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Literature summary for 6.6.1.1 extracted from

  • Sawicki, A.; Willows, R.D.
    Kinetic analyses of the magnesium chelatase provide insights into the mechanism, structure, and formation of the complex (2008), J. Biol. Chem., 283, 31294-31302.
    View publication on PubMed
Search for more literature for 6.6.1.1

KM Value [mM]

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

Organism UniProt Comment Textmining
Rhodobacter capsulatus
-
-
-

Substrates and Products (Substrate)

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

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