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Enzyme Nomenclature
Information on EC 4.99.1.1 - protoporphyrin ferrochelatase
for references in articles please use BRENDA:EC4.99.1.1
Word Map on EC 4.99.1.1
- 4.99.1.1
- protoporphyria
-
erythropoietic
-
photosensitivity
-
ferrous
- erythrocyte
- ala
-
delta-aminolevulinic
-
erythroid
- porphyria
-
5-aminolevulinic
- porphobilinogen
-
dehydratase
-
uroporphyrinogen
- protoporphyrinogen
-
photodynamic
- coproporphyrinogen
- anemia
- erythroleukemia
- tetrapyrrole
-
porphyrinogenic
- mesoporphyrin
- hemin
- deuteroporphyrin
-
uroporphyrin
-
griseofulvin
-
hemoprotein
-
ala-pdt
- coproporphyria
-
3,5-diethoxycarbonyl-1,4-dihydrocollidine
- phototoxicity
-
low-expressed
-
metalloporphyrins
-
microcytic
-
erythroid-specific
-
sideroblast
-
ala-induced
-
coinheritance
-
frataxin
-
delta-aminolaevulinate
-
hypochromic
- medicine
- diagnostics
- biotechnology
-
non-erythroid
- analysis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
4.99.1.1
-
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RECOMMENDED NAME
GeneOntology No.
protoporphyrin ferrochelatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protoheme + 2 H+ = protoporphyrin + Fe2+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
protoheme ferro-lyase (protoporphyrin-forming)
The enzyme catalyses the terminal step in the heme biosynthesis pathways of eukaryotes and Gram-negative bacteria.
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CAS REGISTRY NUMBER
COMMENTARY
9012-93-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
34949, 34961, 34965, 34967, 34968, 34970, 34972, 650802, 651523, 678251, 679185, 681453, 681946, 702862, 703094, 703117, 703119, 704589, 714596, 729221, 730228
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-
-
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
-
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
malfunction
-
mutations in the ferrochelatase gene are not responsible for palmoplantar skin phenotype observed in erythrokeratolysis hiemalis et estivalis of three unrelated Dutch Caucasian patients
malfunction
-
partial defiency of the last enzyme of the heme biosynthetic pathway (namely ferrochelatase) in humans is responsible for erythropoietic protoporphyria
malfunction
homozygous null ferrochelatase 1 mutants exhibit an embryonic-lethal phenotype
malfunction
-
loss of isoform FC2 increases resistance to salt and flagellin treatment. fc2 mutants form abnormally small, pale green rosette leaves; were low in chlorophylls, carotenoids and several photosynthetic proteins; and their photosynthetic performance is impaired. The impairment of isoform FC1 apparently interferes only marginally with stress responses
metabolism
-
ferrochelatase catalyzes the last step in the heme biosynthetic pathway
metabolism
-
the enzymatic product protoheme IX is a well-known cofactor in a wide range of proteins
metabolism
-
ferrochelatase accelerates heme formation via binding the substrates in optimized positions within the active site
metabolism
-
ferrochelatase accelerates heme formation via binding the substrates in optimized positions within the active site
metabolism
-
the enzyme catalyzes the insertion ferrous iron into protoporphyrin IX as the last step in heme biosynthesis
metabolism
ferrochelatase is the key enzyme in the heme biosynthesis pathway
physiological function
-
ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 to facilitate mitochondrial ferrous iron transfer for erythroid heme biosynthesis
physiological function
heme, specifically produced by ferrochelatase 1, may be used as a retrograde signal to coordinate photosynthesis-associated nuclear genes expression with chloroplast development
physiological function
the transgenic plants expressing rice ferrochelatase II without its plastid targeting sequence show higher transgene expression and oxyfluorfen susceptibility than lines expressing the intact ferrochelatase II
physiological function
-
HEM15 encodes a ferrochelatase that catalyses the final step in heme biosynthesis from highly photoreactive porphyrins. The enzyme is essential for viability
physiological function
HEM15 encodes a ferrochelatase that catalyses the final step in heme biosynthesis from highly photoreactive porphyrins. The enzyme is essential for viability
physiological function
-
HEM15 encodes a ferrochelatase that catalyses the final step in heme biosynthesis from highly photoreactive porphyrins. The enzyme is essential for viability
physiological function
-
HEM15 encodes a ferrochelatase that catalyses the final step in heme biosynthesis from highly photoreactive porphyrins. The enzyme is essential for viability
physiological function
-
HEM15 encodes a ferrochelatase that catalyses the final step in heme biosynthesis from highly photoreactive porphyrins. The enzyme is essential for viability
physiological function
-
the apparent surplus of ferrochelatase activity in the wild type is critical for cell viability under high light due to a regulatory role of ferrochelatase in the distribution of chlorophyll into apoproteins
physiological function
-
isoform FC2 is involved in stress responses. Additionally, fc2 plants accumulate protochlorophyllide and display a fluorescent phenotype in the dark
physiological function
a transposon mutant in the hemH gene that encodes the enzyme ferrochelatase shows a characteristic red fluorescence upon UV exposure as a result of porphyrins accumulation. The HemH mutant fails to produce pyoverdine, but the production of the siderophore is restored by introduction of the Pseudomonas aeruginosa hemH gene in trans
physiological function
-
HEM15 encodes a ferrochelatase that catalyses the final step in heme biosynthesis from highly photoreactive porphyrins. The enzyme is essential for viability
-
physiological function
-
HEM15 encodes a ferrochelatase that catalyses the final step in heme biosynthesis from highly photoreactive porphyrins. The enzyme is essential for viability
-
physiological function
-
HEM15 encodes a ferrochelatase that catalyses the final step in heme biosynthesis from highly photoreactive porphyrins. The enzyme is essential for viability
-
physiological function
-
a transposon mutant in the hemH gene that encodes the enzyme ferrochelatase shows a characteristic red fluorescence upon UV exposure as a result of porphyrins accumulation. The HemH mutant fails to produce pyoverdine, but the production of the siderophore is restored by introduction of the Pseudomonas aeruginosa hemH gene in trans
-
physiological function
-
HEM15 encodes a ferrochelatase that catalyses the final step in heme biosynthesis from highly photoreactive porphyrins. The enzyme is essential for viability
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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+
-
in vitro, zinc is the preferred substrate at all concentrations of porphyrin
-
-
?
mesoporphyrin IX + ferrous ammonium sulfate
mesoheme + ammonium sulfate
-
room temperature
-
-
?
protoporphyrin IX + Cu2+
Cu2+-protoporphyrin + H+
-
Cu2+ is a good substrate
-
-
?
protoporphyrin IX + Zn2+
Zn protoporphyrin IX
-
pH 7.4, room temperature
-
-
?
porphyrin + metal ion
metalloporphyrin
-
Co2+, Fe2+, Zn2+, Ni2+ or Mn2+
-
?
porphyrin + metal ion
metalloporphyrin
-
Co2+, Fe2+, Zn2+, Ni2+ or Mn2+
-
?
porphyrin + metal ion
metalloporphyrin
-
Co2+, Fe2+, Zn2+, Ni2+ or Mn2+
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 to facilitate mitochondrial ferrous iron transfer for erythroid heme biosynthesis
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
the kcat of the forward reaction is about 11fold higher than the reverse reaction
-
-
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
-
-
?
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
protoheme + H+
-
pH 7.6, 30°C, unaerobic conditions
-
-
?
protoporphyrin IX + Fe2+
protoheme + H+
-
under strictly anaerobic conditions
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
the enzymatic product protoheme IX is a well-known cofactor in a wide range of proteins
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
enzyme undergoes significant changes in secondary structure during the catalytic cycle
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
substrate is bound deep within an enclosed pocket
-
-
?
additional information
?
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
2,4-disulfonic deuteroporphyrin, 2,4-bisglycol deuteroporphyrin
-
-
-
additional information
?
-
-
2,4-disulfonic deuteroporphyrin, 2,4-bisglycol deuteroporphyrin
-
-
-
additional information
?
-
-
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
-
-
-
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
?
-
-
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
-
?
additional information
?
-
-
overview on active site and substrate binding
-
?
additional information
?
-
-
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
the enzymatic product protoheme IX is a well-known cofactor in a wide range of proteins
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 to facilitate mitochondrial ferrous iron transfer for erythroid heme biosynthesis
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
the kcat of the forward reaction is about 11fold higher than the reverse reaction
-
-
r
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[2Fe-2S]-center
-
ferrochelatase possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis
[2Fe-2S]-center
-
ferrochelatase possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Cu2+
Fe2+
Hg2+
-
human ferrochelatase is capable of catalyzing the insertion of the inhibitory metal ion Hg2+ into a porphyrin macrocycle
Mg2+
Mn2+
Zn2+
[2Fe-2S]cluster
Cd2+
-
human ferrochelatase is capable of catalyzing the insertion of the inhibitory metal ion Cd2+ into a porphyrin macrocycle
Cu2+
-
binding interaction of copper with histidine-60, the highly conserved H60 is a key molecular determinant in directing a catalytically competent mode of metal binding in the active site
Fe2+
-
contains [2Fe-2S] clusters that are coordinated by a group of four cysteine residues contained in an internal amino acid segment of ca. 20 residues in length, role for the [2Fe-2S] cluster in iron affinity
Fe2+
-
single iron in the active site, coordinated in a square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules
Fe2+
-
contains [2Fe-2S] clusters that are coordinated by a group of four cysteine residues contained in an internal amino acid segment of ca. 20 residues in length, role for the [2Fe-2S] cluster in iron affinity
Fe2+
-
metal ion chelation, with a rate constant of 0.96 s-1, is ca. 10times faster than the rate-determining step in the steady state
Fe2+
-
the posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability. Decreased Fe-S cluster availability because of cellular iron depletion or impaired Fe-S cluster assembly causes reduced maturation and stabilization of apoferrochelatase
Fe2+
-
the posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability. Decreased Fe-S cluster availability because of cellular iron depletion or impaired Fe-S cluster assembly causes reduced maturation and stabilization of apoferrochelatase
Fe2+
-
contains [2Fe-2S] cluster that is coordinated by a group of four cysteine residues contained in an internal amino acid segment of ca. 20 residues in length, role for the [2Fe-2S] cluster in iron affinity
Fe2+
-
no [2Fe-2S] cluster, contains three of the four cluster-ligating cysteine residues
Mn2+
-
human ferrochelatase is capable of catalyzing the insertion of the inhibitory metal ion Mn2+ into a porphyrin macrocycle
Zn2+
-
zinc is an effective inhibitor of the reaction as well as being a substrate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ni2+
-
substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components
porphyrin
-
high porphyrin concentrations noticeably increase the extent of zinc inhibition
Cd2+
-
the crystallographic data indicate that the inhibition of ferrochelatase by Cd2+ occurs because the metallated product is poorly released from the enzyme and is not due to a selection mechanism that occurs prior to chelation
Co2+
-
substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components
Cu2+
-
substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components
Hg2+
-
the crystallographic data indicate that the inhibition of ferrochelatase by Hg2+ occurs because the metallated product is poorly released from the enzyme and is not due to a selection mechanism that occurs prior to chelation
Mn2+
-
the crystallographic data indicate that the inhibition of ferrochelatase by Mn2+ because the metallated product is poorly released from the enzyme and is not due to a selection mechanism that occurs prior to chelation
N-Methylprotoporphyrin
-
binds to wild-type ferrochelatase and P255R mutant via a two-step pathway with a kinetically significant intermediate, firstly formation of an initial complex, which subsequently is rearranged into a more stable complex, secondly slow conformational change of the inhibitorprotein complex
Zn2+
-
uncompetitive substrate inhibitor, zinc inhibition is enhanced by increasing porphyrin concentration, zinc inhibits by binding to an enzyme-product complex and is likely to be the second substrate in an ordered mechanism, this inhibition is not observed in the presence of higher concentrations of the detergent cholate, and it is likely that increasing detergent concentrations also increases KM for deuteroporphyrin Ix as substrate and so reduces the concentration of enzymeproduct species for the inhibitor to bind
Zn2+
-
substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components
additional information
-
the inhibitory metals Hg, Cd, and Mn all serve as substrates for the enzyme in that they are inserted into the porphyrin macrocycle. The crystallographic data indicate that the inhibition of ferrochelatase by these metals occurs because the metallated product is poorly released from the enzyme and is not due to a selection mechanism that occurs prior to chelation
-
additional information
-
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
-
additional information
-
no Ni2+ substrate inhibition of ferrochelatase is observed
-
additional information
-
unknown mitochondrial compound with a molecular mass greater than 10 kD, reversible inhibition
-
additional information
the presence of pigments results in lower enzyme activity
-
additional information
-
the presence of pigments results in lower enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
recombinant ferrochelatase exhibits iron removal activity when added together with purified recombinant b5 reductase
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
(25R)-3beta-hydroxycholest-5-en-27-oate
-
mutant E272S, in the presence of 4 mM Mg2+, pH 7.4, room temperature
0.054
(25R)-3beta-hydroxycholest-5-en-27-oate
-
mutant E272S, pH 7.4, room temperature
0.0052
Co2+
-
pH 7.4, 21°C, wild-type enzyme; wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.56
Co2+
-
mutant enzyme Y13M, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication; pH 7.4, 21°C, mutant enzyme Y13M
0.063
Cu2+
-
pH 7.4, 21°C, wild-type enzyme; wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.0026
deuteroporphyrin IX
-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.0461
deuteroporphyrin IX
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.00226
Fe2+
-
wild type enzyme, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00291
Fe2+
-
mutant enzyme S143T, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00728
Fe2+
-
mutant enzyme S143T/F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00895
Fe2+
-
mutant enzyme F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.012
mesoporphyrin
-
mutant H263A, 37°C; mutant H263A, co-expressed with wild-type, 37°C
0.0129
mesoporphyrin IX
-
mutant C236Y, heterodimer, room temperature; mutant Y191H, homodimer, room temperature
0.02206
Ni2+
-
wild type enzyme, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.03218
Ni2+
-
mutant enzyme F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.06521
Ni2+
-
mutant enzyme S143T, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.1037
Ni2+
-
mutant enzyme S143T/F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00022
protoporphyrin IX
wild type enzyme, with Zn2+ as cosubstrate, at pH 8.0 and 30°C
0.00026
protoporphyrin IX
-
wild type enzyme, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00029
protoporphyrin IX
-
mutant enzyme S143T, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.0003
protoporphyrin IX
mutant enzyme FeChDELTA347, with Zn2+ as cosubstrate, at pH 8.0 and 30°C
0.00044
protoporphyrin IX
-
mutant D76G/K102T, pH 7.6, 30°C, unaerobic conditions
0.00078
protoporphyrin IX
-
mutant E61K, pH 7.6, 30°C, unaerobic conditions
0.00079
protoporphyrin IX
-
mutant T302A, pH 7.6, 30°C, unaerobic conditions
0.00086
protoporphyrin IX
-
E61K/L185Q/G212D, pH 7.6, 30°C, unaerobic conditions
0.001
protoporphyrin IX
-
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.00123
protoporphyrin IX
-
mutant enzyme F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00172
protoporphyrin IX
-
wild type enzyme, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00243
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.005
protoporphyrin IX
-
mutant enzyme F283L, at pH 8.0, temperature not specified in the publication
0.00547
protoporphyrin IX
-
mutant enzyme F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00558
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00684
protoporphyrin IX
-
mutant S249A/K250Q/V251C, under strictly anaerobic conditions
0.00831
protoporphyrin IX
-
mutant enzyme S143T, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.01034
protoporphyrin IX
-
mutant Q248P/S249G/K250P/G252W, under strictly anaerobic conditions
0.01125
protoporphyrin IX
-
mutant K250M/V251L/W256Y, under strictly anaerobic conditions
0.116
protoporphyrin IX
-
mutant enzyme H287L, at pH 8.0, temperature not specified in the publication
0.00017
Zn2+
-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.0015
Zn2+
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.024
Zn2+
-
wild-type, in the presence of 4 mM Mg2+, pH 7.4, room temperature
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.065
Cu2+
-
pH 7.4, 21°C, wild-type enzyme; wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.016
Co2+
-
pH 7.4, 21°C, wild-type enzyme; wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.033
Co2+
-
mutant enzyme Y13M, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication; pH 7.4, 21°C, mutant enzyme Y13M
0.0125
protoporphyrin IX
-
wild type enzyme, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.051
protoporphyrin IX
-
mutant K250M/V251L/W256Y, under strictly anaerobic conditions
0.052
protoporphyrin IX
wild type enzyme, with Zn2+ as cosubstrate, at pH 8.0 and 30°C
0.073
protoporphyrin IX
mutant enzyme FeChDELTA347, with Zn2+ as cosubstrate, at pH 8.0 and 30°C
0.142
protoporphyrin IX
-
wild type enzyme, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.212
protoporphyrin IX
-
mutant enzyme F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.234
protoporphyrin IX
-
mutant Q248P/S249G/K250P/G252W, under strictly anaerobic conditions
0.3
protoporphyrin IX
-
mutant S249A/K250Q/V251C, under strictly anaerobic conditions
0.44
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.59
protoporphyrin IX
-
mutant enzyme S143T, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
1.21
protoporphyrin IX
-
mutant enzyme S143T, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
1.6
protoporphyrin IX
-
mutant enzyme F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
1.9
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
3.2
Zn2+
-
no added cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
3.5
Zn2+
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
76
deuteroporphyrin IX
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
1200
deuteroporphyrin IX
-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
62.5
Fe2+
-
wild type enzyme, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
179
Fe2+
-
mutant enzyme F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
261.3
Fe2+
-
mutant enzyme S143T/F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
416.8
Fe2+
-
mutant enzyme S143T, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.56
Ni2+
-
wild type enzyme, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
1.605
Ni2+
-
mutant enzyme F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
4.23
Ni2+
-
mutant enzyme S143T/F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
9.05
Ni2+
-
mutant enzyme S143T, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
47.3
protoporphyrin IX
-
wild type enzyme, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
82.3
protoporphyrin IX
-
wild type enzyme, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
145.7
protoporphyrin IX
-
mutant enzyme S143T, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
173.3
protoporphyrin IX
-
mutant enzyme F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
180
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
292.8
protoporphyrin IX
-
mutant enzyme F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
340.5
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
2015
protoporphyrin IX
-
mutant enzyme S143T, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
2200
Zn2+
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
19000
Zn2+
-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki-values of porphyrin isomers that are not substrates are in the range of 0.013-0.07 mM, Ki-values of metalloporphyrin isomers that are not substrates are in the range of 0.002-0.013 mM, Ki-values for metal inhibitors are in the range of 0.01-0.05 mM
-
0.0712
deuteroporphyrin IX
-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.3376
deuteroporphyrin IX
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.007
Ni2+
-
wild type enzyme, at pH 8.0, temperature not specified in the publication
2.4
Ni2+
-
mutant enzyme F283L, at pH 8.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.959
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
7.5 - 8
7.8
9.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
conversion of mesoporphyrin is dependent on the expression of ferrochelatase, since control Balb/3T3 cells have much lower expression of ferrochelatase than the ferrochelatase transfectants
additional information
-
isoform FC1 shows highest expression in adult leaves, while isoform FC2 exhibits highest expression in juvenile leaves
additional information
-
M-TAT cell, when induced to undergo erythroid differentiation M-TAT cells convert more zinc mesoporphyrin than control cells, accompanied by an increase in hemoglobin-synthesizing cells
additional information
-
MEL cell, clear conversion of zinc mesoporphyrin, marked increase in the conversion in erythroid differentiation-induced MEL cells, in which ferrochelatase is induced
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the recombinant protein expressed in Escherichia coli
additional information