Other names published for PCK1: JPM2, PPC1, phosphoenolpyruvate carboxykinase PCK1, YKR097W
PCK1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
PCK1 - Protein Sequence Features (13)
| Reference | Other Genes Addressed |
|---|---|
| Andrade C, et al. (2010) The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Biol Res 43(2):191-195 | |
| Sepulveda C, et al. (2010) Electrostatic interactions play a significant role in the affinity of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase for Mn2+. Biochimie 92(7):814-9 | |
| Castillo D, et al. (2009) Functional evaluation of serine 252 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Biochimie 91(2):295-9 | |
| Lin YY, et al. (2009) Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis. Cell 136(6):1073-84 | |
| Tobar I, et al. (2008) Relevance of Arg457 for the nucleotide affinity of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Int J Biochem Cell Biol 40(9):1883-9 | |
| Yevenes A, et al. (2007) Relevance of phenylalanine 216 in the affinity of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase for Mn(II). Protein J 26(2):135-41 | |
| Villarreal JM, et al. (2006) Nucleotide specificity of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase Kinetics, fluorescence spectroscopy, and molecular simulation studies. Int J Biochem Cell Biol 38(4):576-88 | |
| Yevenes A, et al. (2006) Site-directed mutagenesis study of the microenvironment characteristics of Lys213 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Biochimie 88(6):663-72 | |
| Gonzalez-Nilo FD, et al. (2002) Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: theoretical and experimental study of the effect of glutamic acid 284 on the protonation state of lysine 213. Biochim Biophys Acta 1599(1-2):65-71 | |
| Krautwurst H, et al. (2002) Lysine 213 and histidine 233 participate in Mn(II) binding and catalysis in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Biochemistry 41(42):12763-70 | |
| Llanos L, et al. (2001) Mutation Arg336 to Lys in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase originates an enzyme with increased oxaloacetate decarboxylase activity. FEBS Lett 493(1):1-5 | |
| Gonzalez-Nilo FD, et al. (2000) Molecular modeling of the complexes between Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase and the ATP analogs pyridoxal 5'-diphosphoadenosine and pyridoxal 5'-triphosphoadenosine. Specific labeling of lysine 290. J Protein Chem 19(1):67-73 | |
| Chavez R, et al. (1997) Site-directed mutagenesis in basic amino acid residues of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. J Protein Chem 16(3):233-6 | |



