EC Number | Cloned (Comment) | Organism |
---|---|---|
1.3.3.4 | gene LMJF_06_1280, the gene forms a potential transcriptional unit with gene LMJF_06_1270 encoding CPO, coproporphyrinogen III oxidase, EC 1.3.3.3, and with gene LMJF_06_1290 for a cytochrome b5, functional complementation of the Escherichia coli C43(DE3) LG285 DELTAhemG strain, recombinant expression of wild-type and mutant enzymes | Leishmania major |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.3.3.4 | R142A | site-directed mutagenesis, the mutant shows 50fold reduced activity compared to the wild-type enzyme | Leishmania major |
1.3.3.4 | Y134F | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Leishmania major |
1.3.3.4 | Y137A | site-directed mutagenesis, inactive mutant | Leishmania major |
1.3.3.4 | Y137F | site-directed mutagenesis, inactive mutant | Leishmania major |
1.3.3.4 | Y137S | site-directed mutagenesis, inactive mutant | Leishmania major |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.3.4 | additional information | Leishmania major | the enzyme from Leishmania major also shows a physiological ferrochelatase activity | ? | - |
? | |
1.3.3.4 | protoporphyrinogen IX + 3 O2 | Leishmania major | - |
protoporphyrin IX + 3 H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.3.3.4 | Leishmania major | Q4QIU7 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.3.3.4 | amastigote | - |
Leishmania major | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.3.4 | additional information | the enzyme from Leishmania major also shows a physiological ferrochelatase activity | Leishmania major | ? | - |
? | |
1.3.3.4 | additional information | purified recombinant Leishmania major HemG gene product reveals PPO activity in vitro using different ubiquinones and triphenyltetrazolium as electron acceptors. FMN is identified as the physiological Leishmania major HemG cofactor | Leishmania major | ? | - |
? | |
1.3.3.4 | protoporphyrinogen IX + 3 O2 | - |
Leishmania major | protoporphyrin IX + 3 H2O2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.3.3.4 | ? | x * 42000, recombinant wild-type enzyme, SDS-PAGE | Leishmania major |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.3.3.4 | HemG | - |
Leishmania major |
1.3.3.4 | HemG-type PPO | - |
Leishmania major |
1.3.3.4 | HemG-type protoporphyrinogen IX oxidase | - |
Leishmania major |
1.3.3.4 | LMJF_06_1280 | - |
Leishmania major |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.3.3.4 | FMN | - |
Leishmania major | |
1.3.3.4 | additional information | purified recombinant Leishmania major HemG gene product reveals PPO activity in vitro using different ubiquinones and triphenyltetrazolium as electron acceptors. FMN is identified as the physiological Leishmania major HemG cofactor | Leishmania major |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.3.3.4 | evolution | HemG proteins are highly related to flavodoxin proteins, crystal structure analysis | Leishmania major |
1.3.3.4 | additional information | the active site residues are essential for HemG catalysis, spectral analysis of heme biosynthesis, overview | Leishmania major |
1.3.3.4 | physiological function | the enzyme also shows a physiological ferrochelatase activity. Partial heme biosynthesis from phagocyte-derived heme precursors in Leishmania major is highly probable. It serves most probably to haemoprotein formation during the amastigotic state in the macrophage, model for the intracellular localization of heme synthetic enzymes and heme trafficking in Leishmania major amastigotes, overview | Leishmania major |