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Literature summary for 1.3.98.5 extracted from

  • Hobbs, C.; Dailey, H.; Shepherd, M.
    The HemQ coprohaem decarboxylase generates reactive oxygen species Implications for the evolution of classical haem biosynthesis (2016), Biochem. J., 473, 3997-4009 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Fe-coproporphyrin III + 2 H2O2 Staphylococcus aureus
-
 protoheme + 2 CO2 + 4 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus A0A0S3DY11
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Fe-coproporphyrin III + 2 H2O2
-
 Staphylococcus aureus protoheme + 2 CO2 + 4 H2O
-
 ?

General Information

General Information Comment Organism
physiological function HemQ can stimulate the generation of protoporphyrin IX but not coproporphyrin III Staphylococcus aureus