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Literature summary extracted from

  • Boeggeman, E.; Qasba, P.K.
    Studies on the metal binding sites in the catalytic domain of beta1,4-galactosyltransferase (2002), Glycobiology, 12, 395-407.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.38 expression in Escherichia coli Bos taurus
2.4.1.90 expression in Escherichia coli Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.38 D254E 0.01% of the activity of the wild-type enzyme Bos taurus
2.4.1.38 D254N 0.01% of the activity of the wild-type enzyme Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 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 Bos taurus
2.4.1.38 additional information mutations of Asp318 and Asp319 abolish enzyme activity Bos taurus
2.4.1.90 D254E 0.01% of the activity of the wild-type enzyme Bos taurus
2.4.1.90 D254N 0.01% of the activity of the wild-type enzyme Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 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 Bos taurus
2.4.1.90 additional information mutations of Asp318 and Asp319 abolish enzyme activity Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.38 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 Bos taurus
2.4.1.90 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 Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.38 Bos taurus
-
-
-
2.4.1.90 Bos taurus
-
-
-