H. Krautwurst

The strongly conserved lysine 256 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase is essential for phosphoryl transfer.

P. Frey, S. Bazaes, A. M. Jabalquinto, 1998, Biochemistry.

Identification of reactive conserved histidines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae.

H. Goldie, L. Montecinos, S. Bazaes, 1997, Biochimica et biophysica acta.

Effects of natural flavones and flavonols on the kinase activity of Cdk5.

R. Maccioni, B. Cassels, G. Zapata-Torres, 2004, Journal of natural products.

Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: theoretical and experimental study of the effect of glutamic acid 284 on the protonation state of lysine 213.

F. González-Nilo, R. Cachau, A. Yévenes, 2002, Biochimica et biophysica acta.

Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: revised amino acid sequence, site-directed mutagenesis, and microenvironment characteristics of cysteines 365 and 458.

P. Frey, R. G. Kemp, S. Latshaw, 1995, Biochemistry.

Lysine 213 and histidine 233 participate in Mn(II) binding and catalysis in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase.

F. González-Nilo, T. Nowak, Hannetz Roschzttardtz, 2002, Biochemistry.