KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.091 | - |
ATP | 30°C, apparent Km value | Rhodobacter capsulatus | |
1.3 | - |
Mg2+ | 30°C, apparent Km value | Rhodobacter capsulatus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodobacter capsulatus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + protoporphyrin IX + Mg2+ + H2O | - |
Rhodobacter capsulatus | ADP + phosphate + Mg-protoporphyrin IX + H+ | - |
? | |
additional information | enzyme is composed of subunits BchI, BchD, BchH. The BchIBchD complex has intrinsic ATPase activity, and addition of BchH greatly increased ATPase activity. This is concentration-dependent and gives sigmoidal kinetics. ATPase activity is about 40fold higher than magnesium chelatase activity and continues despite cessation of magnesium chelation, implying secondary roles for ATP hydrolysis. Porphyrin binding is the rate limiting step in catalysis | Rhodobacter capsulatus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | enzyme is composed of subunits BchI, BchD, BchH. The BchIBchD complex has intrinsic ATPase activity, and addition of BchH greatly increased ATPase activity. This is concentration-dependent and gives sigmoidal kinetics. ATPase activity is about 40fold higher than magnesium chelatase activity and continues despite cessation of magnesium chelation, implying secondary roles for ATP hydrolysis | Rhodobacter capsulatus |