The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

PC  -  pyruvate carboxylase

Gallus gallus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of PCX


High impact information on PCX

  • It does not contain biotin and its constituent polypeptides are smaller than those of pyruvate carboxylase [3].
  • These tetramers, like pyruvate carboxylase, are very cold-labile and are protected from dissociation under these conditions by acetyl-CoA, a specific activator of this enzyme [3].
  • Also, the structures form complexes with avidin and antibiotin antibody and thus, like pyruvate carboxylase, contain biotin [3].
  • Initial velocity and isotope exchange studies confirmed that the over-all reaction, like that catalyzed by pyruvate carboxylase purified from rat liver and chicken liver, was a nonclassical Ping Pong Bi Bi Uni Uni sequence with ATP and HCO3-binding randomly in the Bi Bi partial reaction [4].
  • Effects of Mg(2+) on the pre-steady-state kinetics of the biotin carboxylation reaction of pyruvate carboxylase [5].

Biological context of PCX


Anatomical context of PCX


Associations of PCX with chemical compounds


Physical interactions of PCX


Regulatory relationships of PCX


Other interactions of PCX


Analytical, diagnostic and therapeutic context of PCX


  1. The biochemistry of fatty liver and kidney syndrome. Biotin-mediated restoration of hepatic gluconeogenesis in vitro and its relationship to pyruvate carboxylase activity. Bannister, D.W. Biochem. J. (1976) [Pubmed]
  2. Pyruvate carboxylase from Bacillus stearothermophilus: molecular size, biotin content and subunit constitution. Libor, S., Warwick, R., Sundaram, T.K. Biochem. Soc. Trans. (1975) [Pubmed]
  3. A re-examination of the electron microscopic appearance of pyruvate carboxylase from chicken liver. Cohen, N.D., Beegen, H., Utter, M.F., Wrigley, N.G. J. Biol. Chem. (1979) [Pubmed]
  4. Sheep kidney pyruvate carboxylase. Studies on the coupling of adenosine triphosphate hydrolysis and CO2 fixation. Ashman, L.K., Keech, D.B. J. Biol. Chem. (1975) [Pubmed]
  5. Effects of Mg(2+) on the pre-steady-state kinetics of the biotin carboxylation reaction of pyruvate carboxylase. Branson, J.P., Attwood, P.V. Biochemistry (2000) [Pubmed]
  6. Molecular cloning and domain structure of chicken pyruvate carboxylase. Jitrapakdee, S., Nezic, M.G., Cassady, A.I., Khew-Goodall, Y., Wallace, J.C. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  7. Kinetics of nucleotide binding to pyruvate carboxylase. Geeves, M.A., Branson, J.P., Attwood, P.V. Biochemistry (1995) [Pubmed]
  8. VO2+(IV) complexes with pyruvate carboxylase: activation of oxaloacetate decarboxylation and EPR properties of enzyme-VO2+ complexes. Werneburg, B.G., Ash, D.E. Biochemistry (1997) [Pubmed]
  9. Pyruvate carboxylase activities in red blood cells and liver of chicks and their dependency on biotin status. First results with activation assays.. Glatzle, D., Frigg, M., Weber, F. Acta Vitaminol. Enzymol. (1979) [Pubmed]
  10. The effect of oxalate on gluconeogenesis by isolated chicken hepatocytes. Increased sensitivity to inhibition as a result of biotin deficiency. Bannister, D.W., O'Neill, I.E. Biochim. Biophys. Acta (1983) [Pubmed]
  11. Binding of acetyl-CoA to chicken liver pyruvate carboxylase. Frey, W.H., Utter, M.F. J. Biol. Chem. (1977) [Pubmed]
  12. Decarboxylation of oxalacetate by pyruvate carboxylase. Attwood, P.V., Cleland, W.W. Biochemistry (1986) [Pubmed]
  13. Pyruvate carboxylase catalysis of phosphate transfer between carbamoyl phosphate and ADP. Attwood, P.V., Graneri, B.D. Biochem. J. (1991) [Pubmed]
  14. Isolation of a carboxyphosphate intermediate and the locus of acetyl-CoA action in the pyruvate carboxylase reaction. Phillips, N.F., Snoswell, M.A., Chapman-Smith, A., Keech, D.B., Wallace, J.C. Biochemistry (1992) [Pubmed]
  15. Avidin is a slow-binding inhibitor of pyruvate carboxylase. Duggleby, R.G., Attwood, P.V., Wallace, J.C., Keech, D.B. Biochemistry (1982) [Pubmed]
  16. Avidin as a probe of the conformational changes induced in pyruvate carboxylase by acetyl-CoA and pyruvate. Attwood, P.V., Mayer, F., Wallace, J.C. FEBS Lett. (1986) [Pubmed]
  17. Aspects of metabolism related to the occurrence of skin lesions in biotin-deficient chicks. Whitehead, C.C., Bannister, D.W. Br. Poult. Sci. (1981) [Pubmed]
  18. Localisation of the active site of pyruvate carboxylase by electron microscopic examination of avidin-enzyme complexes. Johannssen, W., Attwood, P.V., Wallace, J.C., Keech, D.B. Eur. J. Biochem. (1983) [Pubmed]
  19. The determination of the availability to chicks of biotin in feed ingredients by a bioassay based on the response of blood pyruvate carboxylase (EC activity. Whitehead, C.C., Armstrong, J.A., Waddington, D. Br. J. Nutr. (1982) [Pubmed]
WikiGenes - Universities