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.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)


The expected taxonomic range for this enzyme is: Escherichia coli

top print hide
EC NUMBER
COMMENTARY hide
1.3.5.3
-
top print hide
RECOMMENDED NAME
GeneOntology No.
protoporphyrinogen IX dehydrogenase (menaquinone)
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol
show the reaction diagram
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3,8-divinyl-chlorophyllide a biosynthesis II (anaerobic)
-
-
heme b biosynthesis II (anaerobic)
-
-
heme metabolism
-
-
Porphyrin and chlorophyll metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
protoporphyrinogen IX:menadione oxidoreductase
This enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments.
top
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protoporphyrinogen IX + 3 menadione
protoporphyrin IX + 3 menadiol
show the reaction diagram
protoporphyrinogen IX + 3 menaquinone
protoporphyrin IX + 3 menaquinol
show the reaction diagram
protoporphyrinogen IX + 3 triphenyltetrazolium chloride
protoporphyrin IX + ?
show the reaction diagram
-
artificial electron acceptor
-
-
?
protoporphyrinogen IX + 3 ubiquinone
protoporphyrin IX + 3 ubiquinol
show the reaction diagram
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
-
-
-
top print hide
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
protoporphyrinogen IX + 3 menadione
protoporphyrin IX + 3 menadiol
show the reaction diagram
-
the enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments
-
-
?
protoporphyrinogen IX + 3 menaquinone
protoporphyrin IX + 3 menaquinol
show the reaction diagram
-
under anaerobic conditions
-
-
?
protoporphyrinogen IX + 3 ubiquinone
protoporphyrin IX + 3 ubiquinol
show the reaction diagram
-
under aerobic conditions
-
-
?
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
top print hide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.281
menadione
-
pH 8.0, 37°C
0.292
protoporphyrinogen IX
-
pH 8.0, 37°C
top print hide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
74.73
menadione
-
pH 8.0, 37°C
41.7
protoporphyrinogen IX
-
pH 8.0, 37°C
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000042
-
membrane associated enzyme with substrates protoporphyrinogen IX and triphenyltetrazolium chloride, pH and temperature not specified in the publication
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
associated
Manually annotated by BRENDA team
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
-
4 * 22000, SDS-PAGE
22500
-
4 * 22500, calculated from sequence
108000
-
gel filtration
150000
-
recombinant enzyme, gel filtration
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
-
tetramer
-
4 * 22000, SDS-PAGE; 4 * 22500, calculated from sequence
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene hemG, expression of His-tagged enzyme in Bacillus megaterium
-
top print hide
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
top
Show AA Sequence (275 entries)
Please use the Sequence Search for a specific query.
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.3.5.3)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)