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Literature summary extracted from

  • Davidson, R.E.; Chesters, C.J.; Reid, J.D.
    Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase (2009), J. Biol. Chem., 284, 33795-33799.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.98.1.1 expression in Escherichia coli JM109 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.98.1.1 deuteroporphyrin IX
-
Homo sapiens
4.98.1.1 additional information no inhibition by deuteroporphyrin Homo sapiens
4.98.1.1 porphyrin high porphyrin concentrations noticeably increase the extent of zinc inhibition Homo sapiens
4.98.1.1 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 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.98.1.1 0.00017
-
Zn2+ for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens
4.98.1.1 0.0015
-
Zn2+ 0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens
4.98.1.1 0.0026
-
deuteroporphyrin IX for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens
4.98.1.1 0.0461
-
deuteroporphyrin IX 0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.98.1.1 Zn2+ zinc is an effective inhibitor of the reaction as well as being a substrate Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.98.1.1 protoporphyrin IX + Fe2+ Homo sapiens
-
protoheme IX + 2 H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.98.1.1 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.98.1.1 chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.98.1.1 deuteroporphyrin IX + Zn2+ in vitro, zinc is the preferred substrate at all concentrations of porphyrin Homo sapiens Zn deuteroporphyrin IX + H+
-
?
4.98.1.1 protoporphyrin IX + Fe2+
-
Homo sapiens protoheme IX + 2 H+
-
?

Synonyms

EC Number Synonyms Comment Organism
4.98.1.1 FeCH
-
Homo sapiens
4.98.1.1 ferrochelatase
-
Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.98.1.1 3.2
-
Zn2+ no added cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens
4.98.1.1 3.5
-
Zn2+ 0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.98.1.1 0.0712
-
deuteroporphyrin IX for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens
4.98.1.1 0.3376
-
deuteroporphyrin IX 0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.98.1.1 76
-
deuteroporphyrin IX 0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens
4.98.1.1 1200
-
deuteroporphyrin IX for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens
4.98.1.1 2200
-
Zn2+ 0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens
4.98.1.1 19000
-
Zn2+ for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin Homo sapiens