Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,4-bisacetal deuteroporphyrin + Fe2+
?
-
-
-
-
?
2,4-disulfonic deuteroporphyrin + Fe2+
?
-
-
-
?
Cd2+-protoporphyrin + H+
protoporphyrin + Cd2+
-
poor substrate
-
-
?
Co2+-protoporphyrin + H+
protoporphyrin + Co2+
-
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
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 + Fe2+
iron-deuteroporphyrin IX + H+
-
-
-
-
?
deuteroporphyrin IX + Zn2+
zinc-deuteroporphyrin IX + H+
-
-
-
?
deuteroporphyrin IX + Zn2+
Zn deuteroporphyrin IX + H+
-
in vitro, zinc is the preferred substrate at all concentrations of porphyrin
-
-
?
deuteroporphyrin IX + Zn2+
Zn-deuteroporphyrin IX + H+
Fe2+-2,4-bis-acetal deuteroporphyrin
?
-
-
-
-
?
Fe2+-2,4-diacetyldeuteroporphyrin
?
-
-
-
-
?
Fe2+-2,4-disulfonate deuteroporphyrin
?
-
-
-
-
?
Fe2+-mesoporphyrin IX + H+
mesoporphyrin IX + Fe2+
-
-
-
-
?
Fe2+-protoporphyrin + H+
protoporphyrin + Fe2+
-
-
-
-
?
hematoporphyrin + Fe2+
?
-
-
-
-
?
heme + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
hemin + H+
mesoporphyrin IX + Zn2+
-
-
-
-
r
hemoglobin + Zn2+
Zn-protoporphyrin + H+
mesoporphyrin + Fe2+
mesoheme
pH 8.0
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
mesoporphyrin + Zn2+
Zn-mesoporphyrin + 2 H+
mesoporphyrin IX + Co2+
cobalt mesoporphyrin IX + 2 H+
mesoporphyrin IX + Fe2+
?
mesoporphyrin IX + Fe2+
Fe-mesoporphyrin IX + 2 H+
mesoporphyrin IX + Fe2+
iron mesoporphyrin IX + 2 H+
-
-
-
?
mesoporphyrin IX + Fe2+
mesoheme + 2 H+
mesoporphyrin IX + ferrous ammonium sulfate
mesoheme + ammonium sulfate
room temperature
-
-
?
mesoporphyrin IX + Zn2+
zinc mesoporphyrin IX + 2 H+
-
-
-
-
?
mesoporphyrin IX + Zn2+
Zn2+-mesoporphyrin + 2 H+
-
-
-
-
r
myoglobin + Zn2+
Zn-protoporphyrin + H+
N-methyl mesoporphyrin + Cu2+
?
pH 7.4
-
-
?
N-methyl mesoporphyrin + Zn2+
?
pH 7.4
-
-
?
porphyrin + Fe2+
heme + H+
-
-
-
?
porphyrin + metal ion
metalloporphyrin
protoheme + H+
protoporphyrin + Fe2+
protoporphyrin + Cu2+
Cu2+-protoporphyrin + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
protoporphyrin + Fe2+
protoheme + H+
protoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
protoporphyrin IX + Co2+
?
-
-
-
?
protoporphyrin IX + Co2+
Co2+-protoporphyrin + H+
-
-
-
?
protoporphyrin IX + Cu2+
?
-
-
-
?
protoporphyrin IX + Cu2+
Cu2+-protoporphyrin + H+
Cu2+ is a good substrate
-
-
?
protoporphyrin IX + Fe2+
?
protoporphyrin IX + Fe2+
Fe-protoporphyrin IX + 2 H+
protoporphyrin IX + Fe2+
Fe2+-protoporphyrin IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
heme + 2 H+
-
-
-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
protoporphyrin IX + FeCl3
protoheme + HCl
pH 7.5, 37°C
-
-
?
protoporphyrin IX + Ni2+
?
-
-
-
-
?
protoporphyrin IX + Zn2+
?
protoporphyrin IX + Zn2+
Zn protoporphyrin IX
pH 7.4, room temperature
-
-
?
protoporphyrin IX + Zn2+
Zn-protoporphyrin + H+
-
-
-
?
protoporphyrin IX + Zn2+
Zn-protoporphyrin IX
protoporphyrin IX + Zn2+
Zn-protoporphyrin IX + H+
-
-
-
-
?
protoporphyrin IX + Zn2+
Zn2+-protoporphyrin IX + H+
-
-
-
-
?
Sn2+-protoporphyrin + H+
protoporphyrin + Sn2+
-
-
-
-
?
Zn2+-mesoporphyrin + H+
mesoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
protoporphyrin + Zn2+
additional information
?
-
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
-
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
-
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + 2 H+
-
-
-
?
deuteroporphyrin IX + Zn2+
Zn-deuteroporphyrin IX + H+
-
-
-
-
?
deuteroporphyrin IX + Zn2+
Zn-deuteroporphyrin IX + H+
-
-
-
-
?
Fe2+-hematoporphyrin
?
-
-
-
-
?
Fe2+-hematoporphyrin
?
-
-
-
-
?
Fe2+-hematoporphyrin
?
-
-
-
-
?
Fe2+-hematoporphyrin
?
-
-
-
-
?
hemoglobin + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
hemoglobin + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
hemoglobin + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
?
mesoporphyrin + Zn2+
Zn-mesoporphyrin + 2 H+
-
-
-
-
?
mesoporphyrin + Zn2+
Zn-mesoporphyrin + 2 H+
37°C
-
-
?
mesoporphyrin IX + Co2+
cobalt mesoporphyrin IX + 2 H+
-
-
-
-
?
mesoporphyrin IX + Co2+
cobalt mesoporphyrin IX + 2 H+
-
-
-
?
mesoporphyrin IX + Fe2+
?
-
-
-
-
?
mesoporphyrin IX + Fe2+
?
-
-
-
-
?
mesoporphyrin IX + Fe2+
?
-
-
-
-
?
mesoporphyrin IX + Fe2+
?
-
-
-
-
?
mesoporphyrin IX + Fe2+
Fe-mesoporphyrin IX + 2 H+
-
-
-
-
?
mesoporphyrin IX + Fe2+
Fe-mesoporphyrin IX + 2 H+
activity measurements were perfomed with a second redox reaction with protoporphyrin IX / protoheme IX as product
-
-
?
mesoporphyrin IX + Fe2+
Fe-mesoporphyrin IX + 2 H+
-
-
-
-
?
mesoporphyrin IX + Fe2+
mesoheme + 2 H+
-
-
-
-
?
mesoporphyrin IX + Fe2+
mesoheme + 2 H+
-
-
-
-
?
mesoporphyrin IX + Fe2+
mesoheme + 2 H+
-
-
-
-
?
myoglobin + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
myoglobin + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
myoglobin + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
porphyrin + metal ion
metalloporphyrin
-
Fe2+, Zn2+, Co2+
-
-
?
porphyrin + metal ion
metalloporphyrin
-
-
-
?
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+
-
?
protoheme + H+
protoporphyrin + Fe2+
-
-
-
-
?
protoheme + H+
protoporphyrin + Fe2+
-
-
-
-
r
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
-
?
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 + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
the kcat of the forward reaction is about 11fold higher than the reverse reaction
-
-
r
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
-
-
-
?
protoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
-
-
-
?
protoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
-
-
-
?
protoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
-
-
-
?
protoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
?
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+
?
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+
?
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+
Fe-protoporphyrin IX + 2 H+
-
-
-
?
protoporphyrin IX + Fe2+
Fe-protoporphyrin IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
pH 7.6, 30°C, unaerobic conditions
-
-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
pH 8.0, 37°C
-
-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
pH 8.1, 30°C
-
-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
under strictly anaerobic conditions
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
?
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 + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
enzyme undergoes significant changes in secondary structure during the catalytic cycle
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
substrate is bound deep within an enclosed pocket
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Zn2+
?
-
-
-
?
protoporphyrin IX + Zn2+
?
-
-
-
?
protoporphyrin IX + Zn2+
Zn-protoporphyrin IX
-
-
-
?
protoporphyrin IX + Zn2+
Zn-protoporphyrin IX
pH 8.0, 35°C
-
-
?
Zn2+-mesoporphyrin + H+
mesoporphyrin + Zn2+
-
-
-
-
?
Zn2+-mesoporphyrin + H+
mesoporphyrin + Zn2+
-
-
-
-
?
Zn2+-protoporphyrin + H+
protoporphyrin + Zn2+
-
-
-
-
?
Zn2+-protoporphyrin + H+
protoporphyrin + Zn2+
-
-
-
-
?
additional information
?
-
-
metal substrates are Fe2+, Zn2+, Cu2+, no substrate: Co2+, Fe3+
-
?
additional information
?
-
ferric iron is not a substrate
-
-
?
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
?
-
-
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
?
-
-
not: isoporphyrin
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
2,4-disulfonic deuteroporphyrin, 2,4-bisglycol deuteroporphyrin
-
-
?
additional information
?
-
-
metal substrates are Fe2+, Zn2+, Co2+
-
?
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
?
-
ferric iron is not a substrate
-
-
?
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
?
-
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
-
-
-
additional information
?
-
-
-
-
-
?
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
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fe2+
-
Zn2+-chelatase activity
metalloporphyrin
-
containing Fe2+, Co2+, Zn2+, Sn2+
-
Mg2+
0.1 mM, reduces the enzymatic activity by more than 60%
N-methyl mesoporphyrin
transition-state inhibitor
N-methyl mesoporphyrin IX
-
specific inhibitor
-
N-methylprotoporphyrin IX
-
Ni2+
-
substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components
p-chloromercuribenzoate
-
-
porphyrin
-
high porphyrin concentrations noticeably increase the extent of zinc inhibition
porphyrin isomer
-
competitive
-
Cd2+
-
-
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+
-
-
Co2+
-
substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components
Cu2+
-
-
Cu2+
-
substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components
heme
-
-
Hg2+
-
-
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
iodoacetamide
-
-
Mn2+
-
-
Mn2+
0.1 mM, reduces the enzymatic activity by more than 60%
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-alkylated porphyrins
-
-
-
N-alkylated porphyrins
-
investigation of structural requirements
-
N-alkylated porphyrins
-
-
-
N-ethylmaleimide
-
-
N-methylmesoporphyrin
-
N-methylmesoporphyrin
-
-
N-methylmesoporphyrin
-
-
N-Methylprotoporphyrin
-
-
N-Methylprotoporphyrin
-
-
N-Methylprotoporphyrin
-
50% inhibition at 4 nM
N-Methylprotoporphyrin
-
-
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
N-Methylprotoporphyrin
-
50% inhibition at 1 nM
Pb2+
-
-
Pb2+
0.1 mM, reduces the enzymatic activity by more than 60%
Porphyrins
-
2,4 position substitution
Porphyrins
-
2,4 position substitution
sulfhydryl reagents
-
-
Zn2+
0.1 mM, inhibits over 90% of the enzyme activity
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
Zn2+
-
iron-chelatase activity
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
no inhibition by deuteroporphyrin
-
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
-
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
-
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
-
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.
0.056
2,4-bisacetal deuteroporphyrin
-
-
0.479
2,4-diacetyldeuteroporphyrin
-
-
0.052
2,4-disulfonic deuteroporphyrin
-
-
0.0213
deuteroporphyrin
-
-
0.0026 - 0.054
deuteroporphyrin IX
0.055
hematoporphyrin
-
-
0.0057
hemin
-
pH 5.5, 45°C
0.004 - 0.1
mesoporphyrin
0.0047 - 0.0302
mesoporphyrin IX
0.012
myoglobin
-
at pH 6.5 and 30°C
-
0.0121 - 0.0246
porphyrin
0.002 - 0.05
protoporphyrin
0.00022 - 0.72
protoporphyrin IX
0.0052
Co2+
wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.0052
Co2+
pH 7.4, 21°C, wild-type enzyme
0.56
Co2+
mutant enzyme Y13M, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.56
Co2+
pH 7.4, 21°C, mutant enzyme Y13M
0.063
Cu2+
wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.063
Cu2+
pH 7.4, 21°C, wild-type enzyme
0.0026
deuteroporphyrin IX
-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.0144
deuteroporphyrin IX
-
pH 7.7, 28°C
0.0461
deuteroporphyrin IX
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.05
deuteroporphyrin IX
mutant E272S, in the presence of 4 mM Mg2+, pH 7.4, room temperature
0.054
deuteroporphyrin IX
mutant E272S, pH 7.4, room temperature
0.00048
Fe2+
mutant Q248P/S249G/K250P/G252W, pH 8.1, 30°C
0.00108
Fe2+
mutant K250M/V251L/W256Y, pH 8.1, 30°C
0.00113
Fe2+
mutant V251L, pH 8.1, 30°C
0.00146
Fe2+
mutant P255R, pH 8.1, 30°C
0.0019
Fe2+
wild-type, pH 8.1, 30°C
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
0.0028
Fe2+
-
mutant C341S
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
0.0038
Fe2+
-
in complex with protoporphyrinogen dehydrogenase PgdH1, pH 8.0, 30°C
0.0039
Fe2+
-
free enzyme, pH 8.0, 30°C
0.0047
Fe2+
-
pH 7.7, 28°C
0.00515
Fe2+
mutant S249A/K250Q/V251C, pH 8.1, 30°C
0.006
Fe2+
-
cosubstrate protoporphyrin
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
0.0083
Fe2+
mutant M267I, heterodimer, room temperature
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
0.0094
Fe2+
M11V/G104A, pH 7.6, 30°C, unaerobic conditions
0.0095
Fe2+
-
presence of CuCl2
0.01
Fe2+
R31G, pH 7.6, 30°C, unaerobic conditions
0.0114
Fe2+
wild-type, heterodimer, room temperature
0.0117
Fe2+
mutant M267I, homodimer, room temperature
0.0119
Fe2+
wild-type, homodimer, room temperature
0.013
Fe2+
wild-type, pH 7.6, 30°C, unaerobic conditions
0.0139
Fe2+
-
mutant C219S
0.014
Fe2+
E61K/L185Q/G212D, pH 7.6, 30°C, unaerobic conditions
0.0141
Fe2+
mutant C236Y, homodimer, room temperature
0.017
Fe2+
mutant E61K, pH 7.6, 30°C, unaerobic conditions
0.0179
Fe2+
mutant C236Y, heterodimer, room temperature
0.019
Fe2+
mutant T302A, pH 7.6, 30°C, unaerobic conditions
0.02
Fe2+
-
absence of Cu2+
0.021
Fe2+
mutant D76G/K102T, pH 7.6, 30°C, unaerobic conditions
0.021
Fe2+
-
mutant R115L
0.0219
Fe2+
mutant Q139L, heterodimer, room temperature
0.0232
Fe2+
mutant K379N, heterodimer, room temperature
0.0235
Fe2+
mutant S264L, heterodimer, room temperature
0.0251
Fe2+
mutant Y191H, homodimer, room temperature
0.0262
Fe2+
mutant Q139L, homodimer, room temperature
0.0331
Fe2+
-
cosubstrate protoporphyrin
0.036
Fe2+
-
cosubstrate mesoporphyrin
0.038
Fe2+
mutant Y191H, heterodimer, room temperature
0.0441
Fe2+
mutant F260L, heterodimer, room temperature
0.0488
Fe2+
mutant P334L, homodimer, room temperature
0.0763
Fe2+
mutant F260L, homodimer, room temperature
0.1101
Fe2+
mutant K379N, homodimer, room temperature
0.004
mesoporphyrin
-
non-saturating Fe2+ concentration
0.0077
mesoporphyrin
mutant H388A, 37°C
0.0085
mesoporphyrin
wild-type, 37°C
0.0092
mesoporphyrin
mutant H388A, co-expressed with wild-type, 37°C
0.0093
mesoporphyrin
mutant C395delta, co-expressed with wild-type, 37°C
0.0105
mesoporphyrin
mutant M267I, co-expressed with wild-type, 37°C
0.0111
mesoporphyrin
mutant I186T, co-expressed with wild-type, 37°C
0.012
mesoporphyrin
mutant H263A, 37°C
0.012
mesoporphyrin
mutant H263A, co-expressed with wild-type, 37°C
0.0047
mesoporphyrin IX
-
mutant C341S
0.0061
mesoporphyrin IX
mutant M267I, heterodimer, room temperature
0.0066
mesoporphyrin IX
-
pH 8.0, 37°C
0.008
mesoporphyrin IX
-
-
0.0087
mesoporphyrin IX
-
wild-type
0.0089
mesoporphyrin IX
-
-
0.0092
mesoporphyrin IX
mutant Q139L, heterodimer, room temperature
0.0094
mesoporphyrin IX
wild-type, heterodimer, room temperature
0.0096
mesoporphyrin IX
-
wild-type
0.0097
mesoporphyrin IX
mutant F260L, heterodimer, room temperature
0.0121
mesoporphyrin IX
wild-type, homodimer, room temperature
0.0123
mesoporphyrin IX
mutant M267I, homodimer, room temperature
0.0127
mesoporphyrin IX
-
mutant C219S
0.0129
mesoporphyrin IX
mutant C236Y, heterodimer, room temperature
0.0129
mesoporphyrin IX
mutant Y191H, homodimer, room temperature
0.0138
mesoporphyrin IX
mutant S264L, heterodimer, room temperature
0.0146
mesoporphyrin IX
mutant F260L, homodimer, room temperature
0.0172
mesoporphyrin IX
mutant Y191H, heterodimer, room temperature
0.0182
mesoporphyrin IX
mutant P334L, homodimer, room temperature
0.0224
mesoporphyrin IX
mutant K379N, homodimer, room temperature
0.0253
mesoporphyrin IX
mutant K379N, heterodimer, room temperature
0.0267
mesoporphyrin IX
-
-
0.0267
mesoporphyrin IX
mutant Q139L, homodimer, room temperature
0.0302
mesoporphyrin IX
mutant C236Y, 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
0.0121
porphyrin
wild-type
0.0123
porphyrin
mutant E343D
0.0168
porphyrin
mutant N75A
0.0246
porphyrin
mutant F337A
0.002
protoporphyrin
-
non-saturating Fe2+ concentration
0.00819
protoporphyrin
-
-
0.009
protoporphyrin
-
in complex with protoporphyrinogen dehydrogenase PgdH1, pH 8.0, 30°C
0.00935
protoporphyrin
-
-
0.01
protoporphyrin
-
free enzyme, pH 8.0, 30°C
0.0125
protoporphyrin
-
-
0.0127
protoporphyrin
-
-
0.0153
protoporphyrin
-
-
0.0168
protoporphyrin
-
-
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
0.00083
protoporphyrin IX
R31G, pH 7.6, 30°C, unaerobic conditions
0.00086
protoporphyrin IX
E61K/L185Q/G212D, pH 7.6, 30°C, unaerobic conditions
0.00091
protoporphyrin IX
wild-type, 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
0.0013
protoporphyrin IX
M11V/G104A, pH 7.6, 30°C, unaerobic conditions
0.0014
protoporphyrin IX
wild-type, pH 8.1, 30°C
0.0014
protoporphyrin IX
wild-type, under strictly anaerobic conditions
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
0.00182
protoporphyrin IX
mutant V251L, pH 8.1, 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
0.00251
protoporphyrin IX
mutant P255G, under strictly anaerobic conditions
0.00265
protoporphyrin IX
mutant P255R, pH 8.1, 30°C
0.00265
protoporphyrin IX
mutant P255R, under strictly anaerobic conditions
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, pH 8.1, 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, pH 8.1, 30°C
0.01034
protoporphyrin IX
mutant Q248P/S249G/K250P/G252W, under strictly anaerobic conditions
0.01125
protoporphyrin IX
mutant K250M/V251L/W256Y, pH 8.1, 30°C
0.01125
protoporphyrin IX
mutant K250M/V251L/W256Y, under strictly anaerobic conditions
0.0285
protoporphyrin IX
-
-
0.116
protoporphyrin IX
-
mutant enzyme H287L, at pH 8.0, temperature not specified in the publication
0.72
protoporphyrin IX
-
pH 7.5, 37°C
0.00017
Zn2+
-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.000488
Zn2+
wild type enzyme, at pH 8.0 and 30°C
0.000836
Zn2+
mutant enzyme FeChDELTA347, at pH 8.0 and 30°C
0.0011
Zn2+
-
pH 8.0, 37°C
0.0015
Zn2+
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.0095
Zn2+
mutant H263A, co-expressed with wild-type, 37°C
0.0105
Zn2+
mutant H388A, co-expressed with wild-type, 37°C
0.0108
Zn2+
mutant H388A, 37°C
0.011
Zn2+
mutant I186T, co-expressed with wild-type, 37°C
0.0114
Zn2+
wild-type, 37°C
0.013
Zn2+
pH 7.4, 21°C, wild-type enzyme
0.018
Zn2+
mutant C395delta, co-expressed with wild-type, 37°C
0.024
Zn2+
mutant M267I, co-expressed with wild-type, 37°C
0.024
Zn2+
wild-type, in the presence of 4 mM Mg2+, pH 7.4, room temperature
0.04
Zn2+
mutant H263A, 37°C
0.055
Zn2+
wild-type, pH 7.4, room temperature
0.06
Zn2+
-
at pH 6.5 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.52
hemin
-
pH 5.5, 45°C
6.7
mesoporphyrin IX
-
pH 8.0, 37°C
0.01167 - 0.0573
porphyrin
0.3 - 1.53
protoporphyrin
0.0125 - 1.9
protoporphyrin IX
0.016
Co2+
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
0.033
Co2+
mutant enzyme Y13M, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.033
Co2+
pH 7.4, 21°C, mutant enzyme Y13M
0.065
Cu2+
wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.065
Cu2+
pH 7.4, 21°C, wild-type enzyme
0.018
Fe2+
-
wild-type
0.02
Fe2+
R31G, pH 7.6, 30°C, unaerobic conditions
0.023
Fe2+
wild-type, pH 7.6, 30°C, unaerobic conditions
0.032
Fe2+
mutant T302A, pH 7.6, 30°C, unaerobic conditions
0.033
Fe2+
mutant D76G/K102T, pH 7.6, 30°C, unaerobic conditions
0.038
Fe2+
M11V/G104A, pH 7.6, 30°C, unaerobic conditions
0.04
Fe2+
mutant E61K, pH 7.6, 30°C, unaerobic conditions
0.05
Fe2+
mutant K250M/V251L/W256Y, pH 8.1, 30°C
0.053
Fe2+
-
mutant F110A
0.053
Fe2+
-
mutant R115L
0.055
Fe2+
E61K/L185Q/G212D, pH 7.6, 30°C, unaerobic conditions
0.063
Fe2+
-
mutant C341S
0.068
Fe2+
wild-type, pH 8.1, 30°C
0.13
Fe2+
mutant P255R, pH 8.1, 30°C
0.138
Fe2+
mutant V251L, pH 8.1, 30°C
0.235
Fe2+
mutant Q248P/S249G/K250P/G252W, pH 8.1, 30°C
0.3
Fe2+
mutant S249A/K250Q/V251C, pH 8.1, 30°C
0.01167
porphyrin
mutant E343D
0.0135
porphyrin
mutant F337A
0.016
porphyrin
mutant N75A
0.0573
porphyrin
wild-type
0.3 - 0.483
protoporphyrin
-
-
1.51
protoporphyrin
-
in complex with protoporphyrinogen dehydrogenase PgdH1, pH 8.0, 30°C
1.53
protoporphyrin
-
free enzyme, pH 8.0, 30°C
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
0.013
protoporphyrin IX
-
pH 7.5, 37°C
0.05
protoporphyrin IX
mutant K250M/V251L/W256Y, pH 8.1, 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
0.068
protoporphyrin IX
wild-type, pH 8.1, 30°C
0.068
protoporphyrin IX
wild-type, under strictly anaerobic conditions
0.0683
protoporphyrin IX
-
wild-type
0.073
protoporphyrin IX
mutant enzyme FeChDELTA347, with Zn2+ as cosubstrate, at pH 8.0 and 30°C
0.098
protoporphyrin IX
mutant P255G, under strictly anaerobic conditions
0.0983
protoporphyrin IX
-
mutant P255G
0.13
protoporphyrin IX
mutant P255R, pH 8.1, 30°C
0.13
protoporphyrin IX
mutant P255R, under strictly anaerobic conditions
0.138
protoporphyrin IX
mutant V251L, pH 8.1, 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
0.235
protoporphyrin IX
mutant Q248P/S249G/K250P/G252W, pH 8.1, 30°C
0.3
protoporphyrin IX
mutant S249A/K250Q/V251C, pH 8.1, 30°C
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
0.034
Zn2+
wild type enzyme, at pH 8.0 and 30°C
0.049
Zn2+
mutant enzyme FeChDELTA347, at pH 8.0 and 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
76 - 1200
deuteroporphyrin IX
0.000092
hemin
-
pH 5.5, 45°C
0.00101
mesoporphyrin IX
-
pH 8.0, 37°C
0.018 - 2015
protoporphyrin IX
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
150
protoporphyrin
-
free enzyme, pH 8.0, 30°C
170
protoporphyrin
-
in complex with protoporphyrinogen dehydrogenase PgdH1, pH 8.0, 30°C
0.018
protoporphyrin IX
-
pH 7.5, 37°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
0.00525
Zn2+
-
pH 8.0, 37°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.
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
malfunction
isoenzyme FC1 deficiency in Arabidopsis perturbs embryo development
malfunction
-
the enzyme binds chlorophyll and carotenoids when its enzymatic activity is low. Decreased enzyme activity results in excess production of chlorophyll in the cell
malfunction
-
the plastid ferrochelatase two mutant (fc2) conditionally accumulates large amounts of O2 in its chloroplasts. Under diurnal light cycling conditions, fc2 mutants experience a burst of O2, which results in the degradation of chloroplasts and eventually cell death. Chloroplasts in fc2 mutants have reduced starch content
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
ferrochelatase catalyzes the last step in the heme biosynthetic pathway
metabolism
ferrochelatase is the key enzyme in the heme biosynthesis pathway
metabolism
-
the enzyme catalyzes the insertion ferrous iron into protoporphyrin IX as the last step in heme biosynthesis
metabolism
the enzymatic product protoheme IX is a well-known cofactor in a wide range of proteins
metabolism
ferrochelatase is the final enzyme for heme formation in the tetrapyrrole 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
-
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
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 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
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
-
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
frataxin catalyzes the formation of heme in vitro when it is incubated with iron and protoporphyrin IX. In combination with cysteine desulfurase NFS1 and small mitochondrial protein ISD11 the ferrochelatase activity is increased
physiological function
isoform FC1 downregulation and overproduction causes reduced and elevated ferrochelatase activity in root tissue, respectively, but are not associated with changes in macroscopic phenotype, plant development or leaf pigmentation. A reduction of FC1 in roots and leaves does not significantly disturb heme accumulation. The mitochondrial ferrochelatase activity in a FC1 overexpressor line increases 5fold in comparison with wild-type mitochondria
physiological function
the disruption of the gene encoding isoform HemH1 results in a significant accumulation of extracellular protoporphyrin IX and decreases intracellular heme levels. Under oxidative stress or exposure of the culture to light, protoporphyrin IX accumulation is suppressed in the HemH1 mutant
physiological function
the expression of isoform HemH2 increases when isoform HemH1 is disrupted. The transcription of HemH2 is regulated by the oxidative stress-associated sigma factor RpoE2
physiological function
a functional complex formed of ATP-binding cassette B7, the enzyme and ATP-binding cassette B10 is required for cellular iron homeostasis, mitochondrial function and heme biosynthesis
physiological function
isozyme FC1-produced heme is essential for embryogenesis and salt stress response. Higher FC1 transcript content contributes essentially to stress tolerance
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
-
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 expression of isoform HemH2 increases when isoform HemH1 is disrupted. The transcription of HemH2 is regulated by the oxidative stress-associated sigma factor RpoE2
-
physiological function
-
the disruption of the gene encoding isoform HemH1 results in a significant accumulation of extracellular protoporphyrin IX and decreases intracellular heme levels. Under oxidative stress or exposure of the culture to light, protoporphyrin IX accumulation is suppressed in the HemH1 mutant
-
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.
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.
D76G/K102T
lower KM-value than the wild-type with protoporphyrin IX as substrate, higher KM-value than the wild-type with Fe2+ as substrate
E272S
more unstable than the wild-type, eliminates the stimulating effect of Mg2+
E61K
lower KM-value than the wild-type with protoporphyrin IX as substrate, higher KM-value than the wild-type with Fe2+ as substrate
E61K/L185Q/G212D
lower KM-value than the wild-type with protoporphyrin IX as substrate, higher KM-value than the wild-type with Fe2+ as substrate
M11V/G104A
higher KM-value than the wild-type with protoporphyrin IX as substrate, lower KM-value than the wild-type with Fe2+ as substrate
Q63A
-
reduction in enzymic activity, but not in growth rate
R31G
lower KM-values than the wild-type
S54A
-
reduced growth rate, accumulation of coproporphyrin III in growth medium, but active enzyme
T302A
lower KM-value than the wild-type with protoporphyrin IX as substrate, higher KM-value than the wild-type with Fe2+ as substrate
W230Y
more unstable than the wild-type, has 7% of the wild-type activity, does not display any Zn2+-induced quenching
H183A
-
less than 1% of wild-type activity
-
C341S
-
loss of the [2Fe-2S] cluster
H60D
-
2fold increased activity
H60N
-
more than 4fold increased activity
C406S
complements the ferrochelatase-deficient delta-hemH Escherichia coli, no activity
E343D
the catalytic efficiency of the variant is significantly diminished from the wild type enzyme
E343Q
the mutant has unmeasurable activity in vitro with iron and protoporphyrin as substrates
F110A/E343D
the catalytic efficiency of the variant is significantly diminished from the wild type enzyme
F337A
P212121 space group as the wild-type enzyme, possesses open active site pockets, spatial orientation of all side chains is identical to that of the wild-type
H157A
co-expressed with wild-type, 23-30% of wild-type activity (homogenate), loss of function (purified enzyme)
H263A
co-expressed with wild-type, 23-30% of wild-type activity (homogenate), 37.5-43% of wild-type activity (purified enzyme), exhibits a heterodimeric form when purified
H263C
P212121 space group as the wild-type enzyme, alteration in the orientation of side chains, possesses open active site pockets, has no activity
H341C
P212121 space group as the wild-type enzyme, alteration in the orientation of side chains, possesses open active site pockets, modestly decreased enzymatic activity
H386P
does not complement the ferrochelatase-deficient delta-hemH Escherichia coli, the heterodimeric form (co-expressed with wild-type) cannot be isolated as pure protein, no activity
H388A
co-expressed with wild-type, 23-30% of wild-type activity (homogenate), 37.5-43% of wild-type activity (purified enzyme), exhibits a heterodimeric form when purified
I186T
causes erythropoietic protoporphyria, co-expressed with wild-type, no activity in the homogenate
K304L
the mutant shows 7% activity compared to the wild type enzyme
M267I
causes erythropoietic protoporphyria, co-expressed with wild-type, no activity in the homogenate
M288K
does not complement the ferrochelatase-deficient delta-hemH Escherichia coli, the heterodimeric form (co-expressed with wild-type) cannot be isolated as pure protein, no activity
M76H
the mutant has a higher affinity for heme relative to the wild type enzyme
M76Y
the variant exhibits decreased kcat, as well as KM for mesoporphyrin IX and Km for iron as compared with the wild-type enzyme. The mutant is not able to utilize copper as a substrate in the in vitro
N75A
possesses intact [2Fe-2S] clusters and is as stable to storage as the wild-type
P62R
-
mutated full-length ferrochelatase, identified in a patient with erythropoietic protoporphyria, successfully targets to mitochondria and does not inhibit cleavage of the mature protein from the leader peptide
Q302A
the mutant shows 40% activity compared to the wild type enzyme
Q302D
the mutant's enzyme activity is below detection limit
R115L/E343D
exhibits similar hyperbolic concentration dependencies on porphyrin and ferrous iron concentrations, characteristic two-step mechanism with rapid substrate binding followed by a slower step of metal ion chelation, 7fold decrease in kcat. Mutation primarily affects events occurring after metal ion chelation
S264L
does not complement the ferrochelatase-deficient delta-hemH Escherichia coli
S303A
the mutant shows 47% activity compared to the wild type enzyme
S303P
the mutant's enzyme activity is below detection limit
S303T
the mutant's enzyme activity is below detection limit
E287A
-
low enzymic activity, protein contains protoporphyrin IX, E287 critical for control of release of product
E289A
enhanced protein stability
E289Q
enhanced protein stability
F283L
-
the mutation eliminates inhibition by Ni2+
H207N
-
addition of metalated porphyrins yields a 1:1 complex comparable with wild type
H287C
-
the mutant is substrate-inhibited by Zn2+ and Cu2+ and shows decreased inhibition by Ni2+ compare to the wild type enzyme
H287L
-
the mutant is not substrate-inhibited by Ni2+ but is weakly inhibited by Co2+, Zn2+, and inhibited by Cu2+
H287N
-
the mutant is substrate-inhibited by Ni2+, Fe2+, Zn2+, and Co2+
K250N
-
can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin
P255G
-
drastically reduced inhibition of the variants by N-methylprotoporphyrin, can form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin, but is not paralleled with a decrease in specificity constant and/or catalytic activity
S249A/K250Q/V251C
the ratio of iron/protein is 50% higher than that of the wild-type enzyme, higher KM-values than the wild-type
C213S
-
loss of the [2Fe-2S] cluster, able to support the growth of the Escherichia coli deltahemH strain
C219S
-
loss of the [2Fe-2S] cluster, able to support the growth of the Escherichia coli deltahemH strain
C220S
-
loss of the [2Fe-2S] cluster, able to support the growth of the Escherichia coli deltahemH strain
C230S
-
loss of the [2Fe-2S] cluster, able to support the growth of the Escherichia coli deltahemH strain
delta209230
-
retains enough activity to complement Escherichia coli deltahemH, but is unstable after purification
D207C
-
does not form a [2Fe-2S] cluster
K202T/D207C
-
does not form a [2Fe-2S] cluster
K202T/deltaV204/D207C
-
does not form a [2Fe-2S] cluster
F323L
-
the mutant exhibits an enhanced Ni2+-chelatase activity over that of the parent wild type ferrochelatase
S143T
-
the mutant exhibits an enhanced Ni2+-chelatase activity over that of the parent wild type ferrochelatase
S143T/F323L
-
the mutant exhibits an enhanced Ni2+-chelatase activity over that of the parent wild type ferrochelatase
D141A
-
no enzymic activity, no dehydrogenase activity
D246V/Y248F
-
dimerization-defective, partially blocked in activity
E314A
-
no enzymic activity
G22D
-
wild type enzymic activity, no dehydrogenase activity
G47Delta
-
no enzymic activity
G47S
-
thermosensitive phenotype
H235L
-
no enzymic activity
H237A
-
retains both enzymic and dehydrogenase activity
L62F
-
increase of Vmax and Km
L62Y
-
no enzymic activity
S102F
-
thermosensitive phenotype
FeChDELTA347
removal of the C-terminal CAB-domain led to a greatly increased turnover number, kcat, compared to the full length protein
E264Q
21% of wild-type activity
E264Q
activity 21% of wild-type, Kd for Zn(II) is 0.0037 mM
E264V
less than 1% of wild-type activity
E264V
activity less than 1% of wild-type
H183A
less than 1% of wild-type activity
H183A
almost inactive enzyme, Kd for Zn(II) is 0.015 mM, 4fold decrease in affinity compared to wild-type enzyme
H183C
inactive
H183C
less than 1% of wild-type activity
H183C
Kd for Zn(II) is 0.00064 mM, 6fold increased affinity compared to wild-type
H88A
5% of wild-type activity
H88A
Kd for Zn(II) is 0.0028 mM, activity is 5% of wild-type
K87A
92% of wild-type activity
K87A
retains 92% of wild-type activity, Kd for Zn(II) is 0.013 mM
Y13F
71% of wild-type activity
Y13F
activity is equal to that of the wild-type enzyme
Y13F
Kd for Zn(II) is 0.0048 mM, Zn(II) bound in a wild-type fashion in the structure
Y13M
the mutant enzyme inserts Co2+ at a higher rate than the wild type ferrochelatase, but it has lost the ability to use Cu2+ as a substrate
Y13M
the modified enzyme inserts Co2+ at a higher rate than the wild-type enzyme but loses the ability to use Cu2+ as a substrate. the mutant enzyme shows the same metal specificity as that of the ferrochelatases from Saccharomyces cerevisiae and human
E264Q
-
21% of wild-type activity
-
E264Q
-
activity 21% of wild-type, Kd for Zn(II) is 0.0037 mM
-
K87A
-
92% of wild-type activity
-
K87A
-
retains 92% of wild-type activity, Kd for Zn(II) is 0.013 mM
-
C395delta
co-expressed with wild-type, 60% of wild-type activity (homogenate), 37.5-43% of wild-type activity (purified enzyme), exhibits a heterodimeric form when purified
C395delta
-
deletion of the C-terminus of the enzyme, where the iron-sulfur is located, results in the loss of both ferrochelatase activity and iron-removal activity
E343K
crystals belong to the triclinic space group P1, possess [2Fe-2S] clusters
E343K
-
upper lip of the active site is altered in spatial orientation in the E343K substrate-bound mutant relative to the wild-type enzyme structure
F110A
-
unaltered Km values, but with a diminished Kcat with respect to wild-type enzyme
F110A
variant of human ferrochelatase
F417S
-
less than 2% of normal activity
F417S
complements the ferrochelatase-deficient delta-hemH Escherichia coli, no activity
M76A
inactive
M76A
possesses intact [2Fe-2S] clusters and is as stable to storage as the wild-type
R115L
exhibits wild-type kinetics, but is more stable than the wild-type
R115L
crystal structure is orthorhombic (P212121), possess [2Fe-2S] clusters, presence of an imidazole in the active site
R115L
-
Kcat is slightly lower than that of wild-type, but the Km for porphyrin is slightly higher
R115L
no impact on enzyme activity, exhibits a stoichiometric burst of product formation and substrate consumption, consistent with a rate-determining step following metal ion chelation
E287Q
-
addition of metalated porphyrins is substoichiometric
E287Q
-
low enzymic activity, protein contains protoporphyrin IX, E287 critical for control of release of product
K250M/V251L/W256Y
higher KM value than the wild-type with protoporphyrin IX as substrate, lower KM-value than the wild-type with Fe2+ as the substrate
K250M/V251L/W256Y
-
can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin
P255R
higher KM value than the wild-type with protoporphyrin IX as substrate, lower KM-value than the wild-type with Fe2+ as the substrate
P255R
-
drastically reduced inhibition of the variants by N-methylprotoporphyrin, can form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin, but is not paralleled with a decrease in specificity constant and/or catalytic activity
Q248P/S249G/K250P/G252W
higher KM value than the wild-type with protoporphyrin IX as substrate, lower KM-value than the wild-type with Fe2+ as the substrate
Q248P/S249G/K250P/G252W
-
can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin
V251L
higher KM value than the wild-type with protoporphyrin IX as substrate, lower KM-value than the wild-type with Fe2+ as the substrate
V251L
-
can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin
additional information
in gun6-1D, a T-DNA insertion is found 8 kb from plastid ferrochelatase 1 causing an about 3fold increase in both ferrochelatase 1 expression and total plastid ferrochelatase activity
additional information
-
in gun6-1D, a T-DNA insertion is found 8 kb from plastid ferrochelatase 1 causing an about 3fold increase in both ferrochelatase 1 expression and total plastid ferrochelatase activity
additional information
-
fusion protein of Saccharomyces cerevisiae N-terminal leader sequence with Bacillus subtilis enzyme targets fusion product to mitochondria but it remains inactive, identification of a N-terminal segment responsible for association of enzyme with the membrane
additional information
gene deletion/disruption mutant, no enzymic activity, failure of cells to survive inside macrophages and HeLa cells, avirulence for BALB/c mice
additional information
-
gene deletion/disruption mutant, no enzymic activity, failure of cells to survive inside macrophages and HeLa cells, avirulence for BALB/c mice
additional information
natural mutant with premature stop codon leads to accumulation of protoporphyrin IX, light-dependent hemolysis and liver disease
additional information
-
natural mutant with premature stop codon leads to accumulation of protoporphyrin IX, light-dependent hemolysis and liver disease
additional information
-
gene deletion mutant, still has similar virulence as wild type
additional information
siRNA transfection downregulates the endogenous gene expression of ferrochelatase in urothelial cancer cell lines
additional information
-
exchange of about 40 amino acid C-terminus with Sacharomyces cerevisiae enzyme leads to total loss of activity and unstable chimeric proteins
additional information
-
exchange of about 40 amino acid C-terminus with Mus musculus enzyme leads to total loss of activity and unstable chimeric proteins, fusion protein of Saccharomyces cerevisiae N-terminal leader sequence with Bacillus subtilis enzyme targets fusion product to mitochondria but it remains inactive, identification of a N-terminal segment responsible for association of enzyme with the membrane
additional information
-
deletion of the CAB domain prevents the DELTAH347 ferrochelatase mutant strain from growing at higher light intensities and affects the cellular accumulation of tetrapyrroles. The mutant is active as a monomer
additional information
-
deltaH324 mutant, mutated hemH gene, contains a truncated FeCH enzyme lacking the C-terminal domain, is localized to the membrane fraction, C-terminal domain is not necessary for membrane association of the enzyme, mutant grows poorly, has dramatically FeCH reduced activity, resulting in highly upregulated 5-aminolevulinic acid synthesis, suffers strongly from photooxidative stress as a consequence of disturbed tetrapyrrole biosynthesis and accumulation of phototoxic intermediates of this pathway. C1.8 mutant strain, carries a short deletion in Chl-binding CP47 protein, grows very slowly, complementation with the mutated hemH gene from mutant deltaH324
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.
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.
co-expression of just one native protein, ferrochelatase, in the presence of 60 microM delta-aminolevulinic acid (10 mg/l) is sufficient for 100% heme incorporation into three unrelated heme proteins derived from different organisms
-
Escherichia coli deltavis cells harbouring plasmids encoding active ferrochelatase mutants, wild-type murine ferrochelatase and mutants overexpressed, under the control of the Escherichia coli alkaline phosphatase promoter phoA, in Escherichia coli BL21(DE3) cells
-
Escherichia coli expressing His-tagged ferrochelatase
-
expressed in a Saccharomyces cerevisiae hem15-deficient strain
expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli HB101 cells
expressed in Escherichia coli Rosetta 2 (DE3) cells
expressed in Oryza sativa cultivar Dongjin
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
expression in Escherichia coli JM109
expression in Escherichia coli, wild-type and mutants E289Q and E289A
ferrochelatase protein is induced in parallel with mitoferrin-1 and Abcb10 during Friend mouse erythroleukemia cell erythroid differentiation
-
into the eukaryotic expression plasmid pEYFP-N1, HeLa cells transiently transfected with YFP-tagged, wild-type FECH
-
into the expression vector pTrcHisA, expressed in Escherichia coli hemH deletion mutant
into the expression vector pTrcHisA, not expressed in Escherichia coli hemH deletion mutant
-
overexpression in Escherichia coli
recombinant full-length and deltaH324 mutant expressed in Escherichia coli using the pET9a-His6 vector
-
recombinant human ferrochelatase (R115L) expressed in Escherichia coli JM109 cells
wild-type and mutants expressed in Escherichia coli BL21(DE3)
-
-
expressed in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli HB101 cells
-
expressed in Escherichia coli HB101 cells
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli JM109
-
expression in Escherichia coli JM109
into the expression vector pTrcHisA, expressed in Escherichia coli hemH deletion mutant
-
into the expression vector pTrcHisA, expressed in Escherichia coli hemH deletion mutant
-
into the expression vector pTrcHisA, expressed in Escherichia coli hemH deletion mutant
-
into the expression vector pTrcHisA, expressed in Escherichia coli hemH deletion mutant
-
into the expression vector pTrcHisA, expressed in Escherichia coli hemH deletion mutant
overexpression in Escherichia coli
-
overexpression in Escherichia coli
-
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.
analysis
-
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
-
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
-
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
-
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
-
enzyme is not essential for bloodstream survival or nasopharyngeal colonization
medicine
-
involvement in erythropoietic protoporphyria, overview
medicine
-
involvement of enzymic defects with erythropoietic protoporphyria, overview
medicine
natural mutant with premature stop codon provides a model for erythropoietic protoporphyria
medicine
-
role in erythropoietic protoporphyria, deficiency of ferrochelatase
medicine
-
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
-
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
-
C-terminal extension is critical for activity of FeCH and it is strictly required for oligomerization of the enzyme
additional information
-
conformational changes in a structurally conserved phi-helix that is predicted to have a central role in product release
additional information
-
convergent evolution in prokaryotes
additional information
-
convergent evolution in prokaryotes
additional information
-
convergent evolution in prokaryotes
additional information
-
convergent evolution in prokaryotes
additional information
-
convergent evolution in prokaryotes
additional information
-
convergent evolution in prokaryotes
additional information
convergent evolution in prokaryotes
additional information
-
convergent evolution in prokaryotes, possesses a cysteine-rich C-terminal extension similar to that of the human enzyme
additional information
-
reverse reaction of ferrochelatase, which may contribute to a new route of the recycling of protoporphyrin and heme in cells
additional information
-
reverse reaction of ferrochelatase, which may contribute to a new route of the recycling of protoporphyrin and heme in cells