Literature summary for 2.1.1.11 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

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Inhibitors

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

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chromatophore	-	Cereibacter sphaeroides	-	-

Organism

Organism	UniProt	Comment	Textmining
Cereibacter sphaeroides	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Cereibacter sphaeroides

Reaction

Reaction	Comment	Organism	Reaction ID
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)

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

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Release 2023.1 (January 2023)