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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

PCK1  -  phosphoenolpyruvate carboxykinase 1 (soluble)

Bos taurus

 
 
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High impact information on PCK1

  • This protein kinase preparation was able to phosphorylate purified PEPCs from soybean nodules, maize leaves, and a sorghum recombinant C4 PEPC [1].
  • Following in vitro phosphorylation of purified dephospho soybean nodule PEPC from stem-girdled plants by the partially purified nodule PEPC kinase, the former's activity and sensitivity to L-malate inhibition increased and decreased, respectively [1].
  • Phosphoenolpyruvate carboxylase protein kinase from soybean root nodules: partial purification, characterization, and up/down-regulation by photosynthate supply from the shoots [1].
  • In contrast, this PEPC kinase was unable to phosphorylate a phosphorylation-site mutant form of sorghum C4 PEPC (S8Y), two other soybean nodule phosphoproteins [nodulin-26 and nodulin-100 (sucrose synthase)], bovine serum albumin, and histone III-S [1].
 

Analytical, diagnostic and therapeutic context of PCK1

References

  1. Phosphoenolpyruvate carboxylase protein kinase from soybean root nodules: partial purification, characterization, and up/down-regulation by photosynthate supply from the shoots. Zhang, X.Q., Chollet, R. Arch. Biochem. Biophys. (1997) [Pubmed]
  2. Cloning and characterization of bovine cytosolic and mitochondrial PEPCK during transition to lactation. Agca, C., Greenfield, R.B., Hartwell, J.R., Donkin, S.S. Physiol. Genomics (2002) [Pubmed]
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