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Literature summary for 1.21.98.3 extracted from

  • Gough, S.P.; Petersen, B.O.; Duus, J.O.
    Anaerobic chlorophyll isocyclic ring formation in Rhodobacter capsulatus requires a cobalamin cofactor (2000), Proc. Natl. Acad. Sci. USA, 97, 6908-6913.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus P26168
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Rhodobacter capsulatus ATCC BAA-309 P26168
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
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Rhodobacter capsulatus 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
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?
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
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Rhodobacter capsulatus ATCC BAA-309 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
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?
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
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Rhodobacter capsulatus 3,8-divinyl protochlorophyllide a + 5'-deoxyadenosine + L-methionine
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?
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
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Rhodobacter capsulatus ATCC BAA-309 3,8-divinyl protochlorophyllide a + 5'-deoxyadenosine + L-methionine
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?
magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine + H2O
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Rhodobacter capsulatus 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
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?
magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine + H2O
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Rhodobacter capsulatus ATCC BAA-309 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
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?

Cofactor

Cofactor Comment Organism Structure
Cobalamin vitamin B12-requiring mutants of the bluE and bluB genes of Rhodobacter capsulatus, grown without B12, accumulate Mg-protoporphyrin monomethyl ester and its 3-vinyl-8-ethyl derivative. Cyclase activity in the B12-dependent mutants requires vitamin B12 but not protein synthesis Rhodobacter capsulatus

General Information

General Information Comment Organism
metabolism proposed reaction mechanism for the Mg-protoporphyrin monomethyl ester-cyclase reaction starts with adenosylcobalamin forming the adenosyl radical, which leads to withdrawal of a hydrogen atom and formation of the benzylic-type 131-radical of Mg-protoporphyrin monomethyl ester. Withdrawal of an electron gives the 131-cation of Mg-protoporphyrin monomethyl ester. Hydroxyl ion attack on the cation gives 131-hydroxy-Mg-protoporphyrin monomethyl ester. Withdrawal of three hydrogen atoms leads successively to 131-keto-Mg-protoporphyrin monomethyl ester, its 132-Mg-protoporphyrin monomethyl ester, and cyclization to protochlorophyllide Rhodobacter capsulatus