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Information on EC 1.3.5.3 - protoporphyrinogen IX dehydrogenase (menaquinone) for references in articles please use BRENDA:EC1.3.5.3
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EC Tree
IUBMB Comments This enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments.
The expected taxonomic range for this enzyme is: Escherichia coli
Synonyms
hemg protein,
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protoporphyrinogen IX oxidase
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protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol
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protoporphyrinogen IX:menadione oxidoreductase
This enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments.
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protoporphyrinogen IX + 3 menadione
protoporphyrin IX + 3 menadiol
protoporphyrinogen IX + 3 menaquinone
protoporphyrin IX + 3 menaquinol
protoporphyrinogen IX + 3 triphenyltetrazolium chloride
protoporphyrin IX + ?
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artificial electron acceptor
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protoporphyrinogen IX + 3 ubiquinone
protoporphyrin IX + 3 ubiquinol
additional information
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potential electron acceptors, i.e. 2, 6-dichloroindophenol, phenazine methosulfate, menadione, and vitamin K1, respectively, directly oxidize the substrate in the absence of HemG
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protoporphyrinogen IX + 3 menadione
protoporphyrin IX + 3 menadiol
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the enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments
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protoporphyrinogen IX + 3 menadione
protoporphyrin IX + 3 menadiol
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HemG is specific for protoporphyrinogen. Neither mesoporphyrinogen nor coproporphyrinogen is oxidized by HemG
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protoporphyrinogen IX + 3 menaquinone
protoporphyrin IX + 3 menaquinol
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protoporphyrinogen IX + 3 menaquinone
protoporphyrin IX + 3 menaquinol
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under anaerobic conditions
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protoporphyrinogen IX + 3 ubiquinone
protoporphyrin IX + 3 ubiquinol
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protoporphyrinogen IX + 3 ubiquinone
protoporphyrin IX + 3 ubiquinol
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under aerobic conditions
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protoporphyrinogen IX + 3 menadione
protoporphyrin IX + 3 menadiol
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the enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments
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protoporphyrinogen IX + 3 menaquinone
protoporphyrin IX + 3 menaquinol
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under anaerobic conditions
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protoporphyrinogen IX + 3 ubiquinone
protoporphyrin IX + 3 ubiquinol
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under aerobic conditions
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FMN
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contains FMN
FMN
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no direct electron transfer to a terminal oxidoreductase
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0.00376
menadione
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pH 8.0, 37°C
0.0173
menaquinone
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recombinant His-tagged enzyme, pH and temperature not specified in the publication
0.007
protoporphyrinogen IX
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pH 8.0, 37°C
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0.281
menadione
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pH 8.0, 37°C
0.292
protoporphyrinogen IX
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pH 8.0, 37°C
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74.73
menadione
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pH 8.0, 37°C
41.7
protoporphyrinogen IX
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pH 8.0, 37°C
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0.0000042
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membrane associated enzyme with substrates protoporphyrinogen IX and triphenyltetrazolium chloride, pH and temperature not specified in the publication
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brenda
gene hemG
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brenda
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associated
brenda
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physiological function
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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
additional information
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detailed model of heme biosynthesis coupled energy generation, overview
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22000
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4 * 22000, SDS-PAGE
22500
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4 * 22500, calculated from sequence
150000
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recombinant enzyme, gel filtration
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tetramer
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4 * 22000, SDS-PAGE; 4 * 22500, calculated from sequence
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additional information
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Escherichia coli strain SASX38 lacks functional protoporphyrinogen IX dehydrogenase activity and is reported to be deficient in HemG. Sequence analysis of the SASX38 hemG gene reveals a deletion from nucleotide 152 to 470. This results in a predicted HemG protein that remains in frame but lacks 106 internal amino acids, including the long chain insert loop
additional information
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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
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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
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six histidine-tagged recombinant protein
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gene hemG, expression of His-tagged enzyme in Bacillus megaterium
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Boynton, T.O.; Daugherty, L.E.; Dailey, T.A.; Dailey, HA.
Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity
Biochemistry
48
6705-6711
2009
Escherichia coli
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Moebius, K.; Arias-Cartin, R.; Breckau, D.; Haennig, A.L.; Riedmann, K.; Biedendieck, R.; Schroeder, S.; Becher, D.; Magalon, A.; Moser, J.; Jahn, M.; Jahn, D.
Heme biosynthesis is coupled to electron transport chains for energy generation
Proc. Natl. Acad. Sci. USA
107
10436-10441
2010
Escherichia coli
brenda
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1.3.5.3 protoporphyrinogen IX dehydrogenase (menaquinone)
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