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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.98.5 expression in Escherichia coli Staphylococcus aureus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.98.5 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)

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

Organism

EC Number Organism UniProt Comment Textmining
1.3.98.5 Staphylococcus aureus A0A0S3DY11
-
-

Substrates and Products (Substrate)

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

General Information

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