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
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propionyl
- decarboxylases
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monoderm
-
uv-vis
Reaction
Synonyms
ChdC, coproheme decarboxylase, coproheme III oxidative decarboxylase, HemQ, Imo2113, lmo2113
ECTree
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General Information
General Information on EC 1.3.98.5 - hydrogen peroxide-dependent heme synthase
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metabolism
physiological function
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the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro
metabolism
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the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro
metabolism
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the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro
metabolism
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the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro
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Actinobacteria and Firmicutes (high-GC and low-GC Gram-positive bacteria) are unable to synthesize protoporphyrin. Instead, they oxidize coproporphyrinogen to coproporphyrin, insert ferrous iron to make Fe-coproporphyrin (coproheme), and then decarboxylate coproheme to generate protoheme. This pathway is specified by three genes named hemY, hemH, and hemQ and is the most ancient heme synthesis pathway in the Eubacteria
physiological function
enzymes HemY, HemH and HemQ act as a coproporphyrinogen III oxidase, coproporphyrin III ferrochelatase and Fe-coproporphyrin III oxidase/dehydrogenase
physiological function
HemQ can stimulate the generation of protoporphyrin IX but not coproporphyrin III
physiological function
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the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme
physiological function
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the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme
physiological function
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the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme