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Literature summary for 2.1.1.11 extracted from

  • Shepherd, M.; McLean, S.; Hunter, C.N.
    Kinetic basis for linking the first two enzymes of chlorophyll biosynthesis (2005), FEBS J., 272, 4532-4539.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
magnesium chelatase 0.004 mM, maximal stimulation of activity Synechocystis sp.

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0173
-
S-adenosyl-L-methionine at 30°C in 100 mM Tris pH 7.5 and 100 mM glycerol, in the presence of 0.004 mM magnesium chelatase Synechocystis sp.
0.0243
-
S-adenosyl-L-methionine at 30°C in 100 mM Tris pH 7.5 and 100 mM glycerol, in the absence of magnesium chelatase Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
strain PCC6803
-

Purification (Commentary)

Purification (Comment) Organism
chelating Sepharose fast-flow resin column chromatography and P-6 desalting gel filtration Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + magnesium protoporphyrin
-
Synechocystis sp. S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
-
?
S-adenosyl-L-methionine + tetrapyrrole
-
Synechocystis sp. ?
-
?

Synonyms

Synonyms Comment Organism
ChlM
-
Synechocystis sp.
magnesium protoporphyrin methyltransferase
-
Synechocystis sp.