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CDC19  -  pyruvate kinase CDC19

Saccharomyces cerevisiae S288c

Synonyms: PK 1, PYK1, Pyruvate kinase 1, YAL038W, cell division cycle protein 19
 
 
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Disease relevance of CDC19

 

High impact information on CDC19

 

Biological context of CDC19

 

Anatomical context of CDC19

 

Associations of CDC19 with chemical compounds

 

Physical interactions of CDC19

 

Enzymatic interactions of CDC19

 

Regulatory relationships of CDC19

  • These results indicate that Mck1 negatively regulates pyruvate kinase activity, possibly by direct phosphorylation [13].
  • Mutants carrying fusions to an enhancer-less version of the PGK1 promoter (PGK1(Delta767)) expressed Pyk1 and Pf1k at about 2.5-fold lower levels than normal [20].
 

Other interactions of CDC19

 

Analytical, diagnostic and therapeutic context of CDC19

References

  1. Isolation and properties of the glycolytic enzymes from Zymomonas mobilis. The five enzymes from glyceraldehyde-3-phosphate dehydrogenase through to pyruvate kinase. Pawluk, A., Scopes, R.K., Griffiths-Smith, K. Biochem. J. (1986) [Pubmed]
  2. Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor. Lebioda, L., Stec, B. Nature (1988) [Pubmed]
  3. Application of mathematical tools for metabolic design of microbial ethanol production. Hatzimanikatis, V., Emmerling, M., Sauer, U., Bailey, J.E. Biotechnol. Bioeng. (1998) [Pubmed]
  4. Molecular and immunological characterization of plastid and cytosolic pyruvate kinase isozymes from castor-oil-plant endosperm and leaf. Plaxton, W.C. Eur. J. Biochem. (1989) [Pubmed]
  5. Characterization of the oxaloacetate decarboxylase and pyruvate kinase-like activities of Saccharomyces cerevisiae and Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinases. Jabalquinto, A.M., Laivenieks, M., Zeikus, J.G., Cardemil, E. J. Protein Chem. (1999) [Pubmed]
  6. The cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase. Murcott, T.H., Gutfreund, H., Muirhead, H. EMBO J. (1992) [Pubmed]
  7. The structure of cat muscle pyruvate kinase. Muirhead, H., Clayden, D.A., Barford, D., Lorimer, C.G., Fothergill-Gilmore, L.A., Schiltz, E., Schmitt, W. EMBO J. (1986) [Pubmed]
  8. Expression of an active tobacco mitogen-activated protein kinase kinase kinase enhances freezing tolerance in transgenic maize. Shou, H., Bordallo, P., Fan, J.B., Yeakley, J.M., Bibikova, M., Sheen, J., Wang, K. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  9. Selective inhibition of transition from sexual agglutination to zygote formation by ethyl N-phenylcarbamate in Saccharomyces cerevisiae. Hasegawa, S., Yanagishima, N. Arch. Microbiol. (1984) [Pubmed]
  10. In vivo and in vitro phosphorylation of two isoforms of yeast pyruvate kinase by protein kinase A. Portela, P., Howell, S., Moreno, S., Rossi, S. J. Biol. Chem. (2002) [Pubmed]
  11. ARS binding factor 1 binds adjacent to RAP1 at the UASs of the yeast glycolytic genes PGK and PYK1. Chambers, A., Stanway, C., Tsang, J.S., Henry, Y., Kingsman, A.J., Kingsman, S.M. Nucleic Acids Res. (1990) [Pubmed]
  12. Glycolysis mutants in Saccharomyces cerevisiae. Clifton, D., Weinstock, S.B., Fraenkel, D.G. Genetics (1978) [Pubmed]
  13. Mck1, a member of the glycogen synthase kinase 3 family of protein kinases, is a negative regulator of pyruvate kinase in the yeast Saccharomyces cerevisiae. Brazill, D.T., Thorner, J., Martin, G.S. J. Bacteriol. (1997) [Pubmed]
  14. 5'-secondary structure formation, in contrast to a short string of non-preferred codons, inhibits the translation of the pyruvate kinase mRNA in yeast. Bettany, A.J., Moore, P.A., Cafferkey, R., Bell, L.D., Goodey, A.R., Carter, B.L., Brown, A.J. Yeast (1989) [Pubmed]
  15. The chemical form of selenium affects insulinomimetic properties of the trace element: investigations in type II diabetic dbdb mice. Mueller, A.S., Pallauf, J., Rafael, J. J. Nutr. Biochem. (2003) [Pubmed]
  16. Dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space of rat-heart mitochondria. Gellerich, F.N., Schlame, M., Bohnensack, R., Kunz, W. Biochim. Biophys. Acta (1987) [Pubmed]
  17. Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate. Boles, E., Schulte, F., Miosga, T., Freidel, K., Schlüter, E., Zimmermann, F.K., Hollenberg, C.P., Heinisch, J.J. J. Bacteriol. (1997) [Pubmed]
  18. Proton donor in yeast pyruvate kinase: chemical and kinetic properties of the active site Thr 298 to Cys mutant. Susan-Resiga, D., Nowak, T. Biochemistry (2004) [Pubmed]
  19. Saccharomyces cerevisiae pyruvate kinase Pyk1 is PKA phosphorylation substrate in vitro. Cytryńska, M., Frajnt, M., Jakubowicz, T. FEMS Microbiol. Lett. (2001) [Pubmed]
  20. Pyruvate kinase (Pyk1) levels influence both the rate and direction of carbon flux in yeast under fermentative conditions. Pearce, A.K., Crimmins, K., Groussac, E., Hewlins, M.J., Dickinson, J.R., Francois, J., Booth, I.R., Brown, A.J. Microbiology (Reading, Engl.) (2001) [Pubmed]
  21. Yeast glycolytic mRNAs are differentially regulated. Moore, P.A., Sagliocco, F.A., Wood, R.M., Brown, A.J. Mol. Cell. Biol. (1991) [Pubmed]
  22. Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae: isolation and characterization of the CDC24 gene and adjacent regions of the chromosome. Coleman, K.G., Steensma, H.Y., Kaback, D.B., Pringle, J.R. Mol. Cell. Biol. (1986) [Pubmed]
  23. Characterization of purified poly(adenylic acid)-containing messenger ribonucleic acid from Saccharomyces cerevisiae. Holland, M.J., Hager, G.L., Rutter, W.J. Biochemistry (1977) [Pubmed]
 
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