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Information on EC 2.4.1.90 - N-acetyllactosamine synthase and Organism(s) Bos taurus and UniProt Accession P08037
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2.4.1.90 N-acetyllactosamine synthaseIUBMB Comments
The reaction is catalysed by a component of EC 2.4.1.22 (lactose synthase), which is identical with EC 2.4.1.38 (beta-N-acetylglucosaminyl-glycopeptide beta-1,4-galactosyltransferase), and by an enzyme from the Golgi apparatus of animal tissues. Formerly listed also as EC 2.4.1.98.
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Word Map
- 2.4.1.90
- oligosaccharide
- glycosyltransferases
-
galactosylation
- n-glycans
- alpha-lactalbumin
- ganglioside
- glycosphingolipids
- zona
- pellucida
- glucosylceramide
-
laccer
- zp3
-
sperm-egg
-
d-pdmp
- ga2
- poly-n-acetyllactosamine
- udp-galnac
- medicine
- synthesis
- biotechnology
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
galtase, galnact, b4galt5, b4galt3, gal-t, beta-1,4-galt-i, lactosylceramide synthase, beta-1,4-galt, beta1,4-galactosyltransferase i, galt1, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyllactosamine synthetase
-
-
-
-
beta-1,4-galactosyltransferase
beta-N-acetylglucosaminide beta1-4-galactosyltransferase
-
-
-
-
beta1,4-GT
-
-
-
-
beta1-4-galactosyltransferase
-
-
-
-
beta1-4GalT
-
-
-
-
Gal-T
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-acetylglucosamine
-
-
-
-
GalTase
-
-
-
-
lactosamine synthase
-
-
-
-
lactosamine synthetase
-
-
-
-
lactose synthetase A protein
-
-
-
-
N-acetyllactosamine synthetase
-
-
-
-
NAL synthetase
-
-
-
-
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-N-acetylglucosamine beta-D-galactosyltransferase
-
-
-
-
UDPgalactose:N-acetylglucosaminyl(beta1-4)galactosyltransferase
-
-
-
-
uridine diphosphogalactose-acetylglucosamine galactosyltransferase
-
-
-
-
additional information
beta-1,4-galactosyltransferase
-
-
-
-
additional information
-
cf. EC 2.4.1.38, the enzyme belongs to the CAZY family 7 of inverting glycosyltransferases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
mechanism
-
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
catalytic mechanism, enzyme undergoes critical conformational changes upon substrate binding from an open, conf-I, to a closed conformation, conf-II, involving 2 flexible loops, a small and a long one, with Trp314 of the small loop being critical for the change interacting with both substrates, catalytic site structure
-
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
sequential ordered catalytic mechanism, enzyme undergoes critical conformational changes upon substrate binding from an open, conf-I, to a closed conformation, conf-II, involving 2 flexible loops, a small and a long one, with Trp314 of the small loop being critical for the change interacting with both substrates, catalytic site structure, Tyr289 determines the specificity for UDP-Gal, the conformational changes create the oligosaccharide-acceptor substrate binding site
-
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
the GlcNAc residue at the nonreducing end of chitobiose makes extensive hydrophobic interactions with the highly conserved Tyr286
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:N-acetyl-D-glucosamine 4-beta-D-galactosyltransferase
The reaction is catalysed by a component of EC 2.4.1.22 (lactose synthase), which is identical with EC 2.4.1.38 (beta-N-acetylglucosaminyl-glycopeptide beta-1,4-galactosyltransferase), and by an enzyme from the Golgi apparatus of animal tissues. Formerly listed also as EC 2.4.1.98.
CAS REGISTRY NUMBER
COMMENTARY
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 + 4-methylumbelliferyl-6-sulfo-N-acetyl-beta-D-glucosaminide
?
substrate with very low efficiency
-
-
?
UDP-alpha-D-galactose + 6-sulfo-N-acetyl-beta-D-glucosamine
?
substrate with very low efficiency
-
-
?
UDP-alpha-D-galactose + N-acetyl-D-glucosamine
UDP + N-acetyllactosamine
-
-
-
?
UDP-alpha-D-galactose + 1-(2-naphthyl) 2-acetamido-2-deoxy-beta-D-glucopyranoside
UDP + ?
-
-
-
-
?
UDP-alpha-D-galactose + N-acetyl-D-glucosamine
UDP + N-acetyllactosamine
-
-
-
-
?
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 + 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-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
-
-
-
-
?
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-D-glucosamine
UDP + N-acetyllactosamine
-
-
-
-
?
UDP-galactose + N-acetyl-D-glucosamine
UDP + N-acetyllactosamine
-
enzyme is highly specific for UDP-galactose as donor substrate, 100fold less active with UDP-glucose
-
-
?
UDP-galactose + N-acetyl-D-glucosamine
UDP + N-acetyllactosamine
-
specific for UDP-galactose
-
-
?
UDP-galactose + N-acetyl-D-glucosamine
UDP + N-acetyllactosamine
-
in presence of alpha-lactalbumin, the enzyme catalyzes reaction of EC 2.4.1.22
-
-
?
UDP-galactose + N-acetylglucosamine
UDP + N-acetyllactosamine
-
partial reaction of EC 2.4.1.22
-
-
?
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
?
-
-
enzyme interacts with alpha-lactalbumin to form the lactose synthase enzyme complex, structural basis for catalytic mechanism, overview
-
-
?
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 2.4.1.22, is not necessary when the acceptors are different glucopyranosides, EC 2.4.1.38, and, in some cases, it can even have an inhibitory effect, e.g. in reaction with the complex glucosides ginsenoside Rg1 and colchicoside, overview
-
-
?
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
?
-
-
substrate specificity, coupling of 6-azido-6-deoxy D-galactose to a GlcNAc-terminated substrate, method development for usage of the enzyme reaction for tagging glycoproteins carrying terminal GlcNAc, overview
-
-
?
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-D-glucosamine
UDP + N-acetyllactosamine
-
-
-
?
UDP-alpha-D-galactose + N-acetyl-D-glucosamine
UDP + N-acetyllactosamine
-
-
-
-
?
UDP-galactose + N-acetyl-D-glucosamine
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
?
-
-
-
-
?
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
Ca2+
-
active only with mutant enzymes M334H and M344E, no activity with wild-type enzyme and mutants M344A, M344S, and M344Q
Co2+
Mg2+
-
active only with mutant enzymes M334H and M344E, no activity with wild-type enzyme and mutants M344A, M344S, and M344Q
Mn2+
Sr2+
-
active only with mutant enzymes M334H and M344E, no activity with wild-type enzyme and mutants M344A, M344S, and M344Q
Zn2+
additional information
-
metal ion specificity of wild-type and mutant enzymes, overview
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
Mn2+
-
required, binding site structure involving Met344 and Asp254, mechanism overview, binding results in conformational changes in the catalytic domain
Mn2+
-
required, metal binding site structure with an uncommon coordination to the Sdelta atom of Met344, the site is located in the hinge region of along flexible loop, which changes from open to closed conformation upon binding of Mn2+ and UDP-galactose creating an oligosaccharide binding site in the enzyme structure, effect occurs specifically with UDP-galactose, not with other UDP-sugars,overview
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
-
additional information
-
the enzyme is totally inactivated by iodination with lactoperoxidase, EC 1.11.1.7. Substrates protect against inactivation
-
additional information
-
not inhibited by 1-(2-naphthyl) 2-acetamido-2-deoxy-beta-D-glucopyranoside
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bovine serum albumin
-
in the presence of 12.5 mg/ml bovine serum albumin, turnover rates increase approximately 2fold and Km values increase by approximately 4fold, for both N-acetyl-D-glucosamine and 1-(2-naphthyl) 2-acetamido-2-deoxy-beta-D-glucopyranoside
-
alpha-lactalbumin
-
stimulates transfer of glucose from UDPglucose to N-acetylglucosamine
-
alpha-lactalbumin
-
stimulates transfer of galactose from UDPgalactose to N-acetylgalactosamine
-
alpha-lactalbumin
-
alters the substrate specificity of EC 2.4.1.38 to EC 2.4.1.90, and leads to complex formation with the enzyme as lactose synthase, EC 2.4.1.22
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
4-methylumbelliferyl-6-sulfo-N-acetyl-beta-D-glucosaminide
at 37°C, pH not specified in the publication
1.7
6-sulfo-N-acetyl-beta-D-glucosamine
at 37°C, pH not specified in the publication
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
0.00008
1-(2-naphthyl) 2-acetamido-2-deoxy-beta-D-glucopyranoside
-
in the absence of bovine serum albumin, at pH 7.0 and 30°C
0.0003
1-(2-naphthyl) 2-acetamido-2-deoxy-beta-D-glucopyranoside
-
in the presence of 12.5 mg/ml bovine serum albumin, at pH 7.0 and 30°C
0.0004
N-acetyl-D-glucosamine
-
in the absence of bovine serum albumin, at pH 7.0 and 30°C
0.0015
N-acetyl-D-glucosamine
-
in the presence of 12.5 mg/ml bovine serum albumin, at pH 7.0 and 30°C
additional information
additional information
-
kinetics, wild-type and mutant M344H enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
-
metal ion specificity of wild-type and mutant enzymes, overview
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
additional information
-
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
additional information
-
enzyme possesses a membrane-spanning domain, a cytoplasmic domain, a stem region, and the catalytic domain that faces the lumen
-
additional information
-
enzyme possesses a membrane-spanning domain, a cytoplasmic domain, a stem region, and the catalytic domain that faces the lumen
-
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
-
enzyme possesses a membrane-spanning domain, a cytoplasmic domain, a stem region, and the catalytic domain that faces the lumen
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme C342T/M344H, hanging drop vapor diffusion method, using 100 mM MES-NaOH buffer pH 6.5, 1.8 M ammonium sulfate and 10% (v/v) 1, 4-dioxane
catalytic enzyme domain without complexed substrate, conf-I' conformation, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
crystal structures of the beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
-
M344H mutant enzyme complexed with UDP-Gal and Mn2+ or Mg2+, hanging drop vapour diffusion method, 30 mg/ml protein in solution with 17 mM UDP-Gal, and 17 mM MgCl2 or MnCl2, precipitated by 10% v/v dioxane, 100 mM MES-NaOH, pH 6.5, and 2.0M ammonium sulfate, room temperature, X-ray diffraction structure determination and analysis at 2.3 A resolution, determination of conformation stereochemistry, modeling
-
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
M344E
-
site-directed mutagenesis, altered metal ion specificity compared to the wild-type enzyme
M344H
M344Q
M344S
-
site-directed mutagenesis, altered metal ion specificity compared to the wild-type enzyme
Y289I
Y289L
Y289N
-
mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type
additional information
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
M344A
-
site-directed mutagenesis, altered metal ion specificity compared to the wild-type enzyme
M344H
-
mutant prefers Mg2+ instead of Mn2+ which is preferred by the wild-type enzyme, with Mn2+ the mutant is arrested in the closed inactive conformation
M344H
-
site-directed mutagenesis, the mutant shows altered conformational changes upon binding of Mn2+ and substrates or substrate analogues compared to the wild-type enzyme, it forms the closed conformation with bound Mn2+ and UDP-hexanolamine, loss of 98% of Mn2+ binding activity, increased activity with Mg2+
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
M344Q
-
site-directed mutagenesis, altered metal ion specificity compared to the wild-type enzyme
Y289I
-
mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type
Y289I
-
mutant shows high activity with UDP-GalNAc in contrary to the wild-type enzyme
Y289L
-
mutation enhances GalNAc-transferase activity. Km for GlcNAc is incereased compared to the wild type
Y289L
-
mutant shows high activity with UDP-GalNAc in contrary to the wild-type enzyme
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+
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
preparation of a series of specific derivatives of the complex protopanaxadiol glycoside ginsenoside Rb1
synthesis
-
development of a method to tag glycoproteins carrying terminal GlcNAc using the enzyme, overview
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.
Effect of Met344His mutation on the conformational dynamics of bovine beta-1,4-galactosyltransferase: crystal structure of the Met344His mutant in complex with chitobiose
Biochemistry
43
12513-12522
2004
Bos taurus
Ramakrishnan, B.; Boeggeman, E.; Ramasamy, V.; Qasba, P.K.
Structure and catalytic cycle of beta-1,4-galactosyltransferase
Curr. Opin. Struct. Biol.
14
593-600
2004
Bos taurus, Homo sapiens
Ramasamy, V.; Ramakrishnan, B.; Boeggeman, E.; Qasba, P.K.
The role of tryptophan 314 in the conformational changes of beta1,4-galactosyltransferase-I
J. Mol. Biol.
331
1065-1076
2003
Bos taurus, Mus musculus
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
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
-
Bosco, M.; Le Gall, S.; Rihouey, C.; Couve-Bonnaire, S.; Bardor, M.; Lerouge, P.; Pannecoucke, X.
6-Azido D-galactose transfer to N-acetyl-D-glucosamine derivative using commercially available beta-1,4-galactosyltransferase
Tetrahedron Lett.
49
2294-2297
2008
Bos taurus
-
Ramakrishnan, B.; Moncrief, A.J.; Davis, T.A.; Holland, L.A.; Qasba, P.K.
Investigations on beta1,4-galactosyltransferase I using 6-sulfo-GlcNAc as an acceptor sugar substrate
Glycoconj. J.
30
835-842
2013
Bos taurus (P08037)
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