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Literature summary extracted from

  • Jensen, P.E.; Reid, J.D.; Hunter, C.N.
    Modification of cysteine residues in the ChlI and ChlH subunits of magnesium chelatase results in enzyme inactivation (2000), Biochem. J., 352, 435-441.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.6.1.1 expression in Escherichia coli Synechocystis sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.6.1.1 N-ethylmaleimide binds to ChlI subunit and inhibits its ATPase activity. The ChlI-ChlD-ATP complex forms but cannot catalyse magnesium chelation. Prior incubation with MgATP2- affords protection. Full protection can also be obtained with 5 mM ATP or 5 mM ADP alone Synechocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.6.1.1 ATP + protoporphyrin IX + Mg2+ + H2O Synechocystis sp.
-
 ADP + phosphate + Mg-protoporphyrin IX + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.6.1.1 Synechocystis sp.
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.6.1.1 ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-protoporphyrin IX + 2 H+ this is the first committed step of chlorophyll biosynthesis and is a branchpoint of two major routes in the tetrapyrrole pathway Synechocystis sp.
a

Substrates and Products (Substrate)

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