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Literature summary for 6.6.1.1 extracted from

  • Reid, J.D.; Hunter, C.N.
    Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803 (2004), J. Biol. Chem., 279, 26893-26899.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0032
-
deuteroporphyrin IX
-
Synechocystis sp.
0.45
-
ATP
-
Synechocystis sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the magnesium-rich form of the chelatase is a more effective catalyst of the chelation reaction. Magnesium activation of the chelatase increases V, as well as the specificity constant for the reaction of MgATP2- Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
PCC6803
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + deuteroporphyrin IX + Mg2+ + H2O
-
Synechocystis sp. ADP + phosphate + Mg-deuteroporphyrin IX + H+
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.013
-
deuteroporphyrin IX
-
Synechocystis sp.