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Mitochondria enzymes

Plant and animal mitochondria Enzyme from hen egg white Aqueous solution... [Pg.51]

Although bacteria lack any internal membranes, aerobic bacteria nonetheless carry out oxidative phosphorylation by the same processes that occur in eukaryotic mitochondria. Enzymes that catalyze the reactions of both the glycolytic pathway and the citric acid cycle are present in the cytosol of bacteria enzymes that oxidize NADFI to NAD and transfer the electrons to the ultimate acceptor O2 are localized to the bacterial plasma membrane. [Pg.326]

Reflect and Apply You wish to separate and purify enzyme A from contaminating enzymes B and C. Enzyme A is found in the matrix of the mitochondria. Enzyme B is embedded in the mitochondrial membrane, and enzyme C is found in the peroxisome. Enzymes A and B have molecular weights of 60,000 Da. Enzyme C has a molecular weight of 100,000 Da. Enzyme A has a pi of 6.5. Enzymes B and C have pi values of 7.5. Design an experiment to separate enzyme A from the other two enzymes. [Pg.140]

The link with the final electron acceptor, O2, is the enzyme cytochrome c oxidase which spans the inner membrane of the mitochondrion. It consists of cytochromes a and a3 along with two, or possibly three, Cu atoms. The details of its action are not fully established but the overall reaction catalysed by the enzyme is ... [Pg.1101]

Energy-linked transhydrogenase, a protein in the inner mitochondrial membrane, couples the passage of protons down the electrochemical gradient from outside to inside the mitochondrion with the transfer of H from intramitochondrial NADH to NADPH for intramitochondrial enzymes such as glutamate dehydrogenase and hydroxylases involved in steroid synthesis. [Pg.99]

The central role of the mitochondrion is immediately apparent, since it acts as the focus of carbohydrate, hpid, and amino acid metabohsm. It contains the enzymes of the citric acid cycle, P-oxidation of fatty acids, and ketogenesis, as well as the respiratory chain and ATP synthase. [Pg.126]

Pymvate dehydrogenase is a mitochondrial enzyme, and fatty acid synthesis is a cytosohc pathway, but the mitochondrial membrane is impermeable to acetyl-CoA. Acetyl-CoA is made available in the cytosol from citrate synthesized in the mitochondrion, transported into the cytosol and cleaved in a reaction catalyzed by ATP-citrate lyase. [Pg.134]

A summary of the steps in the biosynthesis of the porphyrin derivatives from PBG is given in Figure 32-8. The last three enzymes in the pathway and ALA synthase are located in the mitochondrion, whereas the other enzymes are cytosolic. Both erythroid and non-erythroid ( housekeeping ) forms of the first four enzymes are found. Heme biosynthesis occurs in most mammalian cells with the exception of mature erythrocytes, which do not contain mitochondria. However,... [Pg.271]

ALASl. This repression-derepression mechanism is depicted diagrammatically in Figure 32-9. Thus, the rate of synthesis of ALASl increases greatly in the absence of heme and is diminished in its ptesence. The turnover rate of ALASl in rat liver is normally rapid (half-life about 1 hour), a common feature of an enzyme catalyzing a rate-limiting reaction. Heme also affects translation of the enzyme and its transfer from the cytosol to the mitochondrion. [Pg.272]

With the exception of the acetyl-CoA thiolase, all these enzymes are located exclusively in the peroxisomes, whereas the enzymes that are involved in lipid synthesis are found in the microsomes and the mitochondrion. [Pg.118]

Not all the cellular DNA is in the nucleus some is found in the mitochondria. In addition, mitochondria contain RNA as well as several enzymes used for protein synthesis. Interestingly, mitochond-rial RNA and DNA bear a closer resemblance to the nucleic acid of bacterial cells than they do to animal cells. For example, the rather small DNA molecule of the mitochondrion is circular and does not form nucleosomes. Its information is contained in approximately 16,500 nucleotides that func-tion in the synthesis of two ribosomal and 22 transfer RNAs (tRNAs). In addition, mitochondrial DNA codes for the synthesis of 13 proteins, all components of the respiratory chain and the oxidative phosphorylation system. Still, mitochondrial DNA does not contain sufficient information for the synthesis of all mitochondrial proteins most are coded by nuclear genes. Most mitochondrial proteins are synthesized in the cytosol from nuclear-derived messenger RNAs (mRNAs) and then transported into the mito-chondria, where they contribute to both the structural and the functional elements of this organelle. Because mitochondria are inherited cytoplasmically, an individual does not necessarily receive mitochondrial nucleic acid equally from each parent. In fact, mito-chondria are inherited maternally. [Pg.220]

Poly(3HB) is synthesized in bacteria from acetyl-CoA by a three-step reaction (Fig. 1). The first enzyme of the pathway, 3-ketothiolase, catalyzes the condensation of two molecules of acetyl-CoA to form acetoacetyl-CoA. Aceto-acetyl-CoA reductase subsequently reduces acetoacetyl-CoA to R-3-hydroxy-butyryl-CoA, which is then polymerized by the PHA synthase to produce poly(3HB). Since acetyl-CoA is present in plant cells in the cytosol, plastid, mitochondrion, and peroxisome, the synthesis of poly(3HB) in plants could, in... [Pg.208]

The sequence of the carriers in the chain is shown in Figure 9.6. Each of the components of the chain reduces the next, in sequence, according to the redox potential (Table 9.3). The enzymes and their prosthetic groups are organised into complexes, which can be isolated by gentle disruption of the whole mitochondrion or its inner membrane. Ubiqui-... [Pg.184]

The oxaloacetate is then transported from mitochondrion into the cytosol but not directly, since there is no transporter for oxaloacetate in the mitochondrial membrane. This problem is solved by conversion of oxaloacetate to aspartate, by transamination, and it is the aspartate that is transported across the inner mitochondrial membrane to the cytosol, where oxaloacetate is regenerated from aspartate by a cytosolic aminotransferase enzyme. [Pg.192]

The tricarboxylic acid cycle not only takes up acetyl CoA from fatty acid degradation, but also supplies the material for the biosynthesis of fatty acids and isoprenoids. Acetyl CoA, which is formed in the matrix space of mitochondria by pyruvate dehydrogenase (see p. 134), is not capable of passing through the inner mitochondrial membrane. The acetyl residue is therefore condensed with oxaloacetate by mitochondrial citrate synthase to form citrate. This then leaves the mitochondria by antiport with malate (right see p. 212). In the cytoplasm, it is cleaved again by ATP-dependent citrate lyase [4] into acetyl-CoA and oxaloacetate. The oxaloacetate formed is reduced by a cytoplasmic malate dehydrogenase to malate [2], which then returns to the mitochondrion via the antiport already mentioned. Alternatively, the malate can be oxidized by malic enzyme" [5], with decarboxylation, to pyruvate. The NADPH+H formed in this process is also used for fatty acid biosynthesis. [Pg.138]

This zinc-dependent enzyme [EC 3.4.24.59] of the peptidase M3 family catalyzes the hydrolysis of a peptide bond such that there is a release of an N-terminal octa-peptide at the second stage of processing of some proteins imported into the mitochondrion. The natural substrates are precursor proteins that already have been processed by the mitochondrial processing peptidase. [Pg.480]

The theory has been advanced that there exists in the cell a particulate structure somewhat smaller than the mitochondrion, the lyso-some, that contains certain autolytic enzymes in a latent situation. The lysosome theory55,56 is very largely based upon measurements made in sucrose homogenates of rodent liver. Although the results for a-D-mannosidase in this tissue (see Table IV) are not incompatible with the theory, the results for other tissues do not always conform to it. In particular, the contrast between mouse and rat spleen argues against a universal single particle to which a-D-mannosidase is confined. Apart from the results quoted in Table IV, not much work has been done on the intracellular location of a-D-mannosidase. [Pg.408]

Fig. 7.3.1 The heme synthesis pathway starts in the mitochondrion. The next four steps proceed in the cytosol. Coproporphyrinogen oxidase is in the intermembrane space of the mitochondrion, and the last two enzymes reside at the mitochondral matrix side of the inner membrane. The product heme represses the first and rate-limiting enzyme -aminolevulinic acid (5-ALA) synthase at transcription, during the translation step, and by its transport into the mitochondrion... [Pg.755]

Rotte C, Stejskal F, Zhu G, Keithly JS, Martin W (2001) Pyruvate NADP+ oxidoreductase from the mitochondrion of Euglena gracilis and from the apicomplexan Cryptosporidium parvum a biochemical relic linking pyruvate metabolism in mitochondriate and amitochondriate protists. Mol Biol Evol 18 710-720 Schnarrenberger C, Martin W (2002) Evolution of the enzymes of the citric acid cycle and the glyoxylate cycle of higher plants. A case study of endosymbiotic gene transfer. Eur J Biochem 269 868-883... [Pg.178]

Vitamin B12 consists of a porphyrin-like ring structure, with an atom of Co chelated at its centre, linked to a nucleotide base, ribose and phosphoric acid (6.34). A number of different groups can be attached to the free ligand site on the cobalt. Cyanocobalamin has -CN at this position and is the commercial and therapeutic form of the vitamin, although the principal dietary forms of B12 are 5 -deoxyadenosylcobalamin (with 5 -deoxyadeno-sine at the R position), methylcobalamin (-CH3) and hydroxocobalamin (-OH). Vitamin B12 acts as a co-factor for methionine synthetase and methylmalonyl CoA mutase. The former enzyme catalyses the transfer of the methyl group of 5-methyl-H4 folate to cobalamin and thence to homocysteine, forming methionine. Methylmalonyl CoA mutase catalyses the conversion of methylmalonyl CoA to succinyl CoA in the mitochondrion. [Pg.206]


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See also in sourсe #XX -- [ Pg.321 , Pg.322 ]

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Enzymes in mitochondria

Malic enzyme in animal mitochondria

Mitochondria biosynthetic enzymes

Mitochondria enzyme activity

Mitochondria enzyme distribution

Mitochondria structure, enzymes

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