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Gene Review

PEPC  -  peptidase C

Homo sapiens

 
 
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Disease relevance of PEPC

  • A weak association was observed between PEPC levels in breast cyst fluid and menopausal status (p = 0.093) [1].
  • The differences between POPC and PEPC bilayers may be attributed to the different ranges of angles covered by the torsion angles beta10 and beta12 of the single bonds next to the double bond in the oleoyl (O) and elaidoyl (E) chains [2].
  • In contrast, hypoxia, which does not affect water balance, did not promote any induction of PEPC expression [3].
  • This study suggests that Cd stress is a part of the syndrome of metal toxicity, and that a readjustment of the co-ordination between N and C metabolism via the modulation of GDH, PEPC and ICDH activities avoided the accumulation of toxic levels of ammonium [4].
 

High impact information on PEPC

  • In contrast, chloramphenicol, an inhibitor of protein synthesis in chloroplasts, has no effect on the light activation of maize PEPC-PK [5].
  • The proteins predicted by the nucleotide sequence of both groups of cDNAs are small (8 to 10 kilodaltons), are exceptionally rich in proline, glutamine, and cysteine, and contain repeating elements with a common sequence, PK PEPC [6].
  • Phosphoenolpyruvate carboxylases (PEPC, EC 4.1.1.31) from higher plants are regulated by both allosteric effects and reversible phosphorylation [7].
  • Previous x-ray crystallographic analysis of Zea mays PEPC has revealed a binding site for sulfate ion, speculated to be the site for an allosteric activator, glucose 6-phosphate (Glc-6-P) (Matsumura, H., Xie, Y., Shirakata, S., Inoue, T., Yoshinaga, T., Ueno, Y., Izui, K., and Kai, Y. (2002) Structure (Lond.) 10, 1721-1730) [7].
  • In contrast, there is limited posttranslational control over GART and PEPC and close posttranslational control over uricase activity [8].
 

Biological context of PEPC

  • Human peptidase C, PEPC (E.C.3.4.1.1), exhibits a previously undescribed genetic polymorphism, detectable in red cells or leukocytes by starch gel electrophoresis [9].
  • The activity of these enzymes in the worms cultivated in air + 5% CO(2) was highest during M3, and was also generally higher than that of those cultivated in air only, especially during molting from L3 to L4 (e.g., in recently molted L4, PEPCK activity was 3.7 times greater than that of PEPC 2.9 times greater than when cultivated in air) [10].
  • No significant associations were observed for either PEPC or PGDS concentration in breast cyst fluid and number of cysts, recurrence of the disease, family history of breast cancer, number of children, abortion, and breast feeding [1].
  • The heterotropic effect of Glc-6-P on an allosteric inhibitor, l-malate, was also abolished, but sensitivity to Gly, another allosteric activator of monocot PEPC, was essentially not affected, suggesting the distinctness of their binding sites [7].
  • We also discuss the possibility that the FtPEPC-PK gene has co-evolved with the PEPC gene to participate in C(4) photosynthesis [11].
 

Anatomical context of PEPC

  • RESULTS: Quantitative analysis of the breast cyst fluids indicated that PEPC is present in all cyst fluids at various concentrations ranging from 3 to 31,000 ng/mL [1].
  • Recovery of organic acids from root exudates coincided with the increases in PEPC specific activity [12].
  • 2) Differences between proton conductances in gramicidin A channels in GMO and PEPC cannot be explained by surface charge effects on PEPC membranes [13].
  • The light-dependent phosphorylation of PEPC is triggered by an increase in the cytosolic pH (pHc) of mesophyll cell protoplasts [14].
  • More than 400 antibodies-producing hybridomas to PEPC were produced from the fusion of spleen cells from immunized mice with NS1 myeloma cells [15].
 

Associations of PEPC with chemical compounds

  • The PC component of the rHDL contained sn-1 16:0 and sn-2 18:1 (POPC), 20:4 (PAPC), 20:5 n-3 (PEPC), or 22:6 n-3 (PDPC) or 10% of the respective PC species and 90% sn-1 18:1, sn-2 16:0 PC ether (OPPC ether) [16].
  • Linkage data on human peptidase C (PEPC), human factor H (HF), and coagulation factor XIIIB (F13B) are presented [17].
  • PEPC activity showed evidence of increased sensitivity to inhibition by malate but the protein level was stable [8].
  • The present study demonstrates that Dof1 also enhances transcription from the promoters of both cytosolic orthophosphate dikinase (cyPPDK) genes and a non-photosynthetic PEPC gene, which are not present in animals [18].
  • Molecular dynamics simulations of two monounsaturated phosphatidylcholine (PC) bilayers made of 1-palmitoyl-2-oleoyl-PC (POPC; cis-unsaturated) and 1-palmitoyl-2-elaidoyl-PC (PEPC; trans-unsaturated) were carried out to investigate the effect of a double bond in the PC beta-chain and its conformation on the bilayer core [2].
 

Other interactions of PEPC

  • However, among the offspring of males heterozygous for peptidase C (Pep-C) or superoxide dismutase 1 (SOD-1), male progeny tend to inherit one allele, whereas female progeny tend to inherit the other [19].
  • We then examined if the levels of PEPC or PGDS correlate with the type of cyst or with other clinicopathological variables [1].
  • GUK1 and PEPC, known to be syntenic in man, were found to be asyntenic in MIM and could not be assigned [20].
  • The purified nodule SS-kinase (or CDPK) phosphorylated nodule PEP carboxylase (PEPC; EC 4.1.1.31) in the presence of Ca2+ [21].
  • Phosphoglycerate kinase, RubisCO and PEPC were found to possess high specific activities compared to the activities of these enzymes in strain ATCC 25978T [22].
 

Analytical, diagnostic and therapeutic context of PEPC

References

  1. Quantification of pepsinogen C and prostaglandin D synthase in breast cyst fluid and their potential utility for cyst type classification. Borchert, G.H., Melegos, D.N., Yu, H., Giai, M., Roagna, R., Ponzone, R., Sgro, L., Diamandis, E.P. Clin. Biochem. (1999) [Pubmed]
  2. Effects of phospholipid unsaturation on the bilayer nonpolar region: a molecular simulation study. Róg, T., Murzyn, K., Gurbiel, R., Takaoka, Y., Kusumi, A., Pasenkiewicz-Gierula, M. J. Lipid Res. (2004) [Pubmed]
  3. Abiotic stresses affecting water balance induce phosphoenolpyruvate carboxylase expression in roots of wheat seedlings. González, M.C., Sánchez, R., Cejudo, F.J. Planta (2003) [Pubmed]
  4. Effects of cadmium on the co-ordination of nitrogen and carbon metabolism in bean seedlings. Gouia, H., Suzuki, A., Brulfert, J., Ghorbal, M.H. J. Plant Physiol. (2003) [Pubmed]
  5. Protein turnover as a component in the light/dark regulation of phosphoenolpyruvate carboxylase protein-serine kinase activity in C4 plants. Jiao, J., Echevarría, C., Vidal, J., Chollet, R. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  6. Novel protein in human epidermal keratinocytes: regulation of expression during differentiation. Kartasova, T., van Muijen, G.N., van Pelt-Heerschap, H., van de Putte, P. Mol. Cell. Biol. (1988) [Pubmed]
  7. Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation. Takahashi-Terada, A., Kotera, M., Ohshima, K., Furumoto, T., Matsumura, H., Kai, Y., Izui, K. J. Biol. Chem. (2005) [Pubmed]
  8. Effect of short-term N(2) deficiency on expression of the ureide pathway in cowpea root nodules. Smith, P.M., Winter, H., Storer, P.J., Bussell, J.D., Schuller, K.A., Atkins, C.A. Plant Physiol. (2002) [Pubmed]
  9. Genetic polymorphism of human peptidase C, PEPC (E.C.3.4.1.1): formal genetic and population data. Kömpf, J., Prata, M.J., Amorim, A. Hum. Genet. (1989) [Pubmed]
  10. Anisakis simplex: CO(2)-fixing enzymes and development throughout the in vitro cultivation from third larval stage to adult. Dávila, C., Malagón, D., Valero, A., Benítez, R., Adroher, F.J. Exp. Parasitol. (2006) [Pubmed]
  11. Phosphoenolpyruvate carboxylase kinase involved in C(4) photosynthesis in Flaveria trinervia: cDNA cloning and characterization. Tsuchida, Y., Furumoto, T., Izumida, A., Hata, S., Izui, K. FEBS Lett. (2001) [Pubmed]
  12. Phosphorus deficiency in Lupinus albus. Altered lateral root development and enhanced expression of phosphoenolpyruvate carboxylase. Johnson, J.F., Vance, C.P., Allan, D.L. Plant Physiol. (1996) [Pubmed]
  13. Proton conduction in gramicidin A and in its dioxolane-linked dimer in different lipid bilayers. Cukierman, S., Quigley, E.P., Crumrine, D.S. Biophys. J. (1997) [Pubmed]
  14. Flow cytometric analysis of cytosolic pH of mesophyll cell protoplasts from the crabgrass Digitaria sanguinalis. Giglioli-Guivarc'h, N., Pierre, J.N., Vidal, J., Brown, S. Cytometry. (1996) [Pubmed]
  15. Photoregulation process of sorghum leaf phosphoenolpyruvate carboxylase: study with monoclonal antibodies. Thomas, M., Crétin, C., Keryer, E., Vidal, J., Gadal, P., Bidart, J.M., Buhuon, C. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
  16. Long-chain polyunsaturated fatty acids in the sn-2 position of phosphatidylcholine decrease the stability of recombinant high density lipoprotein apolipoprotein A-I and the activation energy of the lecithin:cholesterol acyltransferase reaction. Parks, J.S., Gebre, A.K. J. Lipid Res. (1997) [Pubmed]
  17. Linkage analyses of human peptidase C (PEPC), human factor H (HF), and coagulation factor XIIIB (F13B). Kömpf, J., Luckenbach, C., Kloor, D., Krczal, D., Amorim, A., Ritter, H. Hum. Genet. (1989) [Pubmed]
  18. Dof1 and Dof2 transcription factors are associated with expression of multiple genes involved in carbon metabolism in maize. Yanagisawa, S. Plant J. (2000) [Pubmed]
  19. Two sex-linked loci in the leopard frog, Rana pipiens. Wright, D.A., Richards, C.M. Genetics (1983) [Pubmed]
  20. Gene mapping of Microcebus murinus (Lemuridae): a comparison with man and Cebus capucinus (Cebidae). Cochet, C., Créau-Goldberg, N., Turleau, C., De Grouchy, J. Cytogenet. Cell Genet. (1982) [Pubmed]
  21. Seryl-phosphorylation of soybean nodule sucrose synthase (nodulin-100) by a Ca2+-dependent protein kinase. Zhang, X.Q., Chollet, R. FEBS Lett. (1997) [Pubmed]
  22. Characteristics of an ammonia-oxidizing bacterium with a plasmid isolated from alkaline soils and its phylogenetic relationship. Takahashi, R., Ohishi, M., Ohshima, M., Saitoh, M., Omata, K., Tokuyama, T. J. Biosci. Bioeng. (2001) [Pubmed]
  23. In vivo regulatory phosphorylation of novel phosphoenolpyruvate carboxylase isoforms in endosperm of developing castor oil seeds. Tripodi, K.E., Turner, W.L., Gennidakis, S., Plaxton, W.C. Plant Physiol. (2005) [Pubmed]
  24. Lessened malate inhibition of guard-cell phosphoenolpyruvate carboxylase velocity during stomatal opening. Zhang, S.Q., Outlaw, W.H., Chollet, R. FEBS Lett. (1994) [Pubmed]
  25. The phosphoenolpyruvate carboxylase gene family of Sorghum: promoter structures, amino acid sequences and expression of genes. Crétin, C., Santi, S., Keryer, E., Lepiniec, L., Tagu, D., Vidal, J., Gadal, P. Gene (1991) [Pubmed]
  26. Manipulating PEPC levels in plants. Jeanneau, M., Vidal, J., Gousset-Dupont, A., Lebouteiller, B., Hodges, M., Gerentes, D., Perez, P. J. Exp. Bot. (2002) [Pubmed]
  27. In vivo phosphorylation of phosphoenolpyruvate carboxylase in guard cells of Vicia faba L. is enhanced by fusicoccin and suppressed by abscisic acid. Du, Z., Aghoram, K., Outlaw, W.H. Arch. Biochem. Biophys. (1997) [Pubmed]
 
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