Pyruvate kinase isozymes: Ancient diversity retained in modern plant cells

Pyruvate kinase is a key regulatory enzyme of glycolysis. Phylogenetic analyses of the sequences coding for pyruvate kinase from plants and other organisms revealed unexpected diversity of this glycolytic enzyme in the progenitor of the present-day eukaryotes. Plants contain an ancient lineage of cy...

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Bibliographic Details
Published in:Biochemical Systematics and Ecology 1995-11, Vol.23 (7), p.773,779-777,780
Main Authors: Hattori, Jiro, Baum, Bernard R., Mchugh, Sylvia G., Blakele, Stephen D., Dennis, David T., Miki, Brian L.
Format: Article
Language:English
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Summary:Pyruvate kinase is a key regulatory enzyme of glycolysis. Phylogenetic analyses of the sequences coding for pyruvate kinase from plants and other organisms revealed unexpected diversity of this glycolytic enzyme in the progenitor of the present-day eukaryotes. Plants contain an ancient lineage of cytosolic pyruvate kinase, which may have diverged from the animal pyruvate kinase genes prior to the plant-animal divergence. The plant cytosolic pyruvate kinase genes are no more closely related to the animal and fungal pyruvate kinase genes than to the prokaryotic pyruvate kinase genes. The results suggest that the plant pyruvate kinase genes and the animal-fungal pyruvate kinase genes have descended from divergent isozymes which existed in the progenitor of the present-day eukaryotes and prokaryotes.
ISSN:0305-1978
1873-2925
DOI:10.1016/0305-1978(95)00061-5