Human glyceraldehyde-3-phosphate dehydrogenase in man-rodent somatic cell hybrids.
The human enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) forms heteropolymers with the rodent enzyme in man-rodent somatic cell hybrids. A gene specifying GAPDH is syntenic with the genes specifying the glycolytic enzymes triosephosphate isomerase (TPI) and lactate dehydrogenase B (LDH-B). The synteny of GAPDH, TPI, and LDH-B is the first evidence for the syntenic association of human genes that specify enzymes of the Embden-Meyerhof glycolytic pathway.
D000818:Animals; D002874:Chromosome Mapping; D002906:Chromosomes, Human, 6-12 and X; D005796:Genes; D008040:Genetic Linkage; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000096:biosynthesis*; D006801:Humans; D006822:Hybrid Cells / Q000201:enzymology*; D007770:L-Lactate Dehydrogenase / Q000096:biosynthesis; D009243:NAD / Q000378:metabolism; D011487:Protein Conformation; D012377:Rodentia; D014305:Triose-Phosphate Isomerase / Q000096:biosynthesis
D009243:NAD; D007770:L-Lactate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D014305:Triose-Phosphate Isomerase