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2.4.1.90: N-acetyllactosamine synthase

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

Word Map on EC 2.4.1.90

Reaction

UDP-alpha-D-galactose
+
N-acetyl-D-glucosamine
=
UDP
 +
N-acetyllactosamine

Synonyms

acetyllactosamine synthetase, B4GALT1, B4GALT3, B4GalT5, beta 1,4 galactosyltransferase I, beta 1,4-galactosyltransferase 1, beta 1,4GalT II, beta 1,4GTI, beta(1,4)-galactosyltransferase, beta(1,4)-GT, beta(1-4)galactosyltransferase, beta-1,4-galactosyltransferase, beta-1,4-galactosyltransferase 1, beta-1,4-galactosyltransferase III, beta-1,4-galactosyltransferase IV, beta-1,4-galactosyltransferase-1, beta-1,4-galactosyltransferase-I, beta-1,4-galactosyltransferase-V, beta-1,4-GalT, beta-1,4-GalT-I, beta-1,4-GalT-V, beta-1,4-GT-IV, beta-1,4-N-acetylgalactosaminyltransferase, beta-N-acetylglucosaminide beta1-4-galactosyltransferase, beta1,4-Gal-transferase T1, beta1,4-galactosyltransferase, beta1,4-galactosyltransferase I, beta1,4-galactosyltransferase II, beta1,4-galactosyltransferase V, beta1,4-galactosyltransferase-1, beta1,4-galactosyltransferase-7, beta1,4-galactosyltransferase-I, beta1,4-GT, beta1,4GalT II, beta1,4GalTV, beta1-4-galactosyltransferase, beta1-4GalT, beta4Gal-T, beta4Gal-T1, beta4Gal-T7, beta4GalT, beta4GalT1, betaGALT1, beta[1-4]GalT, EC 2.4.1.98, Gal-T, galactosyltransferase, uridine diphosphogalactose-acetylglucosamine, GalNAcT, GALT, GalT1, GalT7, GalTase, GalTase-I, GTase, Hp1-4GalT, lactosamine synthase, lactosamine synthetase, lactose synthetase A protein, lactosylceramide synthase, More, N-acetyllactosamine synthetase, NAL synthetase, NmLgtB, UDP-beta-1,4-galactosyltransferase, UDP-Gal:betaGlcNAc beta-1,4-galactosyltransferase, polypeptide 5, 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-acetylglucosamine beta1,4 galactosyltransferase, UDP-galactose: N-acetylglucosamine beta 1-4 galactosyltransferase, UDP-galactose:N-acetylglucosaminide beta1-4-galactosyltransferase, UDPgalactose-N-acetylglucosamine beta-D-galactosyltransferase, UDPgalactose:N-acetylglucosaminyl(beta1-4)galactosyltransferase, uridine diphosphogalactose-acetylglucosamine galactosyltransferase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.90 N-acetyllactosamine synthase

Engineering

Engineering on EC 2.4.1.90 - N-acetyllactosamine synthase

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PROTEIN VARIANTS
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
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
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
D315A
-
the mutant shows about 90% of wild type activity
H343A
-
the mutant shows about 3% of wild type activity
M340E
-
the mutant shows about 85% of wild type activity
M340H
-
the mutant shows about 10% of wild type activity
Y268G/W294G
-
inactive
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