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