Inositol-1 (or 4)-monophosphatase from Glycine max embryo axes is a phosphatase with broad substrate specificity that includes phytate dephosphorylation

Biochimica et Biophysica Acta - General Subjects

Volumn 1770, Issue 4, 2007, Pages 543-550

  Islas Flores, Ignacio ^a   Villanueva, Marco A ^a  

^a INSTITUTO DE BIOTECNOLOGÍA   (Mexico)

Author keywords

Germination; Glycine max; IMPase; Phosphatase; Phytate; Seeds

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; COPPER; FLUORIDE SODIUM; GLUCOSE 6 PHOSPHATE; INOSITOL 1 PHOSPHATASE; INOSITOL 4 PHOSPHATASE; INOSITOL PHOSPHATE; LIGASE; LITHIUM; MANGANESE; PHYTATE; PHYTIC ACID; POLYPEPTIDE; PYROPHOSPHATE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CHROMATOGRAPHY; CONTROLLED STUDY; DEPHOSPHORYLATION; ELUTION; EMBRYO; ENZYME ANALYSIS; ENZYME SPECIFICITY; GERMINATION; INCUBATION TIME; ISOELECTRIC FOCUSING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PHOSPHATE METABOLISM; PHYTOCHEMISTRY; PLANT GROWTH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; PROTEIN PURIFICATION; PROTEIN STABILITY; SOYBEAN; TEMPERATURE;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; CATIONS, DIVALENT; DIPHOSPHATES; ENZYME INDUCTION; ENZYME STABILITY; GERMINATION; HEAT; HYDROLYSIS; INOSITOL PHOSPHATES; KINETICS; LITHIUM CHLORIDE; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHORYLATION; PHYTIC ACID; PROTEIN DENATURATION; SEEDS; SODIUM FLUORIDE; SOYBEANS; SUBSTRATE SPECIFICITY; TIME FACTORS;

GLYCINE MAX;

EID: 33847166141     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.12.001     Document Type: Article

References (33)

1. Hegeman C.E., and Grabau E.A. A novel phytase with sequence similarity to purple acid phosphatases is expressed in cotyledons of germinating soybean seedlings. Plant Physiol. 126 (2001) 1598-1608
2. Purich D.L. Enzyme catalysis: a new definition accounting for noncovalent substrate- and product-like states. Trends Biochem. Sci. 26 (2001) 417-421
3. Visser K., Heimovaara-Dijkstra S., Kijne J.W., and Wang M. Molecular cloning and characterization of an inorganic pyrophosphatase from barley. Plant Mol. Biol. 37 (1998) 131-140
4. Nurse P.M. Cyclin dependent kinases and cell cycle control. Biosci. Rep. 22 (2002) 487-499
5. Joubès J., Chevalier C., Dudits D., Heberle-Bors E., Inzé D., Umeda M., and Renaudin J.-P. CDK-related protein kinases in plants. Plant Mol. Biol. 43 (2000) 607-620
6. Weingartner M., Pelayo H.R., Binarova P., Zwerger K., Melikant B., de la Torre C., Heberle-Bors E., and Bogre L. A plant cyclin B2 is degraded early in mitosis and its ectopic expression shortens G2-phase and alleviates the DNA-damage checkpoint. J. Cell Sci. 116 (2003) 487-498
7. Roudier F., Fedorova E., Lebris M., Lecomte P., Gyorgyey J., Vaubert D., Horvath G., Abad P., Kondorosi A., and Kondorosi E. The Medicago species A2-type cyclin is auxin regulated and involved in meristem formation but dispensable for endoreduplication-associated developmental programs. Plant Physiol. 131 (2003) 1091-1103
8. Šamaj J., Baluška F., and Hirt H. From signal to cell polarity: mitogen-activated protein kinases as sensors and effectors of cytoskeleton dynamicity. J. Exp. Bot. 55 (2004) 395-405
9. Gillaspy G.E., Keddie J.S., Oda K., and Gruissem W. Plant inositol monophosphatase is a lithium-sensitive enzyme encoded by a multigene family. Plant Cell 7 (1995) 2175-2185
10. Styer J.C., Keddie J., Spence J., and Gillaspy G.E. Genomic organization and regulation of the LeIMP-1 and LeIMP-2 genes encoding myo-inositol monophosphatase in tomato. Gene 326 (2004) 35-41
11. Loewus M.W., and Murthy P.P.N. Myo-inositol metabolism in plants. Plant Sci. 150 (2000) 1-19
12. + induces hypertrophy and down regulation of myo-inositol monophosphatase in tomato. J. Plant Growth Regul. 20 (2001) 78-86
13. Islas-Flores I., Corrales-Villamar S., Bearer E., Raya J.C., and Villanueva M.A. Isolation of lipoxygenase isoforms from Glycine max embryo axes based on apparent cross-reactivity with anti-myosin antibodies. Biochim. Biophys. Acta 1571 (2002) 64-70
14. Ames B.N. Assay of inorganic phosphate, total phosphate and phosphatases. Methods Enzymol. 8 (1966) 115-118
15. Mermall V., Post P., and Mooseker M.S. Unconventional myosins in cell movement, membrane traffic and signal transduction. Science 279 (1998) 4007-4021
16. Thompson D.B., and Erdman J.W. Phytic acid determination in soybeans. J. Food Sci. 47 (1982) 513-516
17. Kuhn N.J., and Ward S. Purification, properties, and multiple forms of a manganese-activated inorganic pyrophosphatase from Bacillus subtilis. Arch. Biochem. Biophys. 354 (1998) 47-56
18. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
19. O'Farrell P.M. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250 (1975) 4007-4021
20. Bradford M.M. A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 22 (1976) 248-254
21. Altschul S.F., Madden T.L., Schäffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 (1997) 3389-3402
22. Nigou J., Dover L.G., and Besra G.S. Purification and biochemical characterization of Mycobacterium tuberculosis SuhB, an inositol monophosphatase involved in inositol biosynthesis. Biochemistry 2 (2002) 4392-4398
23. Richardson A.E., Hadobas P.A., and Hayes J.E. Extracellular secretion of Aspergillus phytase from Arabidopsis roots enables plants to obtain phosphorus from phytate. Plant J. 25 (2001) 641-649
24. McAllister G., Whiting P., Hammond E.A., Knowles M.R., Atack J.R., Bailey F.J., Maigetter F.J., and Ragan C.I. cDNA cloning of human and rat brain myo-inositol monophosphatase: expression and characterization of the human recombinant enzyme. Biochem. J. 284 (1992) 749-754
25. Janczarek M., and Skorupska A. The Rhizobium leguminosarum bv. trifolii pssB gene product is an inositol monophosphatase that influences exopolysaccharide synthesis. Arch. Microbiol. 175 (2001) 143-151
26. Parthasarathy L., Vadnal R.E., Ramesh T.G., Shyamaladevi C.S., and Parthasarathy R. Myo-inositol monophosphatase from rat testes: purification and properties. Arch. Biochem. Biophys. 304 (1993) 94-101
27. Loewus M.W., and Loewus F.A. Myo-inositol metabolism in plants. Plant Physiol. 70 (1982) 765-770
28. Netting A.G. pH, abscisic acid and the integration of metabolism in plants under stressed and non-stressed conditions: II. Modifications in modes of metabolism induced by variation in the tension on the water column and by stress. J. Exp. Bot. 53 (2002) 151-163
29. Villanueva M.A., Campos F., Díaz C., Colmenero-Flores J.M., Dantán E., Sánchez F., and Covarrubias A.A. Actin expression in germinating seeds of Phaseolus vulgaris L. Planta 207 (1999) 582-589
30. Phiel C.J., and Klein P.S. Molecular targets of lithium action. Annu. Rev. Pharmacol. Toxicol. 41 (2001) 789-813
31. Huang S., McDowell J.M., Weise M.J., and Meagher R.B. The Arabidopsis profilin gene family. Evidence for an ancient split between constitutive and pollen-specific profilin genes. Plant Physiol. 111 (1996) 115-126
32. Guillén G., Valdés-López V., Noguez R., Olivares J., Rodríguez-Zapata L.C., Pérez H., Vidali L., Villanueva M.A., and Sánchez F. Profilin in Phaseolus vulgaris is encoded by two genes (only one expressed in root nodules) but multiple isoforms are generated in vivo by phosphorylation on tyrosine residues. Plant J. 19 (1999) 497-508
33. Michell B. Inositol phosphates. Profusion and confusion. Nature 319 (1986) 176-177