We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 1.3.5.3 - protoporphyrinogen IX dehydrogenase (menaquinone) for references in articles please use BRENDA:EC1.3.5.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments This enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments.
The enzyme appears in viruses and cellular organisms
Synonyms
HemG, HemG protein, PPO, protoporphyrinogen IX oxidase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
protoporphyrinogen IX oxidase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
protoporphyrinogen IX:menadione oxidoreductase
This enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
protoporphyrinogen IX + 3 menadione
protoporphyrin IX + 3 menadiol
protoporphyrinogen IX + 3 menaquinone
protoporphyrin IX + 3 menaquinol
protoporphyrinogen IX + 3 triphenyltetrazolium chloride
protoporphyrin IX + ?
-
artificial electron acceptor
-
-
?
protoporphyrinogen IX + 3 ubiquinone
protoporphyrin IX + 3 ubiquinol
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
-
-
-
protoporphyrinogen IX + 3 menadione
protoporphyrin IX + 3 menadiol
-
the enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments
-
-
?
protoporphyrinogen IX + 3 menadione
protoporphyrin IX + 3 menadiol
-
HemG is specific for protoporphyrinogen. Neither mesoporphyrinogen nor coproporphyrinogen is oxidized by HemG
-
-
?
protoporphyrinogen IX + 3 menaquinone
protoporphyrin IX + 3 menaquinol
-
-
-
-
?
protoporphyrinogen IX + 3 menaquinone
protoporphyrin IX + 3 menaquinol
-
under anaerobic conditions
-
-
?
protoporphyrinogen IX + 3 ubiquinone
protoporphyrin IX + 3 ubiquinol
-
-
-
-
?
protoporphyrinogen IX + 3 ubiquinone
protoporphyrin IX + 3 ubiquinol
-
under aerobic conditions
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
protoporphyrinogen IX + 3 menadione
protoporphyrin IX + 3 menadiol
-
the enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments
-
-
?
protoporphyrinogen IX + 3 menaquinone
protoporphyrin IX + 3 menaquinol
-
under anaerobic conditions
-
-
?
protoporphyrinogen IX + 3 ubiquinone
protoporphyrin IX + 3 ubiquinol
-
under aerobic conditions
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FMN
-
contains FMN
FMN
-
no direct electron transfer to a terminal oxidoreductase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00376
menadione
-
pH 8.0, 37°C
0.0173
menaquinone
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication
0.007
protoporphyrinogen IX
-
pH 8.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.281
menadione
-
pH 8.0, 37°C
0.292
protoporphyrinogen IX
-
pH 8.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
74.73
menadione
-
pH 8.0, 37°C
41.7
protoporphyrinogen IX
-
pH 8.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0000042
-
membrane associated enzyme with substrates protoporphyrinogen IX and triphenyltetrazolium chloride, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
gene hemG
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
associated
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
additional information
-
detailed model of heme biosynthesis coupled energy generation, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
150000
-
recombinant enzyme, gel filtration
22000
-
4 * 22000, SDS-PAGE
22500
-
4 * 22500, calculated from sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
tetramer
-
4 * 22000, SDS-PAGE; 4 * 22500, calculated from sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
six histidine-tagged recombinant protein
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
gene hemG, expression of His-tagged enzyme in Bacillus megaterium
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
Select items on the left to see more content.
html completed