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Literature summary for 2.1.1.11 extracted from

  • Shepherd, M.; Reid, J.D.; Hunter, C.N.
    Purification and kinetic characterisation of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803 (2003), Biochem. J., 371, 351-360.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.11

Inhibitors

Inhibitors Comment Organism Structure
S-adenosyl-L-homocysteine competitive with respect to S-adenosyl-L-methionine and mixed inhibition with respect to magnesium protoporphyrin Synechocystis sp. PCC 6803

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.038
-
 S-adenosyl-L-methionine
-
 Synechocystis sp.
0.038
-
 S-adenosyl-L-methionine
-
 Synechocystis sp. PCC 6803

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
 PCC6803
-
Synechocystis sp. PCC 6803
-
 recombinant enzyme
-

Purification (Commentary)

Purification (Comment) Organism
-
 Synechocystis sp.
-
 Synechocystis sp. PCC 6803

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester ternary complex is likely to be formed either by a random or ordered addition of substrates Synechocystis sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + magnesium mesoporphyrin
-
 Synechocystis sp. S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
-
 ?
S-adenosyl-L-methionine + magnesium protoporphyrin
-
 Synechocystis sp. S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
-
 ?
S-adenosyl-L-methionine + magnesium protoporphyrin reaction proceeds through a ternary complex, substrate binding is not ordered Synechocystis sp. PCC 6803 S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
-
 ?

Synonyms

Synonyms Comment Organism
ChlM
-
 Synechocystis sp. PCC 6803