A protoporphyrinogen oxidase that is encoded in the genome of human. [PRO:DNx, UniProtKB:P50336]
PPO;
EC 1.3.3.4
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 3 (100.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| oxadiazon | Homo sapiens (human) | Ki | 2.9300 | 1 | 1 |
| acifluorfen | Homo sapiens (human) | Ki | 1.7100 | 1 | 1 |
| n-(2,4-dichloro-5-(4-(difluoromethyl)-4,5-dihydro-3-methyl-5-oxo-1h-1,2,4-triazol-1-yl)phenyl)methanesulfonamide | Homo sapiens (human) | Ki | 0.7215 | 2 | 3 |
This protein enables 2 target(s):
| Target | Category | Definition |
|---|---|---|
| oxygen-dependent protoporphyrinogen oxidase activity | molecular function | Catalysis of the reaction: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX. [EC:1.3.3.4, RHEA:25576] |
| flavin adenine dinucleotide binding | molecular function | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. [GOC:ai, GOC:imk, ISBN:0198506732] |
This protein is located in 3 target(s):
| Target | Category | Definition |
|---|---|---|
| mitochondrial inner membrane | cellular component | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. [GOC:ai] |
| mitochondrial intermembrane space | cellular component | The region between the inner and outer lipid bilayers of the mitochondrial envelope. [GOC:mah] |
| mitochondrial membrane | cellular component | Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. [GOC:mah, NIF_Subcellular:sao1045389829] |
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|---|---|
| mitochondrial inner membrane | cellular component | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. [GOC:ai] |
This protein is involved in 6 target(s):
| Target | Category | Definition |
|---|---|---|
| porphyrin-containing compound biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group. [GOC:jl, ISBN:0198506732, Wikipedia:Porphyrin#Natural_formation] |
| protoporphyrinogen IX biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX. [GOC:go_curators] |
| heme biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors. [GOC:jl, PMID:11788607] |
| heme A biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of heme A, a derivative of heme found in cytochrome aa3. [GOC:ai, PMID:11788607] |
| heme B biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of heme B, a Fe(II) porphyrin complex readily isolated from the hemoglobin of beef blood, but also found in other proteins including other hemoglobins, myoglobins, cytochromes P-450, catalases, peroxidases as well as b type cytochromes. [GOC:yaf, PMID:29414780] |
| heme O biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of heme O, a derivative of heme containing a 17-carbon hydroxyethylfarnesyl side chain at position 8 of the tetrapyrrole macrocycle. [GOC:jid] |