Information on EC 1.21.98.3 - anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.21.98.3
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RECOMMENDED NAME
GeneOntology No.
anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine = 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
show the reaction diagram
(1b)
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131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine = 3,8-divinyl protochlorophyllide a + 5'-deoxyadenosine + L-methionine
show the reaction diagram
(1c)
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magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O = 3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
show the reaction diagram
overall reaction
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magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine + H2O = 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
show the reaction diagram
(1a)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Porphyrin and chlorophyll metabolism
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SYSTEMATIC NAME
IUBMB Comments
magnesium-protoporphyrin-IX 13-monomethyl ester,S-adenosyl-L-methionine:H2O oxidoreductase (hydroxylating)
This radical AdoMet enzyme participates in the biosynthesis of chlorophyllide a in anaerobic bacteria, catalysing the formation of an isocyclic ring. Contains a [4Fe-4S] cluster and a cobalamin cofactor. The same transformation is achieved in aerobic organisms by the oxygen-dependent EC 1.14.13.81, magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase. Some facultative phototrophic bacteria, such as Rubrivivax gelatinosus, possess both enzymes.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
show the reaction diagram
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
3,8-divinyl protochlorophyllide a + 5'-deoxyadenosine + L-methionine
show the reaction diagram
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
show the reaction diagram
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overall reaction
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?
magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine + H2O
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cobalamin
[4Fe-4S]-center
BchE sequence displays the conserved CXXXCXXC sequence essential for 4Fe-4S cluster formation and an active 4Fe-4S cluster is present in the protein. Isolated protein is yellow-brown in colour with an absorption peak around 410 nm
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
86000
SDS-PAGE of truncated protein of 384 residues
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 63000, calculated, 2 * 43000, SDS-PAGE of truncated protein of 384 residues
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein, preparation is yellow-brown in color. Only a small fraction can be solubilized with urea (6 M), and most of the iron-sulfur cluster is degraded upon solubilization of inclusion bodies
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the BchE gene is oxygen-independent
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis