Protein Variants | Comment | Organism |
---|---|---|
D41N | specific activity of the mutant enzyme is 9.1% of the wild-type enzyme, activation by Co2+ is less than 2fold the level of activation of the wild-type enzyme | Escherichia coli |
D84N | mutant enzyme exhibits 900fold decreased specific activity and increased level of activation by Co2+, 2700fold compared with approximately 40fold for the wild-type enzyme | Escherichia coli |
E118Q | specific activity of the mutant enzyme is 6.1% of the wild-type enzyme, activation by Co2+ is 2.5fold the level of activation of the wild-type enzyme | Escherichia coli |
H117N | specific activity of the mutant enzyme is 0.037% of the wild-type activity in presence of Co2+ and 0.042% of the wild-type activity in absence of Co2+ | Escherichia coli |
H217N | specific activity of the mutant enzyme is 0.23% of the wild-type enzyme. Activation by Co2+ is approximately 6fold the level of activation of the wild-type enzyme | Escherichia coli |
H43N | specific activity of the mutant enzyme is 0.76% of the wild-type enzyme, activation by Co2+ is 4fold less than the activation of the wild-type enzyme | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | activation is due to zinc ion displacement at only one of two metal-ion-binding sites, displacement occurs at the metal-ion bionding site consisting of the residues Asp84, Asn116, His217 and His252. Km for wild-type enzyme: 0.0925 mM | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |