Pyruvate kinase: current status of regulatory and functional properties.
Pyruvate kinase (PK) is a key enzyme for the glycolytic pathway and carbon metabolism in general. On the basis of the relevance and enormous diverse properties of this enzyme, this paper describes the results of a current and extensive review that determines the sites of conservation and/or difference in PK sequences, and the differences in the functional and regulatory properties of the enzymes. An alignment and analysis of 50 PK sequences from different sources and a phylogenetic tree are presented. This analysis was performed with reference to crystallographically characterized PK principally from E. coli, cat and rabbit muscle. A number of attributes of the enzyme that make it of particular interest in biomedicine and industry are also discussed.
Muñoz
Ma Enriqueta
ME
Facultad de Ciencias Quíicas e Ingenierí, Universidad Autónoma de Baja California, Av. Tecnológico s/n, Mesa de Otay, B.C., Tijuana, Mexico C.P. 22390.
Ponce
Elizabeth
E
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002415:Cats; D016384:Consensus Sequence; D006801:Humans; D008969:Molecular Sequence Data; D010728:Phosphoenolpyruvate / Q000378:metabolism; D010802:Phylogeny; D011770:Pyruvate Kinase / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology*; D011817:Rabbits; D016415:Sequence Alignment
D000244:Adenosine Diphosphate; D010728:Phosphoenolpyruvate; D000255:Adenosine Triphosphate; D011770:Pyruvate Kinase