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1.21.98.3: anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase

This is an abbreviated version!
For detailed information about anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase, go to the full flat file.

Reaction

131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester
+
S-adenosyl-L-methionine
=
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester
+
5'-deoxyadenosine
+
L-methionine

Synonyms

BChE, chlE, Cyan7425_4778, Cyan7822_3999, F_1025, Mg-protoporphyrin IX monomethyl ester cyclase, MPE cyclase, oxygen-independent Mg-protoporphyrin IX monomethyl ester cyclase

ECTree

     1 Oxidoreductases
         1.21 Catalysing the reaction X-H + Y-H = X-Y
             1.21.98 With other, known, physiological acceptors
                1.21.98.3 anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase

Cofactor

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

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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cobalamin
S-adenosyl-L-methionine
[4Fe-4S] cluster
ligated viaCys204, Cys208, Cys211
[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
additional information
membrane-localized BchE requires an additional, heat-sensitive cytosolic cobalamin component for activity, BchE catalysis is not sustained in chimeric experiments when a cytosolic extract from Escherichia coli is used as a substitute
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