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Literature summary for 1.3.3.3 extracted from

  • Silva, P.J.; Ramos, M.J.
    Computational characterization of the substrate-binding mode in coproporphyrinogen III oxidase (2011), J. Phys. Chem. B, 115, 1903-1910.
    View publication on PubMed
Search for more literature for 1.3.3.3

Protein Variants

Protein Variants Comment Organism
D274A site-directed mutagensis, inactive mutant Saccharomyces cerevisiae
H131A site-directed mutagensis, inactive mutant Saccharomyces cerevisiae
R135A site-directed mutagensis, inactive mutant Saccharomyces cerevisiae
R275A site-directed mutagensis, inactive mutant Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
coproporphyrinogen III + O2 + 2 H+ Saccharomyces cerevisiae
-
 protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O reaction mechanism, substrate docking study and binding mode, involving residues H131, R135, D274, and R275, and active site analysis using crystal structures, molecular dynamics simulations, overview. Selectivity of the active site, formed by His131, Asn133, and Ser117, toward substituted tetrapyrroles, nonoccurrence of catalysis on the C and D rings of the tetrapyrrole. The carbonyl oxygen of G276 intervenes in the substrate anchoring by hydrogen bonding of the ring D pyrrole NH group. The pyrrole ring is very unlikely to undergo deprotonation during the catalytic cycle Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
coproporphyrinogen III + O2 + 2 H+
-
 Saccharomyces cerevisiae protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
oxygen-dependent coproporphyrinogen III oxidase
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
metabolism oxygen-dependent coproporphyrinogen III oxidase catalyzes the sequential decarboxylation of the propionate substituents present on the A and B rings of coproporphyrinogen III in the heme biosynthetic pathway Saccharomyces cerevisiae