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

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Gene Review:

pykA - pyruvate kinase

Escherichia coli UTI89

This record was discontinued.

Gibriel, A.Y. et al., Valentini, G. et al.

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Disease relevance of pykA

Aerobic cultures of E. coli K-12 grown on gluconeogenic substrates exhibited pyruvate kinase II activity (non-allosteric), which was stimulated by FDP and by AMP [1].

High impact information on pykA

Pyridoxal 5'-phosphate incorporation into pyruvate kinase II from E. coli was decreased by the substrate phosphoenolpyruvate and increased by the allosteric activator ribose 5-phosphate, the total incorporation being linearly related to inactivation [2].

Associations of pykA with chemical compounds

Pyruvate kinases I is allosteric and pyruvate kinase II is non-allosteric to phosphoenolpyruvate [1].

References

Investigation into pyruvate kinases from Escherichia coli K-12 grown under aerobic and anaerobic conditions. Gibriel, A.Y., Doelle, H.W. Microbios (1975) [Pubmed]
Divergent binding sites in pyruvate kinases I and II from Escherichia coli. Valentini, G., Stoppini, M., Iadarola, P., Malcovati, M., Ferri, G., Speranza, M.L. Biol. Chem. Hoppe-Seyler (1993) [Pubmed]

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