Results 71 to 80 of about 5,252 (212)
Ferrochelatase: the convergence of the porphyrin biosynthesis and iron transport pathways
, 2011 Ferrochelatase (also known as PPIX ferrochelatase; Enzyme Commission number 4.9.9.1.1) catalyzes the insertion of ferrous iron into PPIX to form heme. This reaction unites the biochemically synchronized pathways of porphyrin synthesis and iron transport ...
Gloria C. Ferreira +7 more
core +2 more sources
Disease Models & Mechanisms, 2017 Erythropoietic protoporphyria (EPP) is caused by deficiency of ferrochelatase (FECH), which incorporates iron into protoporphyrin IX (PPIX) to form heme.
Jasmin Barman-Aksözen +9 more
doaj +1 more source
British Journal of Haematology, Volume 209, Issue 4, Page 1469-1481, October 2026.Gene therapy is revolutionizing treatment paradigms for haemoglobinopathies, establishing a translational framework for disorders that impact red blood cell development. In their paper, Joshi et al. describe the preclinical and early clinical landscape of gene therapies for non‐haemoglobinopathy erythroid disorders and highlight common thematic ...
Gaurav Joshi +3 more
wiley +1 more source
, 1995 NIGMS NIH HHS (GM47295)All organisms utilize ferrochelatase (protoheme ferrolyase, EC 4.99.1.1) to catalyze the terminal step of the heme biosynthetic pathway, which involves the insertion of ferrous ion into protoporphyrin IX.
Lloyd, Steven G. +6 more
core +1 more source
Journal of Biological Chemistry, 1994 Ferrochelatase (EC 4.99.1.1) catalyzes the terminal step in the heme biosynthetic pathway, the insertion of ferrous iron into protoporphyrin IX. Herein we report the expression, purification, and characterization of the mature processed form of human and mouse ferrochelatase in Escherichia coli JM109.
H A, Dailey, V M, Sellers, T A, Dailey
openaire +2 more sources
Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes
The FEBS Journal, Volume 293, Issue 20, Page 6272-6288, October 2026.During heme biosynthesis in Gram‐positive bacteria, coproheme decarboxylase (ChdC) catalyzes the conversion of four‐propionate substrate coproheme to the two propionate product heme b. Its active site is universally covered by a flexible linking loop. This study identifies an important histidine residue, which stabilizes the loop in a ChdC homolog.
Nikolaus Falb +4 more
wiley +1 more source
Effect of Cellular Location on the Function of Ferrochelatase [PDF]
Journal of Biological Chemistry, 1995 Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, is a nuclear encoded protein that is synthesized in the cytoplasm in a precursor form and then is translocated to the matrix side of the inner mitochondrial membrane. Since the product of the enzymatic reaction, protoheme IX, is utilized almost exclusively in the cytoplasmic ...
A R, Prasad, H A, Dailey
openaire +2 more sources
Molecular insights into frataxin-mediated iron supply for heme biosynthesis in Bacillus subtilis.
PLoS ONE, 2015 Iron is required as an element to sustain life in all eukaryotes and most bacteria. Although several bacterial iron acquisition strategies have been well explored, little is known about the intracellular trafficking pathways of iron and its entry into ...
Andreas Mielcarek +3 more
doaj +1 more source
Porphyrin-substrate Binding to Murine Ferrochelatase: Effect on the Thermal Stability of the Enzyme
, 2005 Ferrochelatase (EC 4.99.1.1), the terminal enzyme of the haem biosynthetic pathway, catalyses the chelation of Fe(II) into the protoporphyrin IX ring.
Ferreira, Gloria C. +5 more
core +1 more source
Purification and characterization of chicken erythrocyte ferrochelatase [PDF]
Biochemical Journal, 1984 Ferrochelatase (EC 4.99.1.1) was purified 2000-fold to apparent homogeneity from isolated chicken erythrocyte mitochondria. The purified enzyme yields a single band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis with an apparent Mr of 42 000.
J W, Hanson, H A, Dailey
openaire +2 more sources