Abstract
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) is a bifunctional enzyme that catalyzes the synthesis and degradation of Fru-2,6-P2, a key regulator of glycolysis. In mammals, several genes have been found to code for different PFK-2/FBPase-2 isoforms that differ in tissue distribution and enzymatic activities. In the present study, we report the characterization of the PFK-2/FBPase-2 heart isoform gene in humans (PFKFB2), including a full analysis of repetitive sequences and potential transcription binding sites. The genomic sequence of the PFKFB2 gene spans 22,485 bp and contains 15 exons. Heart cDNA analysis shows that PFKFB2 codes for a protein of 505 amino acids with a deduced molecular mass of 58,849 Da. Comparison of the human PFKFB2 gene to the homologous genes in rat and ox outlines a significant conservation of the intron-exon structure, sequence of 5' and 3' flanking regions, and simple sequence repetitive element positions. Most important, the human heart PFK-2/ FBPase-2 protein was found to retain all the important regulatory sites, as well as the catalytic and substrate binding sites identified in the rat and bovine heart isoforms, suggesting that the human enzyme is regulated in a manner similar to that observed in these organisms.
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