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Literature summary for 6.6.1.1 extracted from

  • Viney, J.; Davison, P.A.; Hunter, C.N.; Reid, J.D.
    Direct measurement of metal-ion chelation in the active site of the AAA(+) ATPase magnesium chelatase (2007), Biochemistry, 46, 12788-12794.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + deuteroporphyrin IX + Mg2+ + H2O Synechocystis sp. magnesium chelatase catalyzes the first committed step in chlorophyll biosynthesis ADP + phosphate + Mg-deuteroporphyrin IX + H+
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Organism

Organism UniProt Comment Textmining
Synechocystis sp.
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + deuteroporphyrin IX + Mg2+ + H2O magnesium chelatase catalyzes the first committed step in chlorophyll biosynthesis Synechocystis sp. ADP + phosphate + Mg-deuteroporphyrin IX + H+
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ATP + deuteroporphyrin IX + Mg2+ + H2O MgATP2- binding occurs after the rate-determining step, nucleotide binding acts to clamp the chelatase in a product complex Synechocystis sp. ADP + phosphate + Mg-deuteroporphyrin IX + H+
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