Literature summary for 4.98.1.1 extracted from

Hoggins, M.; Dailey, H.A.; Hunter, C.N.; Reid, J.D.
Direct measurement of metal ion chelation in the active site of human ferrochelatase (2007), Biochemistry, 46, 8121-8127.

Search for more literature for 4.98.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant human ferrochelatase (R115L) expressed in Escherichia coli JM109 cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
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	Homo sapiens
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	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P22830	-	-

Purification (Commentary)

Purification (Comment)	Organism
by gel filtration	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
deuteroporphyrin + Fe2+	-	Homo sapiens	deuteroheme + 2 H+	-	?

Synonyms

Synonyms	Comment	Organism
protoporphyrin IX ferrochelatase	-	Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.1	-	Fe2+	-	Homo sapiens

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Release 2023.1 (January 2023)