Kinetic properties of pig (Sus scrofa domestica) and bovine (Bos taurus) D-fructose-1,6-bisphosphate 1-phosphohydrolase (F1,6BPase) (original) (raw)

2000, Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology

F1,6BPases from porcine and bovine lung were isolated and their kinetic properties were determined. K s , K is and b were determined assuming partial-noncompetitive inhibition (simple intersecting hyperbolic noncompetitive inhibition) of the enzyme by the substrate. Values for K s were 4.1 and 4.4 mM for porcine and bovine F1,6BPase, respectively and values for b were close to 0.55 in both cases. K is were 9 and 15 mM for porcine and bovine F1,6BPase, respectively. I 0.5 for AMP were determined as 7 mM for pig enzyme and 14 mM for F1,6BPase from bovine lung. The enzymes were inhibited by F2,6BP with K i 's of 0.19 and 0.21 mM for porcine and bovine enzymes, respectively. In the presence of AMP concentration equal to I 0.5 , the K i values for pig and bovine enzymes were 0.07 and 0.09 mM, respectively. The levels of F2,6BP, AMP and antioxidant enzymes activities in pig and bovine lung tissues were also determined. The cDNA coding sequence of pig lung F1,6BPase 1 showed a high homology with pig liver enzyme, differing only in four positions (G/C-63, T/A-808, G/C-884 and T/A-1005) resulting in a single amino acid substitution (Gly-295 for Ala-295). It is hypothesized that the lung F1,6BPase participates in gluconeogenesis, surfactant synthesis and antioxidant reactions.