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Volumn 64, Issue 7, 1998, Pages 2609-2615

Cloning and expression of the inositol monophosphatase gene from Methanococcus jannaschii and characterization of the enzyme

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROPHENYL PHOSPHATE; DI MYOINOSITOL 1,1' PHOSPHATE; GLUCOSE 1 PHOSPHATE; INOSITOL MONOPHOSPHATASE; PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 0031813850     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.7.2609-2615.1998     Document Type: Article
Times cited : (40)

References (43)
  • 1
    • 0023810846 scopus 로고
    • Purification and properties of myo-inositol-1-phosphatase from bovine brain
    • Attwood, P. V., J.-B. Ducep, and M.-C. Chanal. 1988. Purification and properties of myo-inositol-1-phosphatase from bovine brain. Biochem. J. 253: 387-394.
    • (1988) Biochem. J. , vol.253 , pp. 387-394
    • Attwood, P.V.1    Ducep, J.-B.2    Chanal, M.-C.3
  • 2
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signaling
    • Berridge, M. J., and R. F. Irvine. 1989. Inositol phosphates and cell signaling. Nature 341:197-205.
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 3
    • 0026493674 scopus 로고
    • Structure of inositol monophosphatase, the putative target of lithium therapy
    • Bone, R., J. P. Springer, and J. R. Atack. 1992. Structure of inositol monophosphatase, the putative target of lithium therapy. Proc. Natl. Acad. Sci. USA 89:10031-10035.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10031-10035
    • Bone, R.1    Springer, J.P.2    Atack, J.R.3
  • 5
    • 0028105959 scopus 로고
    • Structural studies of metal binding by inositol monophosphatase: Evidence for two metal ion catalysis
    • Bone, R., L. Frank, J. P. Springer, S. J. Pollack, S. Osborn, and J. R. Atack. 1994. Structural studies of metal binding by inositol monophosphatase: evidence for two metal ion catalysis. Biochemistry 33:9468-9476.
    • (1994) Biochemistry , vol.33 , pp. 9468-9476
    • Bone, R.1    Frank, L.2    Springer, J.P.3    Pollack, S.J.4    Osborn, S.5    Atack, J.R.6
  • 7
    • 0014027508 scopus 로고
    • Biochemical studies on inositol. IX. D-Inositol-1-phosphate as intermediate in the biosynthesis of inositol from glucose-6-phosphate and characteristics of two reactions in this biosynthesis
    • Chen, I.-W., and C. F. Charalampous. 1966. Biochemical studies on inositol. IX. D-Inositol-1-phosphate as intermediate in the biosynthesis of inositol from glucose-6-phosphate and characteristics of two reactions in this biosynthesis. J. Biol. Chem. 241:2194-2199.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2194-2199
    • Chen, I.-W.1    Charalampous, C.F.2
  • 8
    • 0006277519 scopus 로고
    • Biochemical studies on inositol. VIII. Purification and properties of the enzyme system which converts glucose-6-phosphate to inositol
    • Chen, I.-W., and C. F. Charalampous. 1965. Biochemical studies on inositol. VIII. Purification and properties of the enzyme system which converts glucose-6-phosphate to inositol. J. Biol. Chem. 240:3507-3512.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3507-3512
    • Chen, I.-W.1    Charalampous, C.F.2
  • 9
    • 0013606754 scopus 로고
    • Biochemical studies on inositol. X. Partial purification of yeast inositol-1-phosphatase and its separation from glucose-6-phosphate cyclase
    • Chen, I.-W., and C. F. Charalampous. 1966. Biochemical studies on inositol. X. Partial purification of yeast inositol-1-phosphatase and its separation from glucose-6-phosphate cyclase. Arch. Biochem. Biophys. 117:154-157.
    • (1966) Arch. Biochem. Biophys. , vol.117 , pp. 154-157
    • Chen, I.-W.1    Charalampous, C.F.2
  • 11
    • 0027966149 scopus 로고
    • Occurrence and role of di-myo-inositol-1,1′-phosphate in Methanococcus igneus
    • Ciulla, R. A., S. Burggraf, K. O. Stetter, and M. F. Roberts. 1994. Occurrence and role of di-myo-inositol-1,1′-phosphate in Methanococcus igneus. Appl. Environ. Microbiol. 60:3660-3664.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3660-3664
    • Ciulla, R.A.1    Burggraf, S.2    Stetter, K.O.3    Roberts, M.F.4
  • 12
    • 0023161267 scopus 로고
    • Measurement of biosynthesis of myo-inositol from glucose-6-phosphate
    • Eisenberg, F., Jr., and P. Ranganathan. 1987. Measurement of biosynthesis of myo-inositol from glucose-6-phosphate. Methods Enzymol. 141:127-143.
    • (1987) Methods Enzymol. , vol.141 , pp. 127-143
    • Eisenberg Jr., F.1    Ranganathan, P.2
  • 13
    • 0006575210 scopus 로고
    • Inositol-1-phosphate synthetase and inositol-1-phosphatase from yeast
    • Frixos, C., and I.-W. Chen. 1965. Inositol-1-phosphate synthetase and inositol-1-phosphatase from yeast. Methods Enzymol. 9:698-704.
    • (1965) Methods Enzymol. , vol.9 , pp. 698-704
    • Frixos, C.1    Chen, I.-W.2
  • 14
    • 0025331691 scopus 로고
    • Kinetic studies with myo-inositol monophosphatase from bovine brain
    • Ganzhorn, A. J., and M. C. Chanal. 1990. Kinetic studies with myo-inositol monophosphatase from bovine brain. Biochemistry 29:6065-6071.
    • (1990) Biochemistry , vol.29 , pp. 6065-6071
    • Ganzhorn, A.J.1    Chanal, M.C.2
  • 16
    • 0029582670 scopus 로고
    • Plant inositol monophosphatase is a lithium-sensitive enzyme encoded by a multigene family
    • Gillaspy, G. E., J. S. Keddie, K. Okda, and W. Gruissem. 1995. Plant inositol monophosphatase is a lithium-sensitive enzyme encoded by a multigene family. Plant Cell 7:2175-2185.
    • (1995) Plant Cell , vol.7 , pp. 2175-2185
    • Gillaspy, G.E.1    Keddie, J.S.2    Okda, K.3    Gruissem, W.4
  • 18
    • 84957891654 scopus 로고
    • Further studies on myo-inositol-1-phosphatase from the pollen of lilium longiflorum thunb
    • Rockville
    • Gumber, S. C., M. W. Loewus, and F. A. Loewus. 1984. Further studies on myo-inositol-1-phosphatase from the pollen of lilium longiflorum thunb. Plant Physiol. (Rockville) 76:40-44.
    • (1984) Plant Physiol. , vol.76 , pp. 40-44
    • Gumber, S.C.1    Loewus, M.W.2    Loewus, F.A.3
  • 19
    • 0019127799 scopus 로고
    • The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain
    • Hallcher, L. M., and W. R. Sherman. 1980. The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain. J. Biol. Chem. 255:10896-10901.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10896-10901
    • Hallcher, L.M.1    Sherman, W.R.2
  • 20
    • 0013946834 scopus 로고
    • A new micromethod for the colorimetric determination of inorganic phosphate
    • Itaya, K., and U. Michio. 1966. A new micromethod for the colorimetric determination of inorganic phosphate. Clin. Chim. Acta 14:361-366.
    • (1966) Clin. Chim. Acta , vol.14 , pp. 361-366
    • Itaya, K.1    Michio, U.2
  • 21
    • 0031052258 scopus 로고    scopus 로고
    • Binding of the activation ion Co(II) to myo-inositol monophosphatase monitored by fluorescence and phosphorescence spectroscopy
    • Kwon, O.-S., and J. E. Churchich. 1997. Binding of the activation ion Co(II) to myo-inositol monophosphatase monitored by fluorescence and phosphorescence spectroscopy. J. Protein Chem. 16:1-9.
    • (1997) J. Protein Chem. , vol.16 , pp. 1-9
    • Kwon, O.-S.1    Churchich, J.E.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0002765736 scopus 로고
    • Inositol biosynthesis
    • D. J. Moore, W. F. Boss, and F. A. Loewus (ed.), Wiley-Liss, Inc., New York, N.Y.
    • Loewus, F. A. 1990. Inositol biosynthesis, p. 13-19. In D. J. Moore, W. F. Boss, and F. A. Loewus (ed.), Inositol metabolism in plants. Wiley-Liss, Inc., New York, N.Y.
    • (1990) Inositol Metabolism in Plants , pp. 13-19
    • Loewus, F.A.1
  • 25
    • 0003188062 scopus 로고
    • myo-Inositol-1-phosphatase from the pollen of lilium longiflorum thunb
    • Loewus, M. W., and F. A. Loewus. 1980. myo-Inositol-1-phosphatase from the pollen of lilium longiflorum thunb. Plant Physiol. 70:765-770.
    • (1980) Plant Physiol. , vol.70 , pp. 765-770
    • Loewus, M.W.1    Loewus, F.A.2
  • 26
    • 71849104860 scopus 로고
    • Protein measurements with the Folin phenol reagent
    • Lowry, O. H., N. J. Rosebrough, and R. J. Randall. 1951. Protein measurements with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Randall, R.J.3
  • 27
    • 0026585599 scopus 로고
    • Statistical determination of the average values of the extinction coefficient of tryptophan and tyrosine in native proteins
    • Mach, H., C. R. Middaugh, and R. V. Lewis. 1992. Statistical determination of the average values of the extinction coefficient of tryptophan and tyrosine in native proteins. Anal. Biochem. 200:74-80.
    • (1992) Anal. Biochem. , vol.200 , pp. 74-80
    • Mach, H.1    Middaugh, C.R.2    Lewis, R.V.3
  • 28
    • 0026659202 scopus 로고
    • Inositol phosphate biochemistry
    • Majerus, P. W. 1992. Inositol phosphate biochemistry. Annu. Rev. Biochem. 61:225-250.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 225-250
    • Majerus, P.W.1
  • 29
    • 0028800519 scopus 로고
    • Inositol monophosphatase activity from the Escherichia suhB gene product
    • Matsuhisa, A., N. Suzuki, T. Noda, and K. Shiba. 1995. Inositol monophosphatase activity from the Escherichia suhB gene product. J. Bacteriol. 177: 200-205.
    • (1995) J. Bacteriol. , vol.177 , pp. 200-205
    • Matsuhisa, A.1    Suzuki, N.2    Noda, T.3    Shiba, K.4
  • 30
    • 0026631351 scopus 로고
    • cDNA cloning of human and rat brain myo-inositol monophosphatase: Expression and characterization of the human recombinant enzyme
    • McAllister, G., P. Whiting, E. A. Hammond, M. R. Knowles, J. R. Atack, F. J. Bailey, R. Maigetter, and C. I. Ragan. 1992. cDNA cloning of human and rat brain myo-inositol monophosphatase: expression and characterization of the human recombinant enzyme. Biochem. J. 284:749-754.
    • (1992) Biochem. J. , vol.284 , pp. 749-754
    • McAllister, G.1    Whiting, P.2    Hammond, E.A.3    Knowles, M.R.4    Atack, J.R.5    Bailey, F.J.6    Maigetter, R.7    Ragan, C.I.8
  • 31
    • 0024286261 scopus 로고
    • Rapid purification of inositol monophosphate phosphatase from beef brain
    • Meek, J. L., T. J. Rice, and E. Anton. 1988. Rapid purification of inositol monophosphate phosphatase from beef brain. Biochem. Biophys. Res. Commun. 156:143-148.
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , pp. 143-148
    • Meek, J.L.1    Rice, T.J.2    Anton, E.3
  • 32
    • 0030764899 scopus 로고    scopus 로고
    • Regulation of inositol monophosphatase in Saccharomyces cerevisiae
    • Murray, M., and M. L. Greenberg. 1997. Regulation of inositol monophosphatase in Saccharomyces cerevisiae. Mol. Biol. 25:541-546.
    • (1997) Mol. Biol. , vol.25 , pp. 541-546
    • Murray, M.1    Greenberg, M.L.2
  • 36
    • 0031031303 scopus 로고    scopus 로고
    • Characterization of di-myo-inositol-1,1′-phosphate in the hyperthermophilic bacterium Thermotoga maritima
    • Ramakrishnan, V., M. F. J. M. Verhagen, and M. W. W. Adams. 1997. Characterization of di-myo-inositol-1,1′-phosphate in the hyperthermophilic bacterium Thermotoga maritima. Appl. Environ. Microbiol. 63:347-350.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 347-350
    • Ramakrishnan, V.1    Verhagen, M.F.J.M.2    Adams, M.W.W.3
  • 37
    • 0025015267 scopus 로고
    • Role of phosphoinositides in transmembrane signaling
    • Rana, R. S., and L. E. Hokin. 1990. Role of phosphoinositides in transmembrane signaling. Physiol. Rev. 70:115-161.
    • (1990) Physiol. Rev. , vol.70 , pp. 115-161
    • Rana, R.S.1    Hokin, L.E.2
  • 38
    • 0019615825 scopus 로고
    • Studies on avian erythrocyte metabolism: Purification of myo-inositol-1-phosphatase from chick erythrocytes
    • Roth, S. C., D. R. Harkness, and R. E. Isaacks. 1981. Studies on avian erythrocyte metabolism: purification of myo-inositol-1-phosphatase from chick erythrocytes. Arch. Biochem. Biophys. 210:465-473.
    • (1981) Arch. Biochem. Biophys. , vol.210 , pp. 465-473
    • Roth, S.C.1    Harkness, D.R.2    Isaacks, R.E.3
  • 41
    • 0026766429 scopus 로고
    • Di-myo-inositol-1,1′-phosphate: A new inositol phosphate isolated from Pyrococcus woesei
    • Scholz, S., J. Sonnenbichler, W. Schafer, and R. Hensel. 1992. Di-myo-inositol-1,1′-phosphate: a new inositol phosphate isolated from Pyrococcus woesei. FEBS Lett. 306:239-242.
    • (1992) FEBS Lett. , vol.306 , pp. 239-242
    • Scholz, S.1    Sonnenbichler, J.2    Schafer, W.3    Hensel, R.4
  • 42
    • 0022416443 scopus 로고
    • Purification and properties of myo-inositol-1-phosphatase from rat brain
    • Takimoto, K., M. Okada, Y. Matsuda, and H. Nakagawa. 1985. Purification and properties of myo-inositol-1-phosphatase from rat brain. J. Biochem. 98:363-370.
    • (1985) J. Biochem. , vol.98 , pp. 363-370
    • Takimoto, K.1    Okada, M.2    Matsuda, Y.3    Nakagawa, H.4
  • 43
    • 0010326479 scopus 로고
    • Synthesis of L,L di-myo-inositol-1,1′-phosphate: A novel inositol phosphate from Pyrococcus woesei
    • Van Leeuwen, S. H., G. A. van der Marel, R. Hensel, and J. H. van Boom. 1994. Synthesis of L,L di-myo-inositol-1,1′-phosphate: a novel inositol phosphate from Pyrococcus woesei. Recl. Trav. Chim. Pays-Bas Belg. 113:335-336.
    • (1994) Recl. Trav. Chim. Pays-Bas Belg. , vol.113 , pp. 335-336
    • Van Leeuwen, S.H.1    Van Der Marel, G.A.2    Hensel, R.3    Van Boom, J.H.4


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