Kinetic properties of pig (Sus scrofa domestica) and bovine (Bos taurus) D-fructose-1,6-bisphosphate 1-phosphohydrolase (F1,6BPase): Liver-like isozymes in mammalian lung tissue

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 127, Issue 1, 2000, Pages 123-134

  Rakus, Dariusz ^a   Skalecki, Krzysztof ^a   Dzugaj, Andrzej ^a  

^a UNIVERSITY OF WROC AW   (Poland)

Author keywords

Antioxidant enzymes; F1,6Bpase; Gluconeogenesis; Glucose 6 phosphate; Kinetics; Lung; Primary structure

Indexed keywords

ADENOSINE PHOSPHATE; ANTIOXIDANT; COMPLEMENTARY DNA; FRUCTOSE BISPHOSPHATASE; LUNG ENZYME;

ANIMAL TISSUE; ARTICLE; CATTLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME PURIFICATION; GLUCONEOGENESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SWINE;

ANIMALIA; BOS TAURUS; BOVINAE; MAMMALIA; SUIDAE; SUS; SUS SCROFA; SUS SCROFA DOMESTICA;

EID: 0034283264     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(00)00245-5     Document Type: Article

References (47)

1. Aebi, H.E., 1983. Catalase. In: Bergmeyer, H.U. (Ed.), Methods of Enzymatic Analysis, vol. 3. Verlag Chemie, Weinheim, pp. 273-282.
2. Al-Robaiy, S., Eschrich, K., 1999. Rat muscle fructose-1,6-bisphosphatse: cloning of the cDNA, expression of the recombinant enzyme, and expression analysis in different tissues. Biol. Chem. 380, 1079-1085.
3. Burchell, A., Waddell, I.D., Countaway, J.L., Arion, W.J., Hume, R., 1988. Identification of the human hepatic microsomal glucose-6-phosphatase enzyme. FEBS Lett. 242, 153-156.
4. Chen, L., Hegde, R., Chen, M., Fromm, H.J., 1993. Site directed mutagenesis of the metal binding sites of porcine fructose-1,6-bisphosphatase. Arch. Biochem. Biophys. 307, 350-354.
5. Chomczynski, P., Sacchi, N., 1988. Single step method of RNA isolation by guanidinum thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
6. Creuwels, L.A.J.M., van Golde, L.M.G., Haagsman, H.P., 1997. The pumonary surfactant system: biochemical and clinical aspects. Lung 175, 1-39.
7. Deutsch, J., 1983. Glucose-6-phosphate dehydrogenase. In: Bergmeyer, H.U. (Ed.), Methods of Enzymatic Analysis, vol. 3. Verlag Chemie, Weinheim, pp. 190-197.
8. Dzugaj, A., Kochman, M., 1980. Purification of human liver fructose-1,6-bisphosphatase. Biochim. Biophys. Acta. 614, 407-412.
9. El-Maghrabi, M.R., Gidh-Jain, M., Austin, L.R., Pilkis, S.J., 1993. Isolation of human liver fructose1,6-bisphosphatase cDNA and expression of the protein in Escherichia coli. J. Biol. Chem. 268, 9466-9472.
10. Fournier, P.A., Guderley, H., 1992. Metabolic fate of lactate after vigorous activity in the leopard frog, Rana pipiens. Am. J. Physiol. 262, 245-254.
11. Goldberg, D.M., Spooner, R.J., 1983. Glutathione reductase. In: Bergmeyer, H.U. (Ed.), Methods of Enzymatic Analysis, vol. 3. Verlag Chemie, Weinheim, pp. 258-266.
12. Jaworek, D., Welsch, J., 1983. Adenosine 5′-diphosphate and adenosine 5′-monophosphate. In: Bergmeyer, H.U. (Ed.), Methods of Enzymatic Analysis, vol. 7. Verlag Chemie, Weinheim, pp. 365-370.
13. Kirkman, H.N., Galiano, S., Gaetani, G.F., 1987. The function of catalase-bound NADPH. J. Biol. Chem. 262, 660-666.
14. Latres, E., Alemany, M., Remesar, X., 1992. In vivo glucose metabolism in the rat lung. Biochem. Arch. 8, 175-182.
15. Leatherbarrow, R.J., 1992. GraFit 3.0. Erithacus Software, Staines, UK.
16. Liu, F., Fromm, H.J., 1988. Purification and characterisation of fructose-1,6-bisphosphatase from bovine brain. Arch. Biochem. Biophys. 260, 609-615.
17. Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275.
18. Maniscalco, W.M., Wilson, C.M., Gross, I., Gobran, L., Rooney, S.A., Warshaw, J.B., 1978. Development of glycogen and phospholipid metabolism in fetal and newborn rat lung. Biochim. Biophys. Acta. 530, 333-346.
19. Marcus, C.J., Geller, A.M., Byrne, W.L., 1973. Studies on bovine hepatic fructose 1,6-diphosphatase. J. Biol. Chem. 248, 8567-8573.
20. Maritz, G.S., 1993. Carbohydrate metabolism of lung tissue of suckling and adult rats. Cell. Biol. Int. 17, 773-780.
21. McLane, J.A., Holloszy, J.O., 1979. Glycogen synthesis from lactate in three types of skeletal muscle. J. Biol. Chem. 254, 6548-6553.
22. Mithieux, G., Bordet, J.C., Minassian, C., Ajzannay, A., Mercier, I., Riou, J.P., 1993. Characteristic and specifity of the inhibition of liver glucose-6-phosphatase by arachidonic acid. Eur. J. Biochem. 666, 1-6.
23. Mizunuma, H., Tashima, Y., 1978. Fructose 1,6-bisphosphatase of the small intestine. J. Biochem. 84, 327-336.
24. Mizunuma, H., Tashima, Y., 1990. Survey of fructose 1,6-bisphosphatase isoenzyme in rat organs and ontogenic expression of the enzyme in rat fetus. Int. J. Biochem. 22, 883-888.
25. Newsholme, E.A., Start, C., 1976. Regulation in carbohydrate metabolism in muscle. In: Regulation in Metabolism, Wiley, London, pp. 88-145.
26. Nimmo, H.G., Tipton, K.F., 1975. The allosteric properties of beef-liver fructose bisphosphatase. Eur. J. Biochem. 58, 575-585.
27. Paoletti, F., Mocali, A., 1999. Determination of superoxide dismutase activity by purely chemical system based on NADP(H) oxidation. Methods Enzymol. 186, 209-220.
28. Petrescu, I., Bojan, O., Saied, M., Barzu, O., Schmidt, F., Kühnle, H.F., 1979. Determination of phospho-enolpyruvate carboxykinase activity with de-oxyganosine 5′-diphosphate as nucleotide substrate. Anal. Biochem. 96, 279-281.
29. Pilkis, S.J., El-Maghrabi, M.R., McGrane, M.M., Pilkis, J., Claus, T.H., 1981. The role of fructose 2,6-bisphosphate in regulation of fructose-1,6-bis-phosphatase. J. Biol. Chem. 256, 3619-3622.
30. Pütter, J., Becker, R., 1983. Peroxidases. In: Bergmeyer, H.U. (Ed.), Methods of Enzymatic Analysis, vol. 3. Verlag Chemie, Weinheim, pp. 286-293.
31. Riquelme, P.T., Czarnecki, J.J., 1983. Conformational and allosteric changes in fructose 1,6-bisphosphatase upon photoaffinity labeling with 2-azidoadenosine monophosphate. J. Biol. Chem. 258, 8240-8245.
32. Sambrook, J., Fritsch, E.F., Maniatis, T., 1989. Molecular cloning: A laboratory manual, ed. 2. C.S.H.L. Press, Cold Spring Harbor, NY.
33. Sanger, F., Nicklen, S., Coulson, A.R., 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
34. Segel, I.H., 1975. Rapid equilibrium partial and mixed-type inhibition. In: Enzyme kinetics. Wiley, pp. 166-9.
35. Skalecki, K., Mularczyk, W., Dzugaj, A., 1995. Kinetic properties of D-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle. Biochem. J. 310, 1029-1035.
36. Skalecki, K., Rakus, D., Wiśniewski, J.R., Kołodziej, J., Dzugaj, A., 1999. cDNA sequence and kinetic properties of human lung fructose(1,6)bisphosphatase. Arch. Biochem. Biophys. 365, 1-9.
37. Tejwani, G.A., 1983. Regulation of fructose-bisphosphatase activity. Adv. Enzymol. Relat. Areas Mol. Biol. 54, 121-194.
38. Tillmann, H., Eschrich, K., 1998. Isolation and characterization of an allelic cDNA for human muscle fructose-1,6-bisphosphatase. Gene 212, 295-304.
39. Towbin, H., Staehelin, T., Gordon, J., 1979. Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
40. Van Schaftingen, E., 1987. Fructose 2,6-bisphosphatase. Adv. Enzymol. 59, 15368-15370.
41. Van Schaftingen, E., Hers, H.G., 1981. Inhibition of fructose-1,6-bisphosphatase by fructose-2,6-bisphosphate. Proc. Natl. Acad. Sci. USA 78, 2861-2863.
42. Villeret, V., Huang, S., Zhang, Y., Lipscomb, W.N., 1995. Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography. Biochemistry 34, 4307-4315.
43. Villet, R.H., Dalziel, K., 1969. Purification and properties 6-phosphogluconate dehydrogenase from sheep liver. Biochem. J. 115, 639-643.
44. Weber, K., Osborn, M., 1969. The reliability of molecular weight determination by dodecyl sulphate polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406-4412.
45. Williams, M.K., Kantrowitz, E.R., 1992. Isolation and sequence analysis of cDNA for pig kidney fructose 1,6-bisphosphatase. Proc. Natl. Acad. Sci. USA 89, 3080-3082.
46. 2+ at 2.0 - A resolution: aspects of synergism between inhibitors. Proc. Natl. Acad. Sci. USA 91, 12482-12486.
47. Zhang, Y.P., Liang, J.Y., Huang, S.H., Lipscomp, W.N., 1994. Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase. J. Mol. Biol. 244, 609-624.