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Literature summary for 1.3.5.3 extracted from
- Heme biosynthesis is coupled to electron transport chains for energy generation (2010), Proc. Natl. Acad. Sci. USA, 107, 10436-10441.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene hemG, expression of His-tagged enzyme in Bacillus megaterium | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | four electron transport chains from HemG via diverse quinones to cytochrome bo3, cytochrome bd, nitrate reductase, and fumarate reductase were reconstituted in vitro from purified components, overview | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0173 | - |
menaquinone | recombinant His-tagged enzyme, pH and temperature not specified in the publication | Escherichia coli |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | associated | Escherichia coli | 16020 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 150000 | - |
recombinant enzyme, gel filtration | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protoporphyrinogen IX + 3 menaquinone | Escherichia coli | under anaerobic conditions | protoporphyrin IX + 3 menaquinol | - |
? | |
| protoporphyrinogen IX + 3 ubiquinone | Escherichia coli | under aerobic conditions | protoporphyrin IX + 3 ubiquinol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
gene hemG | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme solubilized from membranes by anion exchange chromatography, recombinant His-tagged enzyme from Bacillus megaterium byy affinity chromatography and gel filtration. Removal of the fused His-tag via protease digestion does not change the catalytic properties | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.0000042 | - |
membrane associated enzyme with substrates protoporphyrinogen IX and triphenyltetrazolium chloride, pH and temperature not specified in the publication | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | potential electron acceptors, i.e. 2, 6-dichloroindophenol, phenazine methosulfate, menadione, and vitamin K1, respectively, directly oxidize the substrate in the absence of HemG | Escherichia coli | ? | - |
? | |
| protoporphyrinogen IX + 3 menaquinone | - |
Escherichia coli | protoporphyrin IX + 3 menaquinol | - |
? | |
| protoporphyrinogen IX + 3 menaquinone | under anaerobic conditions | Escherichia coli | protoporphyrin IX + 3 menaquinol | - |
? | |
| protoporphyrinogen IX + 3 triphenyltetrazolium chloride | artificial electron acceptor | Escherichia coli | protoporphyrin IX + ? | - |
? | |
| protoporphyrinogen IX + 3 ubiquinone | - |
Escherichia coli | protoporphyrin IX + 3 ubiquinol | - |
? | |
| protoporphyrinogen IX + 3 ubiquinone | under aerobic conditions | Escherichia coli | protoporphyrin IX + 3 ubiquinol | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | - |
Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HemG | - |
Escherichia coli |
| PPO | - |
Escherichia coli |
| protoporphyrinogen IX oxidase | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FMN | no direct electron transfer to a terminal oxidoreductase | Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | detailed model of heme biosynthesis coupled energy generation, overview | Escherichia coli |
| physiological function | the FMN enzyme protoporphyrinogen IX oxidase (HemG) of Escherichia coli abstracts six electrons from its substrate and transfers them via ubiquinone, cytochrome bo3 and cytochrome bd oxidase to oxygen. Under anaerobic conditions electrons are transferred via menaquinone, fumarate and nitrate reductase. Cytochrome bo3 , cytochrome bd, and nitrate reductase contribute to the proton motive force that drives ATP formation | Escherichia coli |
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