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Literature summary for 6.6.1.1 extracted from

  • Karger, G.A.; Reid, J.D.; Hunter, C.N.
    Characterization of the binding of deuteroporphyrin IX to the magnesium chelatase H subunit and spectroscopic properties of the complex (2001), Biochemistry, 40, 9291-9299.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Cereibacter sphaeroides
expression in Escherichia coli Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0057
-
deuteroporphyrin pH 7.7, 37ยบC, 100 nM ChlH subunit Synechocystis sp.
0.008
-
deuteroporphyrin pH 7.7, 37ยบC, 200 nM ChlH subunit Synechocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
110000
-
1 * 110000, gel filtration, BchH subunit Cereibacter sphaeroides
148000
-
1 * 148000, gel filtration, ChlH subunit Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-
Synechocystis sp.
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-protoporphyrin IX + 2 H+ complex three-subunit enzyme Cereibacter sphaeroides
ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-protoporphyrin IX + 2 H+ complex three-subunit enzyme Synechocystis sp.
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
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)

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

Subunits

Subunits Comment Organism
More 1 * 148000, gel filtration, ChlH subunit Synechocystis sp.
More 1 * 110000, gel filtration, BchH subunit Cereibacter sphaeroides
More ChlH forms high-molecular aggregates when preincubated with ATP and Mg2+ Synechocystis sp.