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1.3.98.5: hydrogen peroxide-dependent heme synthase

This is an abbreviated version!
For detailed information about hydrogen peroxide-dependent heme synthase, go to the full flat file.

Word Map on EC 1.3.98.5

Reaction

Fe-coproporphyrin III
+ 2 H2O2 =
protoheme
 + 2 CO2 + 4 H2O

Synonyms

ChdC, coproheme decarboxylase, coproheme III oxidative decarboxylase, HemQ, Imo2113, lmo2113

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.98 With other, known, physiological acceptors
                1.3.98.5 hydrogen peroxide-dependent heme synthase

Crystallization

Crystallization on EC 1.3.98.5 - hydrogen peroxide-dependent heme synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and enzyme in complex with Fe-coproporphyrin III, vapor diffusion method, using 0.1 M bicine pH 9.0, 10% (w/v) PEG6000
apo-enzyme, to 2.0 A resolution
HemQ crystallized as a pentamer in space group P1211, to 1.69 A resolution
modeling of structure. HemQ enzymes lack the conserved arginine that is common to chlorite dismutases. A fully conserved tryptophan/tyrosine pair is buried deep in the active site cleft and fully conserved arginine residues at opposite ends of the distal pocket. A fully conserved glutamate residue is adjacent to the conserved tryptophan