EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.3.3.3 | D274A | site-directed mutagensis, inactive mutant | Saccharomyces cerevisiae |
1.3.3.3 | H131A | site-directed mutagensis, inactive mutant | Saccharomyces cerevisiae |
1.3.3.3 | R135A | site-directed mutagensis, inactive mutant | Saccharomyces cerevisiae |
1.3.3.3 | R275A | site-directed mutagensis, inactive mutant | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.3.3 | coproporphyrinogen III + O2 + 2 H+ | Saccharomyces cerevisiae | - |
protoporphyrinogen-IX + 2 CO2 + 2 H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.3.3.3 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.3.3.3 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.3.3 | coproporphyrinogen III + O2 + 2 H+ | - |
Saccharomyces cerevisiae | protoporphyrinogen-IX + 2 CO2 + 2 H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.3.3.3 | dimer | - |
Saccharomyces cerevisiae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.3.3.3 | oxygen-dependent coproporphyrinogen III oxidase | - |
Saccharomyces cerevisiae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.3.3.3 | 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 |