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
Search for more literature for 1.3.98.3

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ copper affects tetrapyrrole biosynthesis presumably at the level of the SAM and [4Fe-4S] containing HemN enzyme. Members of the radical SAM enzyme family are copper sensitive. The excess copper target in the tetrapyrrole pathway is the anaerobic coproporphyrinogen III oxidase [4Fe-4S] containing HemN 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
-
-

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
HemN
-
 Rubrivivax gelatinosus

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S] cluster
-
 Rubrivivax gelatinosus

Expression

Organism Comment Expression
Rubrivivax gelatinosus HemN expression or activity is affected in the copA- mutant under excess copper down

General Information

General Information Comment Organism
malfunction excess copper in the copA- mutant, deficient for Cu+-ATPase CopA via transposon mutagenesis, results in a substantial decrease of the cytochrome c oxidase and the photosystem under microaerobic and anaerobic conditions together with the extrusion of coproporphyrin III. Enzyme CopA is required for the activity of cuproproteins in the purple bacterium Rubrivivax gelatinosus. CopA is not directly required for cytochrome c oxidase activity but is vital for copper tolerance. The Cu+-ATPase CtpA is required only for the activity of cuproproteins in the purple bacterium Rubrivivax gelatinosus Rubrivivax gelatinosus
physiological function coproporphyrinogen III is converted to protoporphyrinogen IX under anaerobiosis and low oxygen tension by the anaerobic coproporphyrinogen III oxidase HemN. The Cu+-ATPase CopA is not directly required for cytochrome c oxidase but is vital for copper tolerance. The physiological role of the copper P1B-type transporter CtpA, though homologous to CopA, differs from that of the effluxATPase CopA, because CtpA is dispensable for copper tolerance in contrast to CopA. HemN, a radical SAM and iron-sulfur containing protein, is a target enzyme in the tetrapyrrole biosynthesis pathway Rubrivivax gelatinosus