Results 171 to 180 of about 4,768 (212)
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BBA - Proteins and Proteomics, 1989
The ability of purified mouse ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) to bind and catalytically utilize a variety of porphyrins has been examined. In all, the kd, Km or Ki values for eleven different porphyrins, the Ki values for four metalloporphyrins and the kd values for two metalloporphyrins were determined.
Harry A Dailey
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The ability of purified mouse ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) to bind and catalytically utilize a variety of porphyrins has been examined. In all, the kd, Km or Ki values for eleven different porphyrins, the Ki values for four metalloporphyrins and the kd values for two metalloporphyrins were determined.
Harry A Dailey
exaly +3 more sources
Structure and function of ferrochelatase
Journal of Bioenergetics and Biomembranes, 1995Ferrochelatase is the terminal enzyme of the heme biosynthetic pathway in all cells. It catalyzes the insertion of ferrous iron into protoporphyrin IX, yielding heme. In eukaryotic cells, ferrochelatase is a mitochondrial inner membrane-associated protein with the active site facing the matrix. Decreased values of ferrochelatase activity in all tissues
G C, Ferreira +5 more
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Properties of the Cobaltochelatase and the Ferrochelatase
Enzyme, 2017The formation of cobaltomesoporphyrin and ferromesoporphyrin in the presence of appropriate chelatases has been studied. The K(m) value for mesoporphyrin differs for the two activities, although the optimum pH value is 8.1 for both. At high cobalt concentrations a slight non-enzymatic reaction occurs which is not seen with ferrous salts.
E T, Canepa, E B, Llambias
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Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis
Structure, 1997 BACKGROUND: The metallation of closed ring tetrapyrroles resulting in the formation of hemes, chlorophylls and vitamin B12 is catalyzed by specific enzymes called chelatases.
Salam Al-Karadaghi +2 more
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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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Saccharomyces cerevisiae Ferrochelatase Forms a Homodimer
Archives of Biochemistry and Biophysics, 2002Ferrochelatase, the last enzyme of the heme biosynthetic pathway, has for years been considered to be active as a monomer. The crystal structure of Bacillus subtilis ferrochelatase confirmed its monomeric structure. However, animal ferrochelatase was found to form a functional dimer.
Ewa A Grzybowska +2 more
exaly +3 more sources
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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