Inactivation of brain myo-inositol monophosphate phosphatase by pyridoxal-5′-phosphate

Journal of Biochemistry and Molecular Biology

Volumn 38, Issue 1, 2005, Pages 58-64

  Dae, Won Kim ^a   Joung, Woo Hong ^b   Won, Sik Eum ^a   Hee, Soon Choi ^a   Soo, Hyun Choi ^a   So, Young Kim ^a   Byung, Ryong Lee ^a   Jae, Jin An ^a   Sun, Hwa Lee ^a   Seung, Ree Lee ^a   Kwon, Oh Shin ^c   Hyeok, Yil Kwon ^a   Cho, Sung Woo ^d   Kil, Soo Lee ^a   Park, Jinseu ^a   Soo, Young Choi ^a  

^a Hallym University   (South Korea)

^b OHIO STATE UNIVERSITY   (United States)

^c Kyungpook National University   (South Korea)

^d University of Ulsan College of Medicine   (South Korea)

Author keywords

Myo inositol monophosphate phosphatase; Peptide analysis; Pyridoxal 5 phosphate; Reactive lysine residue

Indexed keywords

SUIDAE;

AMINO ACID; BORANE DERIVATIVE; INOSITOL 1-PHOSPHATE; INOSITOL PHOSPHATE; LYSINE; MYO INOSITOL 1 (OR 4) MONOPHOSPHATASE; MYO-INOSITOL-1 (OR 4)-MONOPHOSPHATASE; PEPTIDE FRAGMENT; PHENYLTHIOHYDANTOIN; PHOSPHATASE; PYRIDOXAL 5 PHOSPHATE; SODIUM BOROHYDRIDE;

ANIMAL; ARTICLE; BINDING SITE; BRAIN; CATALYSIS; CHEMISTRY; COMPARATIVE STUDY; DRUG ANTAGONISM; DRUG EFFECT; ENZYME ACTIVATION; ENZYMOLOGY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN BINDING; SWINE; TIME;

AMINO ACIDS; ANIMALS; BINDING SITES; BOROHYDRIDES; BRAIN; CATALYSIS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ENZYME ACTIVATION; INOSITOL PHOSPHATES; LYSINE; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PHENYLTHIOHYDANTOIN; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN BINDING; PYRIDOXAL PHOSPHATE; SWINE; TIME FACTORS;

EID: 21244446704     PISSN: 12258687     EISSN: 12258687     Source Type: Journal    
DOI: None     Document Type: Article

References (31)

1. Abdel-Latif, A. A. (1986) Calcium-mobilizing receptor, polyphosphoinositide, and the generation of second messengers. Pharmarcol. Rev. 38, 227-272.
2. Allison, J. H. and Stewart, M. A. (1971) Reduced brain inositol in lithium-treated rats. Nature 233, 267-268.
3. Allison, J. H., Blisner, M. E., Holland, W. H., Hipps, P. P. and Sherman, W. R. (1976) Increased brain myo-inositol-1-phosphate in lithium-treated rats. Biochem. Biophys. Res. Commun. 71, 664-670.
4. Anderson, B. M., Anderson, C. D. and Churchich, J. E. (1996) Inhibition of glutamic dehydrogenase by pyridoxal-5′-phosphate. Biochemistry 5, 2893-2900.
5. Avissar, S., Schreiber, G., Danon, A. and Belmaker, R. H. (1988) Lithium inhibits adrenergic and cholinergic increases in GTP binding in rat cortex. Nature 331, 440-442.
6. Batty, I. and Nahoski, S. R. (1987) Lithium inhibits muscarinic-receptor stimulated inositol terakisphosphate accumulation in rat cerebral cortex. Biochem. J. 247, 797-800.
7. Bello, M. L., Petruzzelli, R., Lucia, R., Ricci, G., Barra, D. and Federici, G. (1992) Chemical modification of human placental glutathione transferase by pyridoxal-5′-phosphate. Biochim. Biophys. Acta 1121, 1384-1389.
8. Berridge, M. J. (1984) Inositol triphosphate and diacylglycerol as second messengers. Biochem. J. 220, 345-360.
9. Berridge, M. J., Downes, C. P. and Hanley, M. R. (1982) Lithium amplifies agonist-dependent phosphatidylinositol responses in brain and salivary glands. Biochem. J. 206, 587-595.
10. Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
11. Camardella, L., Romano, M., di Prisco, G. and Cancedda, F. D. (1981) Human erythrocytes glucose-6-phosphate dehydrogenase; labeling of a reactive lysyl residue by pyridoxal-5′-phosphate. Biochem. J. 103, 1384-1389.
12. Churchich, J. E. (1965) Energy transfer in protein pyridoxamine-5- phosphate conjugates. Biochemistry 4, 1405-1410.
13. Diehl, R. E., Whiting, P., Potter, J., Gee, N. S., Ragan, C. I., Linemeyer, D., Schoepfer, R., Bennet, C. and Dixon, R. A. (1990) Cloning and expression of bovine brain inositol monophosphatase. J. Biol. Chem. 265, 5946-5949.
14. Dong, Q. and Fromm, H. J. (1990) Chemical modification of adenylosuccinate synthetase from Escherichia coli by pyridoxal-5-phosphate conjugates. J. Biol. Chem. 265, 6235-6240.
15. Gee, N. S., Ragan, C. I., Watling, K. J., Aspley, S., Jackson, R. G., Reid, G. G., Gani, D. and Shute, T. K. (1988) The purification and properties of myo-inositol monophosphatase from bovine brain. Biochem. J. 249, 883-889.
16. Godfrey, P. P., McClue, S. J., White, A. M., Wood, A. J. and Grahamesmith, D. G. (1989) Subacute and chronic in vitro lithium treatment inhibits agonist and sodium fluoride-stimulated inositol phosphate production in rat cortex. J. Neurochem. 52, 498-506.
17. Gumber, S. C., Loewas, M. W. and Loewas, F. A. (1984) Further studies on myo-inositol-1-phosphatase from the pollen of Lilium longiflorum Thunb. Plant Physiol. 76, 40-44.
18. Hallcher, L. M. and Sherman, W. R. (1980) The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain. J. Biol. Chem. 255, 10897-10901.
19. Itaya, K. and Ui, M. (1966) A new micro method for the colorimetric determination of inorganic phosphate. Clin. Chim. Acta 14, 361-366.
20. Jeffery, J., Hobbs, L. and Jornvall, H. (1985) Glucose-6-phosphate dehydrogenase from Saccharomyces cerevisiae: characterization of a reactive lysine residue labeled with acetylsalicylic acid. Biochemistry 24, 666-671.
21. Kwon, H. Y., Shin, H. C., Lee, Y. L., Cho, S.-W. and Choi, S. Y. (1993) Purification and properties of myo-inositol monophosphate phosphatase from porcine brain. Mol. Cells 3, 95-99.
22. Lee, B. R., Bahn, J. H., Jeon, S. G., Ahn, Y. K., Yoon, B. H., Kwon, H. Y., Kwon, O. S. and Choi, S. Y. (1999) Chemical modification of porcine brain myo-inositol monophosphate phosphatase by N-bromosuccinimide J. Biochem. Mol. Biol. 32, 294-298.
23. Majerus, P. W. (1992) Inositol phosphate biochemistry. Annu. Rev. Biochem. 61, 225-250.
24. Matsuyama, T., Soda, K., Fukui, T. and Tanizawa, K. (1992) Leucine dehydrogenase from Bacillus stearothermophilus: identification of active-site lysine by modification with pyridoxal phosphate. J. Biochem. 112, 258-265.
25. Mauck, J. L., Wong, Y. H. and Sherman, W. R. (1980) L-myo-inositol phosphate synthetase from bovine testis: Purification to homogeneity and partial characterization. Biochemistry 19, 3623-3629.
26. McAllister, G., Whiting, P. J., Hammond, E. A., Knowles, M. R., Atack, T. R., Bailey, F. J., Maigetler, R. and Ragan, C. I. (1992a) Bovine inositol monophosphatase modification, identification and mutagenesis of reactive cystein residues. Biochem. J. 285, 461-468.
27. McAllister, G., Whiting, P., Hammond, E. A., Knowles, M. R., Atack, J. R., Bailey, F. J., Maigetter, R. and Ragan, C. I. (1992b) cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme. Biochem. J. 284, 749-754.
28. Meek, J. L., Rice, T. J. and Anton, E. (1988) Rapid purification of inositol monophosphate phosphatase from beef brain. Biochem. Biophys. Res. Commun. 156, 143-148.
29. Sherman, W. R., Leavitt, A. L., Honcher, M. P., Hallcher, L. M. and Phillips, B. E. (1981) Evidence that lithium alters phosphoinositides metabolism: Chronic administration elevates primarily D-myo-inositol-1-phosphate in cerebral cortex of the rat. J Neurochem. 36, 1947-1951.
30. Sjoholt, G., Molven, A., Lovlie, R., Wilcos, A., Sikela, J. M. and Steen, V. M. (1997) Genomic structure and chromosomal localization of a human myo-inositol monophosphatase gene (IMPP). Genomics 45, 113-122.
31. Takimoto, K., Okada, M., Matsuda, Y. and Nakagawa, H. (1985) Purification and properties of myo-inositol-1-phosphatase from rat brain. J. Biochem. (Tokyo) 98, 363-370.