Results 131 to 140 of about 4,023 (167)
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Molecular and Cellular Biochemistry, 2004
All organisms utilize ferrochelatase (EC 4.99.1.1) to catalyze the insertion of ferrous iron into protoposphyrin IX in the terminal step of the heme biosynthetic pathway. Different metal-binding affinity for the enzyme leads to changes in enzyme activity. In this work, we have cloned and over-expressed the enzyme from chironomidae in E. coli.
Yuet Kin, Leung +3 more
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All organisms utilize ferrochelatase (EC 4.99.1.1) to catalyze the insertion of ferrous iron into protoposphyrin IX in the terminal step of the heme biosynthetic pathway. Different metal-binding affinity for the enzyme leads to changes in enzyme activity. In this work, we have cloned and over-expressed the enzyme from chironomidae in E. coli.
Yuet Kin, Leung +3 more
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The International Journal of Biochemistry & Cell Biology, 1999
Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX. It is encoded by a single gene, and mutations in the human gene are associated with the inherited disorder, erythropoietic protoporphyria.
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Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX. It is encoded by a single gene, and mutations in the human gene are associated with the inherited disorder, erythropoietic protoporphyria.
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Measurement of Ferrochelatase Activity
Current Protocols in Toxicology, 1999AbstractFerrochelatase is the terminal enzyme in the heme biosynthesis pathway. Under anaerobic conditions it catalyzes the insertion of ferrous iron into the protoporphyrin IX ring to form protoheme. In the absence of iron and under aerobic conditions, the enzyme will use zinc or mercury as a substitute.
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Effects of lipids on the activity of ferrochelatase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1977Removal of lipids from submitochondrial particles or detergent-solubilized mitochondrial preparations of rat liver resulted in a 90% loss of ferrochelatase (protochemeferro-lyase, EC 4.99.1.1) activity. The addition of either a fatty acid or phospholipid restored enzyme activity; the extent of reactivation being correlated with the degree of ...
D M, Simpson, R, Poulson
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Ferrochelatase and N-alkylated porphyrins
Molecular and Cellular Biochemistry, 1984The final step in heme synthesis is catalyzed by the mitochondrial enzyme, ferrochelatase. Characterization of this enzyme has been complicated by a number of factors including the dependence of enzyme activity on lipids. Purification of ferrochelatase from rat and bovine sources has been achieved only relatively recently using blue Sepharose CL-6B ...
S P, Cole, G S, Marks
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Metal Inhibition of Ferrochelatase
Annals of the New York Academy of Sciences, 1987Ferrochelatase activity was examined both in growing MEL cells and in in vitro assays of the purified enzyme to determine what effect a variety of divalent cations would have. Data obtained with the purified enzyme demonstrated that Mn2+ strongly inhibits the activity in a competitive fashion with respect to Fe2+ with a calculated Ki of 15 microM ...
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Proteobacteria-like ferrochelatase in the malaria parasite
Current Genetics, 2003A gene encoding the heme biosynthetic enzyme ferrochelatase (FC) was found in the genomic DNA databases of Plasmodium spp. The predicted amino acid sequence of malarial FC is highly conserved and fairly well conserved by comparison with other orthologues. The FC genes of P. falciparum and P.
Shigeharu, Sato, R J M, Wilson
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Orientation of ferrochelatase in bovine liver mitochondria
Biochemistry, 1985The orientation of ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1), the terminal enzyme of the heme biosynthetic pathway, was examined in bovine liver mitochondria. The ability of a membrane-impermeable sulfhydryl reagent, 4,4'-dimaleimidylstilbene-2,2'-disulfonic acid, to inactivate ferrochelatase in intact or disrupted mitochondria and mitoplasts
B M, Harbin, H A, Dailey
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Protoporphyrinogen oxidase and ferrochelatase in porphyria variegata
European Journal of Clinical Investigation, 1983Abstract. Protoporphyrinogen oxidase activity and ferrochelatase activity were measured in leucocytes from patients with porphyria variegata. The mean activity of protoporphyrinogen oxidase (PPO) in porphyria variegata (PV) was about 50% of normal (P < 0.05). The mean activity of ferrochelatase with 59Fe2+ sulphate and protoporphyrin as substrates (
D J, Viljoen +3 more
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Human ferrochelatase is an iron-sulfur protein
Biochemistry, 1994Recombinant human ferrochelatase has been expressed in Escherichia coli and purified to homogeneity. Metal analyses revealed approximately 2 mol of non-heme Fe per mol of the purified enzyme (M(r) = 40,000). The UV-visible absorption spectrum of the purified enzyme consists of a protein absorption at 278 nm (epsilon approximately 90,000 M-1 cm-1) and ...
H A, Dailey, M G, Finnegan, M K, Johnson
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