Cloned (Comment) | Organism |
---|---|
- |
Pyrococcus horikoshii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
26000 | - |
2 * 26000, calculated. Equilibrium analytical ultracentrifugation measurements performed on the apoenzyme and its complexes with biotin and bio-5-AMP all yield molecular weights for the protein consistent with a dimer. Regardless of ligation state the Pyrococcus horikoshii enzyme is a dimer | Pyrococcus horikoshii |
51200 | - |
sedimentation equilibrium study | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O57883 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant protein | Pyrococcus horikoshii |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
biotin binding shows an equilibrium constant of 200 nMat 20°C. The equilibrium dissociation constant increases by approximately four fold on increasing the temperature from 10°C to 50°C | Pyrococcus horikoshii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + biotin + apo-[acetyl CoA carboxylase] | no coupling is observed in ATP and biotin binding to the BPL | Pyrococcus horikoshii | AMP + diphosphate + acetyl CoA carboxylase | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 26000, calculated. Equilibrium analytical ultracentrifugation measurements performed on the apoenzyme and its complexes with biotin and bio-5'-AMP all yield molecular weights for the protein consistent with a dimer. Regardless of ligation state the Pyrococcus horikoshii enzyme is a dimer | Pyrococcus horikoshii |
Synonyms | Comment | Organism |
---|---|---|
BPL | - |
Pyrococcus horikoshii |