Information on EC 2.4.1.90 - N-acetyllactosamine synthase

Word Map on EC 2.4.1.90
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.4.1.90
-
RECOMMENDED NAME
GeneOntology No.
N-acetyllactosamine synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
9054-94-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
strain AG83 (MHOM/IN/83/AG83)
UniProt
Manually annotated by BRENDA team
tammar wallaby
-
-
Manually annotated by BRENDA team
ATCC 31151
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
var. AZY
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
marsupial, the brushtail possum
-
-
Manually annotated by BRENDA team
at least 2 isoforms
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
knock-down of the B4GALT1 gene and the inhibition of membrane B4GALT1 function results in the significant inhibition of estrogen-induced proliferation of MCF-7 cells
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-beta-D-GlcNAc + UDP-galactose
?
show the reaction diagram
-
Hp1–4GalT specifically recognizes GlcNAc-terminated glycans as acceptors
-
-
?
UDP-alpha-D-galactose + 4-methylumbelliferyl-6-sulfo-N-acetyl-beta-D-glucosaminide
?
show the reaction diagram
substrate with very low efficiency
-
-
?
UDP-alpha-D-galactose + 6-sulfo-N-acetyl-beta-D-glucosamine
?
show the reaction diagram
substrate with very low efficiency
-
-
?
UDP-alpha-D-galactose + N-acetyl-D-glucosamine
UDP + N-acetyllactosamine
show the reaction diagram
UDP-galactose + (beta-1,4-galactan)n
UDP + (beta-1,4-galactan)n+1
show the reaction diagram
UDP-galactose + 2-aminobenzaminated 1,4-linked beta-D-galactoheptaose
UDP + 2-aminobenzaminated 1,4-linked beta-D-galactooctaose
show the reaction diagram
-
fluorogenic synthetic acceptor substrate, elongation at the reducing end
-
-
?
UDP-galactose + 2-aminobenzaminated 1,4-linked beta-D-galactohexaose
UDP + 2-aminobenzaminated 1,4-linked beta-D-galactoheptaose
show the reaction diagram
-
fluorogenic synthetic acceptor substrate, elongation at the reducing end
-
-
?
UDP-galactose + 2-aminobenzaminated 1,4-linked beta-D-galactooligosaccharides
UDP + ?
show the reaction diagram
-
fluorogenic synthetic acceptor substrates, enzyme transfers up to 8 galactose residues to the nonreducing ends of forming beta-1,4-linkages
-
-
?
UDP-galactose + 2-aminobenzaminated 1,4-linked beta-D-galactopentaose
UDP + 2-aminobenzaminated 1,4-linked beta-D-galactohexaose
show the reaction diagram
-
fluorogenic synthetic acceptor substrate, elongation at the reducing end
-
-
?
UDP-galactose + 2-aminobenzaminated 1,4-linked beta-D-galactotetraose
UDP + 2-aminobenzaminated 1,4-linked beta-D-galactopentaose
show the reaction diagram
-
fluorogenic synthetic acceptor substrate, elongation at the reducing end
-
-
?
UDP-galactose + 3-deoxy-3-fluoro-GlcNAcbeta-Bn
UDP + Galbeta(1-4)3-deoxy-3-fluoro-GlcNAcbeta-Bn
show the reaction diagram
-
-
-
-
?
UDP-galactose + 4-methylumbelliferryl beta-D-glucopyranoside
UDP + 4-methylumbelliferyl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
-
-
-
?
UDP-galactose + 4-methylumbelliferyl N-acetyl-beta-D-glucosamine
UDP + 4-methylumbelliferyl 4-O-beta-D-galactopyranosyl-N-acetyl-beta-D-glucosaminopyranoside
show the reaction diagram
-
NmLgtB can use both GlcNAc- and Glc-terminated glycans as acceptor substrates
-
-
?
UDP-galactose + 6-deoxy-GlcNAcbeta-Bn
UDP + Galbeta(1-4)6-deoxy-GlcNAcbeta-Bn
show the reaction diagram
-
low activity
-
-
?
UDP-galactose + 6-thio-GlcNAcbeta-Bn
UDP + Galbeta(1-4)6-thio-GlcNAcbeta-Bn
show the reaction diagram
-
low activity
-
-
?
UDP-galactose + colchicoside
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + D-glucose
UDP + lactose
show the reaction diagram
-
reaction of EC 2.4.1.22
-
-
?
UDP-galactose + ginsenoside Rg1
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + GlcNAcbeta(1,2)Manalpha(1,6)(GlcNAcbeta(1,2)Manalpha(1,3))Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-PA
UDP + Galbeta1,4-GlcNAcbeta(1,2)Manalpha(1,6)(GlcNAcbeta(1,2)Manalpha(1,3))Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-PA
show the reaction diagram
-
-
-
-
-
UDP-galactose + GlcNAcbeta-Bn
UDP + Galbeta(1-4)GlcNAcbeta-Bn
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
16% of the activity with N-acetylglucosamine
-
-
?
UDP-galactose + N-4-toluenesulfonyl-GlcN
UDP + Galbeta(1-4)N-4-toluenesulfonyl-GlcN
show the reaction diagram
-
-
-
-
?
UDP-galactose + N-acetyl-D-glucosamine
UDP + N-acetyllactosamine
show the reaction diagram
UDP-galactose + N-acetylglucosamine
UDP + N-acetyllactosamine
show the reaction diagram
UDP-galactose + N-butyryl-GlcNbeta-Bn
UDP + Galbeta(1-4)N-butyryl-GlcNbeta-Bn
show the reaction diagram
-
-
-
-
?
UDP-galactose + N-methanesulfonyl-GlcN
UDP + Galbeta(1-4)N-methanesulfonyl-GlcN
show the reaction diagram
-
-
-
-
?
UDP-galactose + N-trifluoroacetyl-GlcN
UDP + Galbeta(1-4)N-trifluoroacetyl-GlcN
show the reaction diagram
-
-
-
-
?
UDP-galactose + ovalbumin
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-galactose + T(GlcNAcbeta3GalNAcbeta)TTVTPTPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + T(GlcNAcbeta6GalNAcbeta)TTVTPTPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + T(GlcNAcbeta6[GlcNAcbeta3]GalNAcbeta)TTVTPTPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + TT(GlcNAcbeta3GalNAcbeta)TVTPTPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + TT(GlcNAcbeta6GalNAcbeta)TVTPTPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + TT(GlcNAcbeta6[GlcNAcbeta3]GalNAcbeta)TVTPTPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + TTTV (GlcNAcbeta3GalNAcbeta)TPTPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + TTTV(GlcNAcbeta6GalNAcbeta)TPTPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + TTTV(GlcNAcbeta6[GlcNAcbeta3]GalNAcbeta)TPTPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + TTTVTP(GlcNAcbeta3GalNAcbeta)TPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + TTTVTP(GlcNAcbeta6GalNAcbeta)TPTG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + TTTVTPTP(GlcNAcbeta3GalNAcbeta)TG
?
show the reaction diagram
-
-
-
-
?
UDP-galactose + TTTVTPTP(GlcNAcbeta6[GlcNAcbeta3]GalNAcbeta)TG
?
show the reaction diagram
-
-
-
-
?
UDP-GalNAc + GlcNAc
?
show the reaction diagram
UDP-glucose + colchicoside
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + 2-acetamido-N-(L-aspart-4-oyl)-1,2-dideoxy-beta-glucoside
?
show the reaction diagram
-
65% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + 3-acetamido-3-deoxy-D-xylose
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + agalacto-ovomucoid
?
show the reaction diagram
-
65% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + agalacto-poly-N-acetyllactosamine
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + agalactokeratan
?
show the reaction diagram
-
agalactokeratan from bovine cornea and nasal septum, at 5% and 13% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + alpha1-acid glycoprotein
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + asialo agalacto alpha1 acid glycoprotein
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + asialo-agalacto-alpha1-glycoprotein
?
show the reaction diagram
-
42% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + asialo-agalacto-transferrin
?
show the reaction diagram
-
transfer of galactose to N-acetylglucosamine residues of Asn-linked sugar chains of glycoproteins in a beta1-4linkage
-
-
?
UDPgalactose + asialogalactofetuin
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + chitobiose
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + chitotriose
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + degalactosylated fetuin
UDP + fetuin containing beta-1,4-galactose linkages
show the reaction diagram
UDPgalactose + di-acetylchitobiose
?
show the reaction diagram
-
54% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + fetuin
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + GlcNAcbeta-S-p-NP
UDP + Galbeta1-4 GlcNAcbeta-S-p-NP
show the reaction diagram
-
-
-
?
UDPgalactose + GlcNAcbeta1-6(GlcNAcbeta1-2)Manalpha1-3Manbeta1-O(CH2)8COOCH2-mNP
UDP + Galbeta1-4 GlcNAcbeta1-6(GlcNAcbeta1-2)Manalpha1-3Manbeta1-O(CH2)8COOCH2-mNP
show the reaction diagram
-
-
-
?
UDPgalactose + glucose
lactose + UDP
show the reaction diagram
UDPgalactose + immunoglobulin heavy chain
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + lacto-N-triaosylceramide
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + lacto-N-triose II
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + N-acetamido-3-deoxy-D-glucose
?
show the reaction diagram
-
-
-
-
?
UDPgalactose + N-acetyl-beta-D-glucosaminyl-glycopeptide
UDP + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminylglycopeptide
show the reaction diagram
UDPgalactose + N-acetylglucosamine
UDP + N-acetyllactosamine
show the reaction diagram
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
show the reaction diagram
UDPgalactose + N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
UDP + galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
show the reaction diagram
-
-
galactose is transferred much faster to the N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-branch than to the N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-branch
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl-beta-1,3-galactose
UDP + galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,3-galactose
show the reaction diagram
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl-beta-1,6-galactose
UDP + galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,6-galactose
show the reaction diagram
-
-
-
-
?
UDPgalactose + ovalbumin
?
show the reaction diagram
UDPgalactose + ovomucoid
UDP + ovomucoid with beta-1,4-bound galactose
show the reaction diagram
-
-
-
?
UDPgalactose + p-nitrophenyl 2-acetamido-2-deoxy-beta-glucoside
?
show the reaction diagram
UDPgalactose + tri-N-acetylchitotriose
?
show the reaction diagram
-
64% of the activity with N-acetylglucosamine
-
-
?
UDPgalactose + UDPglucose
UDP + lactose
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + N-acetyl-D-glucosamine
UDP + N-acetyllactosamine
show the reaction diagram
UDP-galactose + (beta-1,4-galactan)n
UDP + (beta-1,4-galactan)n+1
show the reaction diagram
-
enzyme elongates beta-1,4-galactan side chains of rhamnogalacturonan I components of the cell wall pectin
-
-
?
UDP-galactose + N-acetyl-D-glucosamine
UDP + N-acetyllactosamine
show the reaction diagram
UDP-galactose + N-acetylglucosamine
UDP + N-acetyllactosamine
show the reaction diagram
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Sr2+
-
active only with mutant enzymes M334H and M344E, no activity with wild-type enzyme and mutants M344A, M344S, and M344Q
additional information
-
metal ion specificity of wild-type and mutant enzymes, overview
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,6-dithio-N-butyryl-GlcNbeta-(2-naphthyl)
-
45% inhibition at 1.0 mM
1-thio-N-butyryl-GlcNbeta-(2-naphthyl)
-
uncompetitive, complete inhibition at 1.0 mM, 85% inhibition at 0.2 mM
1-thioGlcNAcbeta-(2-naphthyl)
-
91% inhibition at 1.0 mM
6-thio-N-butyryl-GlcNbeta-(2-naphthyl)
-
19% inhibition at 1.0 mM
acetone
-
20% v/v, 37% inhibition
acetonitrile
-
20% v/v, complete inhibition
alpha-lactalbumin
-
alpha1-Acid glycoprotein
-
above 1.4 mM with respect to acceptor sites
-
ammonium
enzyme activity is decreased in ammonium treated cell culture
Dimethylsulfoxide
-
20% v/v, 62% inhibition
ethanol
-
20% v/v, 42% inhibition
GlcNAcbeta-(2-naphthyl)
-
92% inhibition at 1.0 mM
N,N-Dimethylformamide
-
20% v/v, 84% inhibition
N-acetylglucosamine
N-Acetylimidazole
-
activity is partially restored by treatment with hydroxylamine
N-butyryl-GlcNbeta-(2-naphthyl)
-
87% inhibition at 1.0 mM
N-methylpyrrolidone
-
20% v/v, 9% inhibition
p-hydroxymercuribenzoate
-
-
p-nitrophenyl 2-acetamido-2-deoxy-beta-glucoside
-
competitively inhibits the transfer of galactose to glycoprotein substrates
-
phosphatidic acid
phosphatidylethanolamine
-
-
phosphatidylglycerol
-
-
phosphatidylserine
-
-
poly(L-Glu)
-
-
tetrahydrofuran
-
20% v/v, complete inhibition
UMP
-
competitively inhibits the transfer of galactose to glycoprotein substrates
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-lactalbumin
-
dimyristoylphosphatidylcholine
dioleoylphosphatidylcholine
-
activation
dipalmitoylphosphatidylcholine
-
activation
Distearoylphosphatidylcholine
-
activation
histone
-
activation
lysophosphatidylcholine
-
activation
Methylphosphatidylic acid
-
activation
phosphatidylcholine
phosphatidylethanolamine
-
activation
phosphatidylglycerol
-
activation
poly(L-Arg)
-
activation
poly(L-Lys)
-
activation
Protamine sulfate
-
activation
-
Triton X-100
additional information
-
the enzyme regulation/stimulation is a complex system involving the hormones insulin, prolactine, hydrocortisone, triiodothyronine, and 17beta-estradiol, andalso the extracellular matrix and the sucking stimulus
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
2-aminobenzaminated 1,4-linked beta-D-galactoheptaose
-
pH 6.5, 25°C
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
-
0.17
agalacto-poly-N-acetyllactosamine
-
-
-
2.8
agalactokeratan
-
-
-
0.2
alpha1-Acid glycoprotein
-
-
-
0.056 - 0.064
asialo-agalacto-transferrin
-
0.0608
asialogalactofetuin
-
-
-
1 - 21
D-glucose
0.029
fetuin
-
-
-
6.28
galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
-
-
0.25
glycopeptide prepared from porcine IgG immunoglobulin
-
-
-
0.02
IgG immunoglobulin heavy chain
-
-
-
0.83
lacto-N-triaosylceramide
-
-
0.19
lacto-N-triose II
-
-
0.8
N-acetylgalactosamine
-
-
0.0039 - 40
N-acetylglucosamine
0.43
N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
-
-
0.13
N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
-
-
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
0.054 - 0.27
ovalbumin
-
0.66
p-nitrophenyl 2-acetamido-2-deoxy-beta-glucoside
-
-
-
0.23
UDP-alpha-D-galactose
at 37°C, pH not specified in the publication
0.032
UDP-galactose
-
pH 6.5, 25°C
0.0108 - 0.25
UDPgalactose
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.097 - 3.6
UDP-galactose
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
1-thio-N-butyryl-GlcNbeta-(2-naphthyl)
-
pH 7.0
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000013
-
mutant M344H in presence of 5 mM Mn2+
0.00000032
-
mutant M344E in presence of 5 mM Mn2+
0.00000191
-
mutant M344Q in presence of 5 mM Mn2+
0.00000197
-
mutant M344S in presence of 5 mM Mn2+
0.00000416
-
mutant M344A in presence of 5 mM Mn2+
0.00000535
-
wild-type enzyme in presence of 5 mM Mn2+
0.00008
-
EoL-1 cell extract
0.00013
-
KU-812 cell extract
0.00014
-
THP-1 cell extract, HEL cell extract, and HL-60 cell extract
0.00015
-
MOLT-4 cell extract
0.00016
-
Bowes melanoma cell extract
0.00021
-
T-24 cell extract
0.00025
-
HuO-3N1 cell extract
0.00037
-
Namalga cell extract
0.00039
-
HepG2 cell extract
0.00044
-
YMB-1 cell extract
0.00053
-
A-549 cell extract
0.0006
-
CACO-2 cell extract, and HeLaS3 cell extract
0.00065
-
BALL-1 cell extract
0.00084
-
OS-RC-2 cell extract
0.00122
-
BeWo cell extract
0.035
-
-
0.535
-
-
6.9
-
N-deglycosylated recombinant enzyme
8.4
-
recombinant enzyme
10.7
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 7.6
-
-
6.5 - 7
7.2
-
assay at
7.4
-
assay at
7.5 - 10.5
-
-
8.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.3
-
pH 5.0: about 60% of maximal activity, pH 9.3: about 45% of maximal activity
5.5 - 8
-
less than 50% of maximal activity above and below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
-
less than 50% of maximal activity above and below
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.05 - 5.95
-
diverse isoforms from patients with rheumatoid arthritis and from healthy individuals separated by isoelectric focusing, profiling, overview
additional information
-
amount of the diverse isoforms is different in serum from patients with rheumatoid arthritis and in serum from healthy individuals, overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
lung carcinoma cell line
Manually annotated by BRENDA team
-
acute promyelocytic leukemia cell line
Manually annotated by BRENDA team
-
choriocarcinoma cell line, high activity
Manually annotated by BRENDA team
-
Namalwa cells
Manually annotated by BRENDA team
-
colon adenocarcinoma cell line
Manually annotated by BRENDA team
-
BeWo cells, high activity
Manually annotated by BRENDA team
-
of patients with colorectal cancer 48% have down-regulated expression of beta-1,4-GT-IV in the tumor tissue, while 28% of patients exhibit elevated beta-1,4-GT-IV levels, the patient group with tumor beta-1,4-GT-IV overexpression strongly predicts for tumor metastasis, overview
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
eosinophilic leukemia cell line, low activity
Manually annotated by BRENDA team
-
EoL-1 cells, low activity
Manually annotated by BRENDA team
-
erythroid leukemia cell line
Manually annotated by BRENDA team
-
cervical carcinoma cell line
Manually annotated by BRENDA team
-
hepatocellular carcinoma cell line
Manually annotated by BRENDA team
-
Hep-G2 cells
Manually annotated by BRENDA team
-
; osteosarcoma cell line
Manually annotated by BRENDA team
-
ileal-colonic
Manually annotated by BRENDA team
-
regional distribution
Manually annotated by BRENDA team
-
chronic myelogenous leukemia cell line
Manually annotated by BRENDA team
-
fetal
Manually annotated by BRENDA team
-
A-549 cells
Manually annotated by BRENDA team
-
ATCC No. CCL22
Manually annotated by BRENDA team
-
Bowes melanoma cell line
Manually annotated by BRENDA team
-
T cell leukemia cell line
Manually annotated by BRENDA team
-
chronic, KU-812 cells
Manually annotated by BRENDA team
-
; renal cell carcinoma cell line
Manually annotated by BRENDA team
-
acute, BALL-1 cells
Manually annotated by BRENDA team
-
anterior head of sperm head
Manually annotated by BRENDA team
-
during differentiation from spermatogonia to pachytene spermatocytes the amount of UDP beta1,4-galactosyltransferase mRNA is reduced to barley detectable levels
Manually annotated by BRENDA team
-
from caput and cauda epididymis, quantification of enzyme protein on the sperm surface, overview
Manually annotated by BRENDA team
-
urinary bladder carcinoma cell
Manually annotated by BRENDA team
-
MOLT-4 cells
Manually annotated by BRENDA team
-
monocytic leukemia cell line
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
; breast cancer cell line
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
estrogen-induced expression of B4GALT1 is localized in intracellular compartments and in the plasma membrane
Manually annotated by BRENDA team
-
estrogen-induced expression of B4GALT1 is localized in intracellular compartments and in the plasma membrane
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
x * 38000, SDS-PAGE
42200
-
x * 42200, SDS-PAGE
42960
-
calculation from gene sequence, short form, transmembrane enzyme
43000
-
x * 43000, SDS-PAGE
44420
-
long form with NH2-terminal extension of 13 amino acids, calculation from gene sequence
44880
-
unglycosylated enzyme, calculation from gene sequence
47000
-
x * 47000, deglycosylated enzyme form, SDS-PAGE
48000
-
x * 48000, glycosylated enzyme form
51000
-
x * 51000, SDS-PAGE
53000
-
x * 53000, SDS-PAGE
54000
-
x * 54000, enzyme from milk, SDS-PAGE
55000
-
2 * 55000, SDS-PAGE
57000
-
sucrose density gradient centrifugation
59000
-
gel filtration
66000
-
x * 66000, SDS-PAGE
70000
-
gel filtration
74000
-
1 * 74000, SDS-PAGE
85000 - 90000
-
gel filtration
106000
-
calculation from light-scattering experiments
440000
-
gel filtration
additional information
-
two related forms of enzyme of 399 and 386 amino acids are synthesized as a consequence of alternative translation initiation. The long enzyme form has a NH2-terminal extension of 13 amino acids
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 55000, SDS-PAGE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic enzyme domain without complexed substrate, conf-I' conformation, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
crystal structure of enzyme-alpha-lactalbumin complex with UDP-Glc
-
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
-
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
recombinant enzyme, crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I
-
crystal structure of the catalytic domain of beta4Gal-T7 from Drosophila melanogaster in the presence of manganese and UDP at 1.81 A resolution is shown. In the crystal structure, a new manganese ion-binding motif is observed. Superposition of the crystal structures of beta4Gal-T7 and beta4Gal-T1 shows that the catalytic pocket and the substrate-binding sites in these proteins are similar
-
enzyme in complex with Mn2+, UDP-GalNAc, glucose, and alpha-lactalbumin, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
W314A enzyme mutant complexed with alpha-lactalbumin in presence of N-acetylglucoamine, UDP, and Mn2+, conf-II conformation, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
-
489493
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
4 h, 18% loss of activity
45
-
stable up to
50
-
1 h, complete loss of activity
56
-
inactivation at
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate stabilizes during storage
-
glycerol stabilizes during storage
-
more than 50% loss of activity on freezing
-
Triton X-100 essential for stability during purification
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.02 M Tris/HCl buffer, pH 7.5, stable for several months
-
-20°C, 1 mg/ml bovine serum albumin
-
-20°C, 10% glycerol, up to 14 months, no loss of activity
-20°C, bovine serum albumin, stable for up to 60 d
-
-20°C, partially purified enzyme stable for several weeks, purified enzyme stable for 1 week
-
-20°C, stable fo at least 1 month
-
-20°C, stable for 3 weeks
-
-20°C, stable for at least 2 months
-
4°C, 0.1% bovine serum albumin, stable for 3 months
-
4°C, concentrated enzyme
-
4°C, more than 50% loss of activity after 1 week
-
4°C, purified and concentrated enzyme is stable for 4 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae
-
partially, preparation of the Golgi fraction
-
recombinant enzyme
recombinant wild-type enzyme and mutant W314A from Escherichia coli after solubilization from inclusion bodies by alpha-lactalbumin affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into pMAL-c4X vector and expressed in Escherichia coli Origami B (DE3) cells as an N-maltose binding protein (MBP)-tagged and C-His6-tagged fusion protein
-
cloning and sequencing of cDNA
-
cloning and sequencing of the full-length cDNA
-
comparison of sequences of enzyme from placenta and HeLa cells
-
DNA and amino acid sequence determination and analysis, promoter activity analysis
DNA fragments coding the catalytic domain (Cd7) sequence (residues 71-322) and the C-terminal 11-amino acid deletion (Cd7DELTAC) sequence (residues 71-311) are cloned into a pET23a vector and expressed in Escherichia coli
-
enzymatically active soluble N-deglycosylated enzyme form
-
enzyme fused to protein A is expressed as a soluble form in COS-7 cells
expression as GFP-tagged enzyme in HeLa cells
-
expression in Cos-1 cells
-
expression in Escherichia coli
expression in Sf9 cells. Sfbeta4GalT cell, unlike the parental Sf9 cells, can terminally beta1,4-galactosylate gp64 during baculovirus infection
-
expression of mutant cDNA from a patient with the congenital disorder of glycosylation type IId leads to the synthesis of a truncated, inactive polypeptide, which is localized to the endoplasmic reticulum
-
expression of short and long enzyme form in CHO-cells
-
expression of wild-type and mutant enzymes in Escherichia coli
-
expression of wild-type enzyme and mutant W314A in Escherichia coli in inclusion bodies
-
expression under the control of the T7 promoter in Escherichia coli BL21
HeLa cells expressing the murine enzyme on their surface spread more rapidly on laminin substrates than do control cells
-
histidine-tagged 46000 Da protein produced in Escherichia coli
-
isolation and characterization of the genomic locus
-
isolation of a cDNA clone that encodes a major portion of galactosyltransferase
-
molecular cloning and nucleotide sequencing
-
NmLgtB is cloned into pET15b vector and expressed in Escherichia coli BL21 (DE3) cells as N-terminal His6-tagged fusion protein. Under common expression conditions only a low amount of soluble active enzyme is obtained. The expression level is improved 15fold to 12.5 mg/L culture under osmotic stress condition using LB medium supplemented with 0.2% glucose and a higher concentration of NaCl
-
quantitative enzyme expression analysis in strains UR6 and AG83, overview
recombinant enzyme is N-glycosylated
-
transient functional overexpression in 7721 hepatocarcinoma cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
estrogen induces B4GALT1 expression
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C134S
-
complete loss of activity
C342S
-
33fold increase in the apparent Km-value for UDPgalactose
D254E
-
0.01% of the activity of the wild-type enzyme
D254N
-
0.01% of the activity of the wild-type enzyme
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
M344E
-
site-directed mutagenesis, altered metal ion specificity compared to the wild-type enzyme
M344S
-
site-directed mutagenesis, altered metal ion specificity compared to the wild-type enzyme
Y289N
-
mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type
DELTA1-70
-
crystallization of a refolded Drosophila Cd7 protein coding the catalytic domain (Cd7) sequence (residues 71-322) is not successful
DELTA1-70/DELTA312-322
-
a DNA fragment bearing the Cd7 catalytic domain and C-terminal 11-amino acid deletion (Cd7DELTAC) sequence (residues 71-311) shows no difference in catalytic activity or folding but crystalization is not possible
I285Y
-
site-directed mutagenesis, the mutation converts the betaGALNAcT1 enzyme into an efficient beta4Gal-T1, the N-acetylgalactosaminyltransferase activity is reduced by nearly 1000fold, while the galactosyltransferase activity is enhanced by 80fold
Y289L/C342T
-
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
W314A
-
site-directed mutagenesis, mutant shows highly reduced activity, i.e. 0.6% of wild-type galactosyltransferase activity, substrate binding, and reduced binding to the effector alpha-lactalbumin as well as reduced susceptibility to cleavage by proteases Glu-C and Lys-C compared to the wild-type enzyme, overview
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
refolding of the wild-type enzyme and mutant W314A from inclusion bodies after recombinant expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
enzyme can be useful in the glycosylation of cytokines, enzymes or other glycosylated compounds modifying their functions for use in medical therapies
medicine
synthesis