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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Application on EC 4.98.1.1 - protoporphyrin ferrochelatase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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Pro255 has a crucial role in maintaining an appropriate protein conformation and modulating the selectivity and/or regiospecificity of ferrochelatase, ferrochelatase mutants with improved tolerance towards N-methylprotoporphyrin may be potentially used in cell assay systems to study physiological responses to haem deficiency
biotechnology
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co-expression with ferrochelatase along with the addition of a small amount of delta-aminolevulinic acid, is sufficient to produce fully incorporated heme protein. This method is applicable for both Cys-ligated and His-ligated heme proteins
diagnostics
medicine
additional information
diagnostics
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mutations in the ferrochelatase gene are not responsible for palmoplantar skin phenotype observed in erythrokeratolysis hiemalis et estivalis of three unrelated Dutch Caucasian patients
diagnostics
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partial defiency of the last enzyme of the heme biosynthetic pathway (namely ferrochelatase) in humans is responsible for erythropoietic protoporphyria
medicine
enzyme is essential for multiplication and intracellular survival as well as for the establishment of chronic disease
medicine
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enzyme is not essential for bloodstream survival or nasopharyngeal colonization
medicine
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involvement of enzymic defects with erythropoietic protoporphyria, overview
medicine
natural mutant with premature stop codon provides a model for erythropoietic protoporphyria
medicine
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photodynamic therapy (PDT) for tumors is based on the tumor-selective accumulation of a photosensitizer, protoporphyrin IX (PpIX), followed by irradiation with visible light, PpIX accumulation in 5-aminolevulinic acid, treated U937 cells is increased by the inhibition of ferrochelatase
medicine
siRNA-mediated knockdown of ferrochelatase suppresses heme synthesis and significantly increases intracellular protoporphyrin IX (PpIX) accumulation, this improves the phototoxicity of 5-aminolevulinic acid-based photodynamic therapy in urothelial cancer cell lines
medicine
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in bladder cancer cells, the expression of ferrochelatase shows a significant negative correlation with protoporphyrin IX accumulation in vitro. The expression of peptide transporter 1, heme oxygenase-1, and ferrochelatase in resected bladder specimens is correlated with protoporphyrin IX accumulation in bladder cancer cells in voided urine. The expression of ferrochelatase is a significant factor to predict positive 5-aminolevulinic acid-induced fluorescent cytology
additional information
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C-terminal extension is critical for activity of FeCH and it is strictly required for oligomerization of the enzyme
additional information
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conformational changes in a structurally conserved phi-helix that is predicted to have a central role in product release
additional information
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convergent evolution in prokaryotes, possesses a cysteine-rich C-terminal extension similar to that of the human enzyme
additional information
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reverse reaction of ferrochelatase, which may contribute to a new route of the recycling of protoporphyrin and heme in cells
additional information
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reverse reaction of ferrochelatase, which may contribute to a new route of the recycling of protoporphyrin and heme in cells
