-galactose
UDP + galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,6-galactose
-
-
-
-
?
UDPgalactose + p-nitrophenyl 2-acetamido-2-deoxy-beta-glucoside
?
-
67% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + tri-N-acetylchitotriose
?
-
64% of the activity with N-acetylglucosamine
-
-
?
UDP-galactose + N-acetyl-beta-D-glucosaminylglycopeptide
UDP + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminylglycopeptide
-
-
-
-
?
UDP-galactose + N-acetyl-beta-D-glucosaminylglycopeptide
UDP + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminylglycopeptide
-
catalytic cycle: Mn2+ binds first before UDP-Gal, two flexible loops, a long and a short loop, change their conformation from open to closed
-
-
?
UDP-galactose + TT-(GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TVTPTPTG
UDP + TT-(Galbeta1-4GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TVTPTPTG
-
pH 7.0, 0.5 mM, 30% activity
-
-
?
UDP-galactose + TT-(GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TVTPTPTG
UDP + TT-(Galbeta1-4GlcNAcbeta-1-6[Galbeta1-3]GalNAcalpha1-)TVTPTPTG
-
pH 7.0, 0.5 mM, 35% activity
-
-
?
UDP-GalNAc + GlcNAc
?
-
transfer of GalNAc is only 1% of galactose transfer in wild type enzyme. Mutant enzyme Y289L exhibits nearly 100% of the galactose transferase activity
-
-
?
UDPgalactose + glucose
lactose + UDP
-
in presence of alpha-lactalbumin
-
?
UDPgalactose + glucose
lactose + UDP
-
in presence of alpha-lactalbumin
-
?
UDPgalactose + glucose
lactose + UDP
-
in presence of alpha-lactalbumin
-
-
?
UDPgalactose + N-acetylglucosamine
UDP + N-acetyllactosamine
-
-
-
-
?
UDPgalactose + N-acetylglucosamine
UDP + N-acetyllactosamine
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
the enzyme facilitates sperm binding to the oocyte zona pellucida
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
enzyme participates in the biosynthesis of the oligosaccharide structures of glycoproteins and glycolipids
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
enzyme functions in the coordinate biosynthesis of complex oligosaccharides, proposed to function in intercellular recognition and/or adhesion
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
biosynthesis of keratan sulfate-like polysaccharides
-
-
?
additional information
?
-
-
regioselectivity towards specific C(4)glucose OH group in the complex protopanaxadiol glycoside ginsenoside Rb1
-
-
?
additional information
?
-
-
enzyme also catalyzes unusual galactosyl transfer to the 3-OH position of L-sugars
-
-
?
additional information
?
-
-
enzyme also catalyzes transfer of glucose from UDPglucose to N-acetylglucosamine
-
-
?
additional information
?
-
-
substrate specificity in presence or absence of alpha-lactalbumin, overview, the 'specifier' protein alpha-lactalbumin, which interacts with beta-1,4-GalT forming the lactose synthase complex, EC 2.4.1.2 and changing the substrate specificity to the reaction of EC 2.4.1.90, alpha-lactalbumin is not necessary when the acceptors are different glucopyranosides and, in some cases, it can even have an inhibitory effect, e.g. in reaction with the complex glucosides ginsenoside Rg1 and colchicoside, overview, in absence of alpha-lactalbumin, the enzyme is not active with glucose as acceptor
-
-
?
additional information
?
-
-
the enzyme catalyzes the transfer of Gal from UDP-Gal to GlcNAc-terminating acceptors with inversion of configuration of the glycosidic linkage, in presence of beta-lactalbumin, the enzyme changes its specificity to become lactose synthase, EC 2.4.1.22, and transfers Gal to glucose to synthesize lactose, substrate specificity, e.g. with GlcNAc-terminating O-glycopeptides, no activity with N-trimethylacetyl-GlcN, N,N-dimethyl-GlcN, N-isopropyl-GlcN, and N-(4-MeOBn)GlcN, overview
-
-
?
additional information
?
-
-
no activity with Glcbeta(1->3)Lacbeta-MU, GlcNAc6Sbeta(1->3)Lacbeta-MU, GlcNAc6N3beta(1->3)Lacbeta-MU, GlcNAc6NH2beta(1->3)Lacbeta-MU, GlcNAcPhPhbeta(1->3)Lacbeta-MU, GlcNGcbeta(1->3)Lacbeta-MU, GlcNH2beta(1->3)Lacbeta-MU, GalNAcbeta(1->3)Lacbeta-MU or Galbeta(1->)3Lacbeta-MU as acceptor
-
-
-
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-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide
UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
-
-
-
?
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide
UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
-
-
-
-
?
UDP-galactose + N-acetyl-beta-D-glucosaminylglycopeptide
UDP + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminylglycopeptide
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
the enzyme facilitates sperm binding to the oocyte zona pellucida
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
enzyme participates in the biosynthesis of the oligosaccharide structures of glycoproteins and glycolipids
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
enzyme functions in the coordinate biosynthesis of complex oligosaccharides, proposed to function in intercellular recognition and/or adhesion
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
biosynthesis of keratan sulfate-like polysaccharides
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mn2+
-
the catalytic domain of the enzyme has two metal binding sites, each with a distinct affinity. Site I binds Mn2+ with high affinity and does not bind Ca2+. Site II binds a variety of metal ions, including Ca2+. In the primary metal binding site the Mn2+ ion is coordinated to five ligands, two supplied by the phosphates of the sugar nucleotide and the other three by D254, H347 and M344
Mn2+
-
binding of two Mn(II) per mol of enzyme in the ternary enzyme-manganese-UDPgalactose complex. The affinity of the enzyme for manganese is much higher in the presence of UDPgalactose than in its absence
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-thio-N-butyryl-GlcNbeta-(2-naphthyl)
-
uncompetitive, complete inhibition at 1.0 mM, 85% inhibition at 0.2 mM
N-Acetylimidazole
-
activity is partially restored by treatment with hydroxylamine
UDP
-
treatment with periodate-cleaved UDP and NaCNBH3 results in a loss of 80% of enzyme activity, which is largely prevented by UDP-galactose
alpha-lactalbumin
-
inhibits reaction with UDPgalactose and N-acetylglucosamine
-
alpha-lactalbumin
-
inhibits the reaction of EC 2.4.1.38 with the complex glucoside colchicoside
-
additional information
-
the enzyme is totally inactivated by iodination with lactoperoxidase, EC 1.11.1.7. Substrates protect against inactivation
-
additional information
-
inhibitor synthesis and potency, mechanism of inhibition, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-lactalbumin
-
stimulates transfer of glucose from UDPglucose to N-acetylglucosamine
-
alpha-lactalbumin
-
stimulates transfer of galactose from UDPgalactose to N-acetylgalactosamine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.4
N-acetylglucosaminyl-beta-1,3-(galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,6-)galactose
-
-
1.5
N-acetylglucosaminyl-beta-1,6-galactose
-
N-acetylglucosaminyl-beta-1,3-(N-acetylglucosaminyl-beta-1,6-)galactose
0.0007
N-acetylglucosamine
-
cosubstrate: UDP-galactose, in presence of alpha-lactalbumin, mutant enzyme R228K
0.0013
N-acetylglucosamine
-
cosubstrate: UDP-glucose, in presence of alpha-lactalbumin, mutant enzyme R228K
0.0025
N-acetylglucosamine
-
cosubstrate: UDP-glucose, in presence of alpha-lactalbumin, wild-type enzyme
0.009
N-acetylglucosamine
-
cosubstrate: UDP-glucose, without alpha-lactalbumin, mutant enzyme R228K
0.011
N-acetylglucosamine
-
cosubstrate: UDP-galactose, without alpha-lactalbumin, mutant enzyme R228K
0.011
N-acetylglucosamine
-
cosubstrate: UDP-galactose, without alpha-lactalbumin, wild-type enzyme
0.074
N-acetylglucosamine
-
cosubstrate: UDP-glucose, without alpha-lactalbumin, wild-type enzyme
0.0105
UDP-galactose
-
cosubstrate: N-acetylglucosamine, in presence of alpha-lactalbumin, mutant enzyme R228K
0.087
UDP-galactose
-
cosubstrate: N-acetylglucosamine, without alpha-lactalbumin, mutant enzyme R228K
0.093
UDP-galactose
-
cosubstrate: N-acetylglucosamine, without alpha-lactalbumin, wild-type enzyme
0.031
UDP-glucose
-
cosubstrate: N-acetylglucosamine, in presence of alpha-lactalbumin, wild-type enzyme
0.044
UDP-glucose
-
cosubstrate: N-acetylglucosamine, in presence of alpha-lactalbumin, mutant enzyme R228K
0.091
UDP-glucose
-
cosubstrate: N-acetylglucosamine, without alpha-lactalbumin, mutant enzyme R228K
0.148
UDP-glucose
-
cosubstrate: N-acetylglucosamine, without alpha-lactalbumin, wild-type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
N-acetylglucosamine
-
cosubstrate: UDP-glucose, without alpha-lactalbumin, wild-type enzyme
0.17
N-acetylglucosamine
-
cosubstrate: UDP-glucose, without alpha-lactalbumin, mutant enzyme R228K
0.25
N-acetylglucosamine
-
cosubstrate: UDP-glucose, in presence of alpha-lactalbumin, wild-type enzyme
0.33
N-acetylglucosamine
-
cosubstrate: UDP-galactose, in presence of alpha-lactalbumin, mutant enzyme R228K
0.52
N-acetylglucosamine
-
cosubstrate: UDP-galactose, without alpha-lactalbumin, mutant enzyme R228K
0.96
N-acetylglucosamine
-
cosubstrate: UDP-glucose, in presence of alpha-lactalbumin, mutant enzyme R228K
14
N-acetylglucosamine
-
cosubstrate: UDP-galactose, without alpha-lactalbumin, wild-type enzyme
0.33
UDP-galactose
-
cosubstrate: N-acetylglucosamine, in presence of alpha-lactalbumin, mutant enzyme R228K
0.52
UDP-galactose
-
cosubstrate: N-acetylglucosamine, without alpha-lactalbumin, mutant enzyme R228K
14
UDP-galactose
-
cosubstrate: N-acetylglucosamine, without alpha-lactalbumin, wild-type enzyme
0.06
UDP-glucose
-
cosubstrate: N-acetylglucosamine, without alpha-lactalbumin, wild-type enzyme
0.17
UDP-glucose
-
cosubstrate: N-acetylglucosamine, without alpha-lactalbumin, mutant enzyme R228K
0.25
UDP-glucose
-
cosubstrate: N-acetylglucosamine, in presence of alpha-lactalbumin, wild-type enzyme
0.96
UDP-glucose
-
cosubstrate: N-acetylglucosamine, in presence of alpha-lactalbumin, mutant enzyme R228K
additional information
additional information
-
turnover number for UDPglucose in absence of alpha-lactalbumin is 3.48 and 14.8 in presence of alpha-lactalbumin
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
determination of beta1,4-galactosyltransferase enzymatic activity by capillary electrophoresis and laser-induced fluorescence detection, high sensitivity of product detection
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
-
short and long enzyme form are resident trans-Golgi proteins, the NH2-terminal segment contains the cytoplasmic and transmembrane domains
-
N-terminal hydrophobic segment serves as the membrane anchor, the C-terminal region is oriented within the lumen of the Golgi membranes
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). B4GT1_BOVIN
402
1
44843
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structure analysis, open and closed conformation change of the enzyme upon Mn2+ and substrate binding, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain of R228K-Gal-T1 and mouse recombinant alpha-lactalbumin are cocrystallized in the presence of UDP-galactose and MnCl2. Crystals are grown at room temperature by the hanging drop method. Crystal structure of R228K-Gal-T1 complexed with alpha-lactalbumin, UDP-galactose, and Mn2+, determined at 1.9 Å resolution shows that the Asp318 side chain exhibits a minor alternate conformation, compared to that in the wild type
-
crystal structures of the beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
-
purified recombinant pentenary complex of bovine M344H-Gal-T1 mutant-Mn2+-UDP-GalNAc-Glc-alpha-lactalbumin, hanging-drop vapor diffusion method, using 20 mg/ml of beta-M344H-Gal-T1 and 10 mg/ml of mouse alpha-lactalbumin in the presence of 10 mM each ofUDP-Gal and CaCl2, with the precipitant containing 100 mM NaCl, 100 mM Mes-NaOH buffer, pH 6.0, and 12.5% PEG 4000, the crystals of the complex cannot be obtained in the absence of CaCl2, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution
-
recombinant enzyme, crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D320A
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
site-directed mutagenesis, substrate binding structure in comparison to the wild-type enzyme, overview
M344Q
-
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
-
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
-
mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type
Y289L
-
mutation enhances GalNAc-transferase activity. Km for GlcNAc is incereased compared to the wild type
Y289N
-
mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type
additional information
additional information
-
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
-
covalent immobilization of the enzyme in the absence of alpha-lactalbumin for use as biocatalyst, method evaluation, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the N-terminal stem extension enhances the in vitro folding efficiency of the catalytic domain by several fold, it increases the solubility of even the misfolded protein
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Sf9 cells. Sfbeta4GalT cell, unlike the parental Sf9 cells, can terminally beta1,4-galactosylate gp64 during baculovirus infection
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the folding efficiency of the catalytic domain is increased further if the protein is renatured in a buffer that has polyethylene glycol and L-arginine
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
preparation of a series of specific derivatives of the complex protopanaxadiol glycoside ginsenoside Rb1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Paquet, M.R.; Moscarello, M.A.
A kinetic comparison of partially purified rat liver Golgi and rat serum galactosyltransferases
Biochem. J.
218
745-751
1984
Bos taurus, Rattus norvegicus
Ramakrishnan, B.; Qasba, P.K.
Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I
J. Mol. Biol.
310
205-218
2001
Bos taurus
Blanken, W.M.; van den Eijnden, D.H.
Biosynthesis of terminal Gal alpha (1-3)Gal beta 1-4)GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide alpha(1-3)galactosyltransferase from calf thymus
J. Biol. Chem.
260
12927-12934
1985
Bos taurus
Shaper, N.L.; Shaper, J.H.; Meuth, J.L.; Fox, J.L.; Chang, H.; Kirsch, I.R.; Hollis, G.F.
Bovine galactosyltransferase: identification of a clone by direct immunological screening of a cDNA expression library
Proc. Natl. Acad. Sci. USA
83
1573-1577
1986
Bos taurus
Narimatsu, H.; Sinha, S.; Brew, K.; Okayama, H.; Qasba, P.K.
Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-4)galactosyltransferase
Proc. Natl. Acad. Sci. USA
83
4720-4724
1986
Bos taurus
Yadav, S.; Brew, K.
Identification of a region of UDP-galactose:N-acetylglucosamine beta 4-galactosyltransferase involved in UDP-galactose binding by differential labeling
J. Biol. Chem.
265
14163-14169
1990
Bos taurus
D'Agostaro, G.; Bendiak, B.; Tropak, M.
Cloning of cDNA encoding the membrane-bound form of bovine beta 1,4-galactosyltransferase
Eur. J. Biochem.
183
211-217
1989
Bos taurus
Mitranic, M.M.; Moscarello, M.A.
The influence of various lipids on the activity of bovine milk galactosyltransferase
Can. J. Biochem.
58
809-814
1980
Bos taurus
Russo, R.N.; Shaper, N.L.; Taatjes, D.J.; Shaper, J.H.
Beta 1,4-galactosyltransferase: a short NH2-terminal fragment that includes the cytoplasmic and transmembrane domain is sufficient for Golgi retention
J. Biol. Chem.
267
9241-9247
1992
Bos taurus
Blanken, W.M.; Hooghwinkel, G.J.M.; van den Eijnden, D.H.
Biosynthesis of blood-group I and i substances. Specificity of bovine colostrum beta-N-acetyl-D-glucosaminide beta 1-4 galactosyltransferase
Eur. J. Biochem.
127
547-552
1982
Bos taurus
Tsopanakis, A.D.; Herries, D.G.
Bovine galactosyl transferase. Substrate.managanese complexes and the role of manganese ions in the mechanism
Eur. J. Biochem.
83
179-188
1978
Bos taurus
Andree, P.J.; Berliner, L.J.
Metal ion and substrate binding to bovine galactosyltransferase
Biochemistry
19
929-934
1980
Bos taurus
Christner, J.E.; Distler, J.J.; Jourdian, G.W.
Biosynthesis of keratan sulfate: purification and properties of a galactosyltransferase from bovine cornea
Arch. Biochem. Biophys.
192
548-558
1979
Bos taurus
Tengowski, M.W.; Wassler, M.J.; Shur, B.D.; Schatten, G.
Subcellular localization of beta1,4-galactosyltransferase on bull sperm and its function during sperm-egg interactions
Mol. Reprod. Dev.
58
236-244
2001
Bos taurus
Chandler, D.K.; Silvia, J.C.; Ebner, K.E.
Inactivation of galactosyltransferase by lactoperoxidase and N-acetylimidazole
Biochim. Biophys. Acta
616
179-187
1980
Bos taurus
Ramakrishnan, B.; Shah, P.S.; Qasba, P.K.
alpha-Lactalbumin (LA) stimulates milk beta-1,4-galactosyltransferase I (beta4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine. Crystal structure of beta4Gal-T1*LA complex with UDP-Glc
J. Biol. Chem.
276
37665-37671
2001
Bos taurus
Gebhardt, S.; Bihler, S.; Schubert-Zsilaveez, M.; Riva, S.; Monti, D.; Falcone, L.; Danieli, B.
Biocatalytic generation of molecular diversity: modification of ginsenoside Rb1 by beta-1,4-galactosyltransferase and Candida antarctica lipase
Helv. Chim. Acta
85
1943-1959
2002
Bos taurus
-
Hollister, J.R.; Shaper, J.H.; Jarvis, D.L.
Stable expression of mammalian beta1,4-galactosyltransferase extends the N-glycosylation pathway in insect cells
Glycobiology
8
473-480
1998
Bos taurus
Ramakrishnan, B.; Qasba, P.K.
Structure-based design of beta 1,4-galactosyltransferase I (beta4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens beta 4Gal-T1 donor specificity
J. Biol. Chem.
277
20833-20839
2002
Bos taurus
Herrmann, G.F.; Elling, L.; Krezdorn, C.H.; Kleene, R.; Berger, E.G.; Wandrey, C.
Use of transformed whole yeast cells expressing beta-1,4-galactosyltransferase for the synthesis of N-acetyllactosamine
Bioorg. Med. Chem. Lett.
5
673-676
1995
Bos taurus, Homo sapiens
-
Snow, D.M.; Shaper, J.H.; Shaper, N.L.; Hart, G.W.
Determination of beta1,4-galactosyltransferase enzymatic activity by capillary electrophoresis and laser-induced fluorescence detection
Anal. Biochem.
271
36-42
1999
Bos taurus
Gastinel, L.N.; Cambillau, C.; Bourne, Y.
Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
EMBO J.
18
3546-3557
1999
Bos taurus
Boeggeman, E.E.; Balajai, P.V.; Qasba, P.K.
Functional domains of bovine beta-1,4-galactosyltransferase
Glycoconjugate J.
12
865-878
1995
Bos taurus
Nishida, Y.; Tamakoshi, H.; Kitagawa, Y.; Kobayashi, K.; Thiem, J.
A novel bovine beta-1,4-galactosyltransferase reaction to yield beta-D-galactopyranosyl-(1-3)-linked disaccharides from L-sugars
Angew. Chem.
39
2000-2003
2000
Bos taurus
Boeggeman, E.; Qasba, P.K.
Studies on the metal binding sites in the catalytic domain of beta1,4-galactosyltransferase
Glycobiology
12
395-407
2002
Bos taurus
Ramakrishnan, B.; Boeggeman, E.; Qasba, P.K.
Mutation of arginine 228 to lysine enhances the glucosyltransferase activity of bovine beta-1,4-galactosyltransferase I
Biochemistry
44
3202-3210
2005
Bos taurus
Boeggeman, E.E.; Ramakrishnan, B.; Qasba, P.K.
The N-terminal stem region of bovine and human beta1,4-galactosyltransferase I increases the in vitro folding efficiency of their catalytic domain from inclusion bodies
Protein Expr. Purif.
30
219-229
2003
Bos taurus, Homo sapiens
Brockhausen, I.; Benn, M.; Bhat, S.; Marone, S.; Riley, J.G.; Montoya-Peleaz, P.; Vlahakis, J.Z.; Paulsen, H.; Schutzbach, J.S.; Szarek, W.A.
UDP-Gal: GlcNAc-R beta1,4-galactosyltransferase - a target enzyme for drug design. Acceptor specificity and inhibition of the enzyme
Glycoconj. J.
23
525-541
2006
Bos taurus
Ramakrishnan, B.; Ramasamy, V.; Qasba, P.K.
Structural snapshots of beta-1,4-galactosyltransferase-I along the kinetic pathway
J. Mol. Biol.
357
1619-1633
2006
Bos taurus, Homo sapiens
Pisvejcova, A.; Rossi, C.; Husakova, L.; Kren, V.; Riva, S.; Monti, D.
beta-1,4-Galactosyltransferase-catalyzed glycosylation of sugar derivatives: Modulation of the enzyme activity by alpha-lactalbumin, immobilization and solvent tolerance
J. Mol. Catal. B
39
98-104
2006
Bos taurus
-
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 (O60909)
Krupicka, M.; Tvaroska, I.
Hybrid quantum mechanical/molecular mechanical investigation of the beta-1,4-galactosyltransferase-I mechanism
J. Phys. Chem. B
113
11314-11319
2009
Bos taurus
Geisler, C.; Mabashi-Asazuma, H.; Kuo, C.W.; Khoo, K.H.; Jarvis, D.L.
Engineering beta1,4-galactosyltransferase I to reduce secretion and enhance N-glycan elongation in insect cells
J. Biotechnol.
193
52-65
2015
Bos taurus (P08037)
Li, Y.; Xue, M.; Sheng, X.; Yu, H.; Zeng, J.; Thon, V.; Chen, Y.; Muthana, M.; Wang, P.; Chen, X.
Donor substrate promiscuity of bacterial beta1-3-N-acetylglucosaminyltransferases and acceptor substrate flexibility of beta1-4-galactosyltransferases
Bioorg. Med. Chem.
24
1696-1705
2016
Bos taurus, Helicobacter pylori, Neisseria meningitidis
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