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Literature summary extracted from

  • Reid, J.D.; Hunter, C.N.
    Current understanding of the function of magnesium chelatase (2002), Biochem. Soc. Trans., 30, 643-645.
    View publication on PubMed

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 Arabidopsis thaliana
-
ADP + phosphate + Mg-protoporphyrin IX + H+
-
?
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 Arabidopsis thaliana
-
-
-
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 Arabidopsis thaliana
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.

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
6.6.1.1 More ChlI subunit forms high-molecular-mass aggregates Synechocystis sp.