Results 201 to 210 of about 42,175 (244)
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The biochemistry of heme biosynthesis
Archives of Biochemistry and Biophysics, 2008Heme is an integral part of proteins involved in multiple electron transport chains for energy recovery found in almost all forms of life. Moreover, heme is a cofactor of enzymes including catalases, peroxidases, cytochromes of the P(450) class and part of sensor molecules.
Ilka U, Heinemann +2 more
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The Biosynthesis of Heme O and Heme A Is Not Regulated by Copper
Biochemistry, 2005Heme A is an obligatory cofactor in all eukaryotic and many prokaryotic cytochrome c oxidase (CcO) enzymes. Despite its obvious importance to CcO and the electron transport pathway, essentially nothing is known concerning the regulation of heme A. Because CcO is the only natural target for heme A and copper is also required for CcO activity, it was ...
M Scott, Morrison +2 more
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EcoSal Plus, 2007
This review is concerned specifically with the structures and biosynthesis of hemes in E. coli and serovar Typhimurium. However, inasmuch as all tetrapyrroles share a common biosynthetic pathway, much of the material covered here is applicable to tetrapyrrole biosynthesis in other organisms.
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This review is concerned specifically with the structures and biosynthesis of hemes in E. coli and serovar Typhimurium. However, inasmuch as all tetrapyrroles share a common biosynthetic pathway, much of the material covered here is applicable to tetrapyrrole biosynthesis in other organisms.
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Bilirubin Inhibition of Heme Biosynthesis
Science, 1959The conversion of protoporphyrin and iron to heme is catalyzed by a soluble enzyme prepared from rat liver. This reaction is inhibited by bilirubin, and initial kinetic studies suggest that the inhibition is due in part to a competition between protoporphyrin and the bile pigment. Implications of this finding in hyperbilirubinemia are mentioned.
R F, LABBE, M R, ZASKE, R A, ALDRICH
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Heme biosynthesis and trafficking
Free Radical Biology and Medicine, 2018Heme is an essential cofactor involved in a plethora of vital functions. Heme is required to be in most subcellular compartments, but the way, in which it is transported from the mitochondria - its site of synthesis - to those compartments is poorly understood.
Jonathan Dietz +5 more
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Fumarate Reductase in the Control of Heme Biosynthesis
Science, 1966A drug-induced stimulation of heme biosynthesis in mouse liver was accompanied by altered fumarate metabolism. In liver homogenate, fumarate-1,4-C 14 was incorporated, via succinate and succinyl coenzyme A, into heme at an accelerated rate.
T, Kurumada, R F, Labbe
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Terminal Oxidation in the Regulation of Heme Biosynthesis
Science, 1963Turnover of the tricarboxylic acid cycle and the rate of succinyl-coenzyme A formation may be important factors in the regulation of heme biosynthesis in liver homogenate. Acting as hydrogen acceptor, acetoacetate appears to have a unique role in influencing these metabolic processes.
J, ONISAWA, R F, LABBE
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Disorders of Heme Biosynthesis
2006X-linked sideroblastic anemia is due to a deficiency of the erythroid form of the first enzyme in the heme biosynthetic pathway, 5-aminolevulinic acid synthase. Characteristics of the disease are variable, but typically include adult onset anemia, ineffective erythropoiesis with formation of ring sideroblasts, iron accumulation and pyridoxine ...
Norman G. Egger +2 more
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Schweizerische medizinische Wochenschrift, 1976
300--400 mg of heme is synthesized daily in the organism. Heme is the prosthetic groups of hemoglobulin, cytochromes and other hemoproteins. Major sites of heme synthesis are bone marrow and liver. At least 7 enzymes and intermediary products are involved in the sequence of reactions that lead from glycine and succinyl coenzyme A to heme. delta-Aminole-
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300--400 mg of heme is synthesized daily in the organism. Heme is the prosthetic groups of hemoglobulin, cytochromes and other hemoproteins. Major sites of heme synthesis are bone marrow and liver. At least 7 enzymes and intermediary products are involved in the sequence of reactions that lead from glycine and succinyl coenzyme A to heme. delta-Aminole-
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The biosynthesis of heme and chlorophyll
The Botanical Review, 1966Introduction ...... 56 Formation of Heme and Chlorophyll Precursors 60 1. b-Aminolevulinic Acid 60 2. Succinate-Glycine Cycle 62 3. Porphobilinogen 63 4. Uroporphyrinogen III 64 5. Coproporphyrinogen III 69 6. Protoporphyrin IX 70 Insertion of Iron into Protoporphyrin IX 71 Cytochromes and Heme Enzymes 72 The Relationship Between ...
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