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Literature summary for 2.4.1.38 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)

Cloned (Comment) Organism
expression in Escherichia coli Bos taurus

Protein Variants

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

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Bos taurus
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