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Literature summary for 6.6.1.1 extracted from

  • Willows, R.D.; Gibson, L.C.; Kanangara, C.G.; Hunter, C.N.; von Wettstein, D.
    Three separate proteins constitute the magnesium chelatase of Rhodobacter sphaeroides (1996), Eur. J. Biochem., 235, 438-443.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Cereibacter sphaeroides

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
2 * 40000, BchI subunit Cereibacter sphaeroides
70000
-
8 * 70000, D subunit, the molecular mass of the polymeric protein is approximately 550000 Da Cereibacter sphaeroides
140000
-
1 * 140000, BchH subunit Cereibacter sphaeroides

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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 Cereibacter sphaeroides

Subunits

Subunits Comment Organism
dimer 2 * 40000, BchI subunit Cereibacter sphaeroides
More 1 * 140000, BchH subunit Cereibacter sphaeroides
More the enzyme has three subunits, BchI, BchH and BchD Cereibacter sphaeroides
octamer 8 * 70000, D subunit, the molecular mass of the polymeric protein is approximately 550000 Da Cereibacter sphaeroides