PMID:12798932
| Citation |
Muñoz, ME and Ponce, E (2003) Pyruvate kinase: current status of regulatory and functional properties. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 135:197-218 |
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| Abstract |
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. |
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| Keywords |
Adenosine Diphosphate/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Animals; Binding Sites; Cats; Consensus Sequence; Humans; Molecular Sequence Data; Phosphoenolpyruvate/metabolism; Phylogeny; Pyruvate Kinase/chemistry; Pyruvate Kinase/metabolism; Pyruvate Kinase/physiology; Rabbits; Sequence Alignment |
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