Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A genetically linked marker locus is sought for the Booroola gene (FecB), a major gene which confers increased prolificacy in sheep. We examined 18 polymorphic proteins in sheep and found 10 to be informative in half-sib families where the Booroola gene was segregating. Recombination was observed between each of the protein loci and the Booroola gene. The loci and exclusion distance for each (calculated as the recombination fraction where the lod score was equal to -2.0) are as follows: NADH diaphorase, DIA1 (9.2 cM); arylesterase, EsA (11.9 cM); haemoglobin beta chain, HBB (17.5 cM); leucine amino peptidase, LAP (19.7 cM); malic enzyme, ME1 (14.8 cM); ovine plasminogen antigen, OPA (12.6 cM); alpha-1-protease inhibitor, PI2 (5.7 cM), erythrocyte 'X' protein, Prot-X (25.3 cM); post transferrin, PTF (2.2 cM); transferrin, TF (33.8 cM).
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PMID:Genetic linkage analysis between protein polymorphisms and the FecB major gene in sheep. 141 47

Multicatalytic proteinase (MCP) is thought to play a central role in the processing and turnover of intracellular proteins in eukaryotic cells. Immunocytochemistry was used to determine the intracellular distribution of the MCP in the claw muscles of the land crab, Gecarcinus lateralis, and the claw and abdominal muscles of the American lobster, Homarus americanus. Cryosections were stained with an affinity-purified polyclonal antibody to lobster MCP that cross-reacted with the land crab enzyme. Two types of staining were observed: a diffuse cytoplasmic staining, and a dense aggregate staining primarily associated with invaginations of the cell membrane. The cytoplasmic staining appeared reticulated in favorable transverse sections due to a preferential localization of MCP to the intermyofibrillar space. The aggregate staining was associated with neither nuclei nor mitochondria, since stains specific for these organelles (Hoechst stain and nicotinamide adenine dinucleotide diaphorase histochemistry, respectively) did not colocalize with the aggregates. Trypsinlike peptidase activities of isolated microsomal and postmicrosomal fractions indicated that less than 1% of the total MCP was associated with the microsomal fraction. Immunoprecipitation of the same fractions confirmed the presence of MCP in the microsomes as well as in the cytosol. These results suggest that the MCP is primarily associated with cytoplasmic components; the aggregate staining may result from the association of the MCP with cellular membrane systems.
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PMID:Immunocytochemical localization of the multicatalytic proteinase (proteasome) in crustacean striated muscles. 151 11

A histological and histochemical study of ingested food material, energy stores and enzymes in the monogenean Pseudodactylogyrus anguillae, parasitizing the gills of the European eel (Anguilla anguilla) is presented. It was found that mucus, epithelial cells and blood from the gills were ingested. Glycogen deposits were small and primarily located in the parenchyma and to a minor extent in the vitellariae. Numerous globules of neutral lipids were found in the vitellariae. A marked esterase activity was found in the gut and a less marked activity in the vitellariae. Acid phosphatase activity was found throughout the body whereas alkaline phosphatase and leucine-amino-peptidase were not detected. Marked activity of succinate dehydrogenase and NADH-diaphorase was found in all cells, indicating a predominantly aerobic metabolism in this monogenean.
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PMID:The nutrition of the gill parasitic monogenean Pseudodactylogyrus anguillae. 342 77

Cytochrome c reductase from potato is a bifunctional protein complex located in the inner mitochondrial membrane, which is involved in respiratory electron transport and processing of mitochondrial precursor proteins. The three largest subunits of the complex share the highest degree of sequence identity with the alpha- and beta-subunits of the soluble processing peptidase (MPP) from fungi and mammals. Evidence is provided that another substoichiometric polypeptide of the cytochrome c reductase complex resembles the alpha-subunit of MPP. A cDNA clone corresponding to the second alpha-MPP protein (alpha-II MPP) encodes a polypeptide of 504 amino acids which is 84% identical to alpha-I MPP. The two different alpha-MPP polypeptides have similar sizes on SDS-polyacrylamide gels but can be distinguished with an antibody raised against a decapeptide that is specific for alpha-II MPP. The presequences of both alpha-subunits of MPP are proteolytically removed by the integrated processing enzyme complex indicating that it acts on the targeting signals of its own precursor proteins. Gene-specific oligonucleotides reveal that the genes encoding alpha-subunit I and alpha-subunit II of MPP are differentially expressed in all tissues analysed but the transcript levels do not vary between tissues.
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PMID:The mitochondrial processing peptidase from potato: a self-processing enzyme encoded by two differentially expressed genes. 781 32

The mitochondrial iron-sulfur protein (also termed Rieske iron-sulfur protein) of cytochrome c reductase was purified from potato tubers and identified with heterologous antibodies. The sequences of the N-terminus of this 25 kDa protein and of an internal peptide were determined to design oligonucleotide mixtures for screening a cDNA library. One class of cDNA clones containing an open reading frame of 265 amino acids was isolated. The encoded protein contains the peptide sequences of the 25 kDa protein and shares about 50% sequence identity with the Rieske iron-sulfur proteins from fungi and around 43% with those from mammals. In vitro transcription and translation of the cDNA reveals that the iron-sulfur protein is made as a larger precursor of 30 kDa which is processed by the cytochrome c reductase/processing peptidase complex from potato. The processing product obtained after in vitro processing has the same size as the mature protein imported into isolated mitochondria. The presequence, which targets the protein to the organelle, is 53 amino acids long and has molecular features different from those found in presequences of fungal iron-sulfur proteins, which are processed in two steps. Our results indicate that, unlike in yeast and Neurospora, the presequence of the iron-sulfur protein from potato is removed by a single processing enzyme in one step.
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PMID:Molecular features, processing and import of the Rieske iron-sulfur protein from potato mitochondria. 801 75

Epimastigotes of Trypanosoma cruzi, the causative agent of Chagas disease, catabolize proteins and amino acids with production of MH3, and glucose with production of reduced catabolites, chiefly succinate and L-alanine, even under aerobic conditions. This "aerobic fermentation of glucose" is probably due to both the presence of low levels of some cytochromes, causing a relative inefficiency of the respiratory chain for NADH, reoxidation during active glucose catabolism, and the lack of NADH dehydrogenase and phosphorylation site I, resulting in the entry of reduction equivalents into the chain mostly as succinate. Phosphoenol pyruvate carboxykinase and pyruvate kinase may play an essential role in diverting glucose carbon to succinate or L-alanine, and L-malate seems to be the major metabolite for the transport of glucose carbon and reduction equivalents between glycosome and mitochondrion. The parasite contains proteinase and peptidase activities. The major lysosomal cysteine proteinase, cruzipain, has been characterized in considerable detail, and might be involved in the host/parasite relationship, in addition to its obvious role in parasite nutrition. Among the enzymes of amino acid catabolism, two glutamate dehydrogenases (one NADP- and the other NAD-linked), alanine aminotransferase, and the major enzymes of aromatic amino acid catabolism (tyrosine aminotransferase and aromatic alpha-hydroxy acid dehydrogenase), have been characterized and proposed to be involved in the reoxidation of glycolytic NADH.
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PMID:Intermediate metabolism in Trypanosoma cruzi. 805 82

In potato, cytochrome c reductase, a protein complex of the respiratory chain, exhibits processing activity toward mitochondrial precursor proteins. One of the two cooperating components of the processing peptidase was shown to be identical with subunit III of the complex. Here we report that two additional proteins of the complex (subunit I and II) share 40-50% sequence identity with the processing enhancing protein, the other component of the processing enzyme from fungi and mammals. Thus the composition and structure of the complex integrated processing peptidase seems to be different from its fungal and mammalian counterparts. Cytochrome c reductase from potato is extraordinarily stable, and separation of subunit III from the complex leads to aggregation of the remaining subcomplex and irreversible loss of processing activity. Expression of the three high molecular weight subunits of the complex allowed purification of each individual protein. Neither the individual subunits nor their combinations are active in in vitro processing assays suggesting that they may need the structural support of the complex for activity. In contrast to mitochondrial processing peptidases from other organisms, the purified potato enzyme is active in the presence of high salt (above 1 M NaCl) and works efficiently without addition of metal ions. These data indicate that potato cytochrome c reductase is a bifunctional protein complex with unique features. Possibly, there is a more general evolutionary relationship between cytochrome c reductases and mitochondrial processing peptidases than hitherto assumed.
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PMID:Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria. 836 Jan 83