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Literature summary extracted from

  • Hinchigeri, S.B.; Richards, W.R.
    The purification and reaction mechanism of S-adenosyl-L-methionine:magnesium protoporphyrin methyltransferase from Rhodopseudomonas sphaeroides (1982), Photosynthetica, 16, 554-560.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.11 S-adenosyl-L-homocysteine non-competitive inhibitor of Mg protoporphyrin Cereibacter sphaeroides

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.11 chromatophore
-
 Cereibacter sphaeroides
-
-

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.11 Cereibacter sphaeroides
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.11
-
 Cereibacter sphaeroides

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.11 S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester equilibrium-ordered bi bi mechanism Cereibacter sphaeroides
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.11 S-adenosyl-L-methionine + magnesium mesoporphyrin
-
 Cereibacter sphaeroides S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
-
 ?
2.1.1.11 S-adenosyl-L-methionine + magnesium protoporphyrin
-
 Cereibacter sphaeroides S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
-
 ?