4.98.1.1: protoporphyrin ferrochelatase
This is an abbreviated version!
For detailed information about protoporphyrin ferrochelatase, go to the full flat file.
Word Map on EC 4.98.1.1
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4.98.1.1
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ataxia
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friedreich
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protoporphyria
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erythropoietic
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iron-sulfur
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cardiomyopathy
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fe-s
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ferrous
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ala
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photosensitivity
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aconitase
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porphyria
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expansions
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delta-aminolevulinic
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trinucleotide
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triplet
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5-aminolevulinic
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erythroid
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coproporphyrinogen
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iron-binding
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spinocerebellar
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overload
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photodynamic
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hemin
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iscu
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desulfurase
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ferritin
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protoporphyrinogen
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porphobilinogen
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tetrapyrrole
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uroporphyrinogen
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diagnostics
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biotechnology
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griseofulvin
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sideroblast
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coproporphyria
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iron-mediated
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uroporphyrin
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analysis
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dysarthria
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cluster-containing
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phototoxicity
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microcytic
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porphyrinogenic
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deferiprone
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erythroid-specific
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coinheritance
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erythroleukemia
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ala-pdt
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medicine
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idebenone
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deuteroporphyrin
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mesoporphyrin
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delta-aminolaevulinate
- 4.98.1.1
-
ataxia
-
friedreich
-
protoporphyria
-
erythropoietic
-
iron-sulfur
-
cardiomyopathy
- fe-s
-
ferrous
- ala
-
photosensitivity
- aconitase
-
porphyria
-
expansions
-
delta-aminolevulinic
- trinucleotide
-
triplet
-
5-aminolevulinic
-
erythroid
- coproporphyrinogen
-
iron-binding
-
spinocerebellar
-
overload
-
photodynamic
- hemin
- iscu
-
desulfurase
- ferritin
- protoporphyrinogen
- porphobilinogen
- tetrapyrrole
- uroporphyrinogen
- diagnostics
- biotechnology
-
griseofulvin
-
sideroblast
-
coproporphyria
-
iron-mediated
-
uroporphyrin
- analysis
-
dysarthria
-
cluster-containing
-
phototoxicity
-
microcytic
-
porphyrinogenic
- deferiprone
-
erythroid-specific
-
coinheritance
-
erythroleukemia
-
ala-pdt
- medicine
- idebenone
- deuteroporphyrin
- mesoporphyrin
-
delta-aminolaevulinate
Reaction
Synonyms
chelatase, ferro-, EC 4.99.1.1, FC1, FC2, FeC, FeCH, ferro-protoporphyrin chelatase, ferrochelatase, ferrochelatase 1, ferrochelatase I, ferrochelatase II, frataxin, HEM15, heme synthase, heme synthetase, hemH, HemH1, HemH2, hFC, host red cell ferrochelatase, iron chelatase, parasite genome-coded ferrochelatase, PfFC, PPIX ferrochelatase, protohaem ferrolyase, protoheme ferro-lyase, protoheme ferrolyase, protoheme lyase, protoporhyrin IX ferrochelatase, protoporphyrin (IX) ferrochelatase, protoporphyrin IX ferrochelatase, Shew_1140, Shew_2229, type II ferrochelatase
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Substrates Products
Substrates Products on EC 4.98.1.1 - protoporphyrin ferrochelatase
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REACTION DIAGRAM
deuteroporphyrin + Mn2+
? + H+
in contrast to protoporphyrin IX, deuteroporphyrin lacks the vinyl groups at the 2- and 4-ring positions, and therefore, it is possible to structurally discriminate enzyme-bound (metallated) deuteroporphyrin from any possible heme (protoheme) carryover from the enzyme preparation
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-
?
deuteroporphyrin + Ni2+
? + H+
the Ni-deuteroporphyrin structure is distinctly different from the Mn-deuteroporphyrin model, despite the only variation in enzyme preparation being the addition of either Ni or Mn
-
-
?
deuteroporphyrin IX + Zn2+
Zn deuteroporphyrin IX + H+
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in vitro, zinc is the preferred substrate at all concentrations of porphyrin
-
-
?
mesoporphyrin IX + ferrous ammonium sulfate
mesoheme + ammonium sulfate
room temperature
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-
?
protoporphyrin IX + Cu2+
Cu2+-protoporphyrin + H+
Cu2+ is a good substrate
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-
?
protoporphyrin IX + Zn2+
Zn protoporphyrin IX
pH 7.4, room temperature
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-
?
mesoporphyrin IX + Fe2+
Fe-mesoporphyrin IX + 2 H+
activity measurements were perfomed with a second redox reaction with protoporphyrin IX / protoheme IX as product
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-
?
porphyrin + metal ion
metalloporphyrin
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Co2+, Fe2+, Zn2+, Ni2+ or Mn2+
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?
porphyrin + metal ion
metalloporphyrin
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Co2+, Fe2+, Zn2+, Ni2+ or Mn2+
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-
?
porphyrin + metal ion
metalloporphyrin
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Co2+, Fe2+, Zn2+, Ni2+ or Mn2+
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
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ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 to facilitate mitochondrial ferrous iron transfer for erythroid heme biosynthesis
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-
?
protoporphyrin + Fe2+
protoheme + H+
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the kcat of the forward reaction is about 11fold higher than the reverse reaction
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-
r
protoporphyrin IX + Fe2+
?
insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264
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-
?
protoporphyrin IX + Fe2+
?
insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264
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-
?
protoporphyrin IX + Fe2+
?
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final step of heme biosynthesis
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-
?
protoporphyrin IX + Fe2+
?
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final step of heme biosynthesis
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-
?
protoporphyrin IX + Fe2+
?
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final step of heme biosynthesis
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-
?
protoporphyrin IX + Fe2+
?
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final step of heme biosynthesis
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-
?
protoporphyrin IX + Fe2+
?
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final step of heme biosynthesis
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-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
pH 7.6, 30°C, unaerobic conditions
-
-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
under strictly anaerobic conditions
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-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
the enzymatic product protoheme IX is a well-known cofactor in a wide range of proteins
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-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
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-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
enzyme undergoes significant changes in secondary structure during the catalytic cycle
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-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
substrate is bound deep within an enclosed pocket
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-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
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-
-
?
?
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-
metal substrates are Fe2+, Zn2+, Cu2+, no substrate: Co2+, Fe3+
-
?
additional information
?
-
the enzyme is highly specific for ferrous ion in vivo, however in vitro ferrochelatase catalyzes insertion of a remarkable variety of divalent metal ions into protoporphyrin and other closely related porphyrins
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-
?
additional information
?
-
the enzyme is promiscuous in vitro and can insert Zn2+, Co2+, Cu2+, and Ni2+ into protoporphyrin IX in addition to the physiological substrate Fe2+, however, the insertion of metal ions other than Fe2+ occurs rarely in vivo
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-
?
additional information
?
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-
the enzyme is promiscuous in vitro and can insert Zn2+, Co2+, Cu2+, and Ni2+ into protoporphyrin IX in addition to the physiological substrate Fe2+, however, the insertion of metal ions other than Fe2+ occurs rarely in vivo
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-
?
additional information
?
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2,4-disulfonic deuteroporphyrin, 2,4-bisglycol deuteroporphyrin
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-
?
additional information
?
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2,4-disulfonic deuteroporphyrin, 2,4-bisglycol deuteroporphyrin
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-
?
additional information
?
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-
frataxin binds at nanomolar affinity to the ferrochelatase and the iron-sulfur cluster assembly apparatus, monomeric frataxin interacts with the ferrochelatase dimer predominantly utilizing frataxins helical surface, including iron binding residues in the helix-1/strand-1 conserved acidic residue patch of the protein
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-
?
additional information
?
-
the enzyme is highly specific for ferrous ion in vivo, however in vitro ferrochelatase catalyzes insertion of a remarkable variety of divalent metal ions into protoporphyrin and other closely related porphyrins
-
-
?
additional information
?
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ATP-binding cassette Abcb7 interacts with the enzyme and Abcb10 in G1E-ER4 cells during differentiation. Formation of a functional ABCB7/enzyme complex is required for enzyme stability and completion of heme synthesis
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-
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additional information
?
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in wild type and H207N mutant, addition of porphyrin yields a 1:1 complex with protein, in E287Q mutant addition is in in substoichiometric ratio with protein
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?
additional information
?
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-
overview on active site and substrate binding
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?
additional information
?
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-
the inhibitory metal ion-binding site of ferrochelatase is composed of multiple residues but primarily defined by His-287 and Phe-283 and is crucial for optimal activity at low metal ion concentrations. This binding site may be important for ferrous iron acquisition and desolvation in vivo
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-
?