Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.98.3 extracted from

  • Azzouzi, A.; Steunou, A.S.; Durand, A.; Khalfaoui-Hassani, B.; Bourbon, M.L.; Astier, C.; Bollivar, D.W.; Ouchane, S.
    Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu+-ATPase mutant copA- of Rubrivivax gelatinosus (2013), Mol. Microbiol., 88, 339-351.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ Cu2+ affects tetrapyrrole biosynthesis presumably at the level of the S-adenosyl-L-methionine and [4Fe-4S] containing HemN enzyme, copper targets the 4Fe-4S clusters in the anaerobic enzyme Rubrivivax gelatinosus
O2 O2 affects tetrapyrrole biosynthesis presumably at the level of the S-adenosyl-L-methionine and [4Fe-4S] containing HemN enzyme Rubrivivax gelatinosus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ HemN is a radical S-adenosyl-L-methionine and [4Fe-4S] containing enzyme Rubrivivax gelatinosus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
coproporphyrinogen III + 2 S-adenosyl-L-methionine Rubrivivax gelatinosus
-
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
?

Organism

Organism UniProt Comment Textmining
Rubrivivax gelatinosus I0HU37 gene hemN
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
coproporphyrinogen III + 2 S-adenosyl-L-methionine
-
Rubrivivax gelatinosus protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
?

Synonyms

Synonyms Comment Organism
anaerobic coproporphyrinogen III oxidase
-
Rubrivivax gelatinosus
coproporphyrinogen III oxidase
-
Rubrivivax gelatinosus
HemN
-
Rubrivivax gelatinosus

Cofactor

Cofactor Comment Organism Structure
heme
-
Rubrivivax gelatinosus
S-adenosyl-L-methionine HemN is a radical S-adenosyl-L-methionine and [4Fe-4S] containing enzyme Rubrivivax gelatinosus

General Information

General Information Comment Organism
evolution the anaerobic [4Fe-4S] containing enzymes have been replaced in metabolic pathways by more efficient and stable aerobic versions as a response and adaptation to oxygen appearance on earth, with copper damages [4Fe-4S] cluster under anaerobiosis or limited oxygen tensionplaying a role in the selection pressure leading to the evolution of copper/oxygen tolerant enzymes, copper targets the 4Fe-4S clusters in the anaerobic enzymes Rubrivivax gelatinosus
malfunction oxidized coproporphyrinogen III accumulates in a hemN2- mutant in Rubrivirax gelatinosus only under oxygen limited conditions Rubrivivax gelatinosus
metabolism the enzyme is involved in the O2-independent tetrapyrrole biosynthesis pathway, regulation overview Rubrivivax gelatinosus
additional information a mutant Rubrivivax gelatinosus deficient in the Cu2+-ATPase CopA accumulates coproporphyrinogen III, excess copper affects the synthesis of tetrapyrroles, affecting the heme and chlorophyll containing complexes Rubrivivax gelatinosus