2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE IS CONSERVED AMONG DIFFERENT PHYLOGENIC KINGDOMS

We have previously demonstrated that maize (Zea mays) 2,3-bisphosphogl ycerate-independent phosphoglycerate mutase (PGAM-i) is not related to 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. With the a id of specific anti-maize PGAM-i antibodies, we demonstrate here the p resence of a closely related PGAM-i in other plants. We also describe the isolation and sequencing of a cDNA-encoding almond (Prunus amygdal us) PGAM-i that further demonstrates this relationship among plant PGA M-i. A search of the major databases for related sequences allowed us to identify some novel PGAM-i from different sources: plants (Arabidop sis thaliana, Oryza sativa and Antithamniom sp.), monera (Escherichia coli, Bacillus subtilis and Bacillus magaterium) and animals (Caenorha bditis elegans). All of these amino acid sequences share a high degree of homology with plant PGAM-i. These observations suggest that the PG AM-i from several biological kingdoms constitute a family of protein d ifferent from other proteins with related enzymatic function and arose from a common ancestral gene that has diverged throughout its evoluti on.