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
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1.3.98.5
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propionate
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raman
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listeria
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monocytogenes
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propionyl
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decarboxylases
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monoderm
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uv-vis
- 1.3.98.5
- propionate
-
raman
-
listeria
- monocytogenes
-
propionyl
- decarboxylases
-
monoderm
-
uv-vis
Reaction
Synonyms
ChdC, coproheme decarboxylase, coproheme III oxidative decarboxylase, HemQ, Imo2113, lmo2113
ECTree
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Cofactor
Cofactor on EC 1.3.98.5 - hydrogen peroxide-dependent heme synthase
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heme
ferric five-coordinated coproheme iron of HemQ is weakly bound by a neutral proximal histidine H174
heme
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heme is a high spin ferric iron and is ligated by a conserved histidine with the sixth coordination site available for binding a small molecule
heme
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heme is a high spin ferric iron and is ligated by a conserved histidine with the sixth coordination site available for binding a small molecule
heme
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heme is a high spin ferric iron and is ligated by a conserved histidine with the sixth coordination site available for binding a small molecule
heme
the presence of a heme cofactor bound to the enzyme does not seem to modify the biochemical and enzymatic properties of HemQ