메뉴 건너뛰기




Volumn 187, Issue 12, 2005, Pages 4270-4275

A phosphohexomutase from the archaeon Sulfolobus solfataricus is covalently modified by phosphorylation on serine

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GLUCOSE 1 PHOSPHATE; GLUCOSE 6 PHOSPHATE; GLUCOSE 6 PHOSPHATE ISOMERASE; MANNOSE 6 PHOSPHATE; MANNOSE PHOSPHATE; PHOSPHOSERINE; RECOMBINANT PROTEIN;

EID: 20444485358     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.12.4270-4275.2005     Document Type: Article
Times cited : (19)

References (45)
  • 1
    • 0017184389 scopus 로고
    • A rapid and simple method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and simple method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 0035489058 scopus 로고    scopus 로고
    • The glycogen-bound polyphosphate kinase from Sulfolobus acidocaldarius is actually a glycogen synthase
    • Cardona, S., F. Remonsellez, N. Guiliani, and C. A. Jerez. 2001. The glycogen-bound polyphosphate kinase from Sulfolobus acidocaldarius is actually a glycogen synthase. Appl. Environ. Microbiol. 67:4773-47780.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4773-47780
    • Cardona, S.1    Remonsellez, F.2    Guiliani, N.3    Jerez, C.A.4
  • 3
    • 0018787232 scopus 로고
    • Mechanism of phosphoacetylglucosamine mutase
    • Cheng, P.-W., and D. M. Carlson. 1979. Mechanism of phosphoacetylglucosamine mutase. J. Biol. Chem. 254:8353-8357.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8353-8357
    • Cheng, P.-W.1    Carlson, D.M.2
  • 4
    • 0031904531 scopus 로고    scopus 로고
    • A novel amino-peptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus
    • Condo, I., D. Ruggero, R. Reinhardt, and P. Londel. 1998. A novel amino-peptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus. Mol. Microbiol. 29:775-785.
    • (1998) Mol. Microbiol. , vol.29 , pp. 775-785
    • Condo, I.1    Ruggero, D.2    Reinhardt, R.3    Londel, P.4
  • 5
    • 0035920129 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of p85 relieves its inhibitory activity on phosphatidylinositol 3-kinase
    • Cuevas, B. D., Y. Lu, M. Mao, J. Zhang, R. LaPushin, K. Siminovitch, and G. B. Mills. 2001. Tyrosine phosphorylation of p85 relieves its inhibitory activity on phosphatidylinositol 3-kinase. J. Biol. Chem. 276:27455-27461.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27455-27461
    • Cuevas, B.D.1    Lu, Y.2    Mao, M.3    Zhang, J.4    LaPushin, R.5    Siminovitch, K.6    Mills, G.B.7
  • 6
    • 0029809057 scopus 로고    scopus 로고
    • Purification and properties of an enzyme involved in the ATP-dependent activation of the methanol: 2-Mercaptoethanesulfonic acid methyltransferase reaction in Methanosarcina barkeri
    • Daas, P. J. H., R. W. Wassenaar, P. Willemsen, R. J. Theunissen, J. T. Keltjens, C. van der Drift, and G. D. Vogels. 1996. Purification and properties of an enzyme involved in the ATP-dependent activation of the methanol: 2-mercaptoethanesulfonic acid methyltransferase reaction in Methanosarcina barkeri. J. Biol. Chem. 271:22339-22345.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22339-22345
    • Daas, P.J.H.1    Wassenaar, R.W.2    Willemsen, P.3    Theunissen, R.J.4    Keltjens, J.T.5    Van Der Drift, C.6    Vogels, G.D.7
  • 7
    • 0024380864 scopus 로고
    • Phosphorylation inactivates Escherichia coli isocitrate dehydrogenase by preventing isocitrate binding
    • Dean, A. M., M. H. I. Lee, and D. E. Koshland, Jr. 1989. Phosphorylation inactivates Escherichia coli isocitrate dehydrogenase by preventing isocitrate binding. J. Biol. Chem. 264:20482-20486.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20482-20486
    • Dean, A.M.1    Lee, M.H.I.2    Koshland Jr., D.E.3
  • 8
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks, G., T. L. Steck, and D. F. H. Wallace. 1971. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606-2617.
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallace, D.F.H.3
  • 9
    • 0141844487 scopus 로고    scopus 로고
    • Cell cyclin-dependent phosphorylation of human DNA ligase I at the cyclin-dependent kinase sites
    • Ferrari, G., R. Ariossi, D. Arioso, A. Vindigni, G. Biamonti, and A. Montecucco. 2003. Cell cyclin-dependent phosphorylation of human DNA ligase I at the cyclin-dependent kinase sites. J. Biol. Chem. 278:37761-37767.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37761-37767
    • Ferrari, G.1    Ariossi, R.2    Arioso, D.3    Vindigni, A.4    Biamonti, G.5    Montecucco, A.6
  • 11
    • 0034868902 scopus 로고    scopus 로고
    • Autophosphorylation of archaeal Cdc6 homologs is regulated by DNA
    • Grabowski, B., and Z. Kelman. 2001. Autophosphorylation of archaeal Cdc6 homologs is regulated by DNA. J. Bacteriol. 183:545-95464.
    • (2001) J. Bacteriol. , vol.183 , pp. 545-95464
    • Grabowski, B.1    Kelman, Z.2
  • 12
    • 7944222398 scopus 로고    scopus 로고
    • Regulation of phosphoglucomutase 1 phosphorylation and activity by a signaling kinase
    • Gururaj, A., C. J. Barnes, R. K. Vadlamudi, and R. Kumar. 2004. Regulation of phosphoglucomutase 1 phosphorylation and activity by a signaling kinase. Oncogene 23:8118-8127.
    • (2004) Oncogene , vol.23 , pp. 8118-8127
    • Gururaj, A.1    Barnes, C.J.2    Vadlamudi, R.K.3    Kumar, R.4
  • 13
    • 1642280378 scopus 로고    scopus 로고
    • Pseudophosphorylation of tau protein alters its ability for self-aggregation
    • Haase, C., J. T. Steiler, T. Arendt, and M. Holzer. 2004. Pseudophosphorylation of tau protein alters its ability for self-aggregation. J. Neurochem. 88:1509-1520.
    • (2004) J. Neurochem. , vol.88 , pp. 1509-1520
    • Haase, C.1    Steiler, J.T.2    Arendt, T.3    Holzer, M.4
  • 14
    • 0029976603 scopus 로고    scopus 로고
    • Using CLUSTAL for multiple sequence alignments
    • Higgins, D. G., J. D. Thompson, and T. J. Gibson. 1996. Using CLUSTAL for multiple sequence alignments. Methods Enzymol. 266:383-402.
    • (1996) Methods Enzymol. , vol.266 , pp. 383-402
    • Higgins, D.G.1    Thompson, J.D.2    Gibson, T.J.3
  • 16
    • 0025217677 scopus 로고
    • Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the enzyme
    • Hurley, J. H., A. M. Dean, P. E. Thorsness, D. E. Koshland, Jr., and R. M. Stroud. 1990. Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the enzyme. J. Biol. Chem. 265:3599-3602.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3599-3602
    • Hurley, J.H.1    Dean, A.M.2    Thorsness, P.E.3    Koshland Jr., D.E.4    Stroud, R.M.5
  • 17
    • 0242586098 scopus 로고    scopus 로고
    • Enhanced phoshorylation and enzymatic activity of phosphoglucomutase by the Btk29A tyrosine kinase in Drosophila
    • Inoue, H., S. Kondo, Y. Hinohara, N. Juni, and D. Yamamoto. 2003. Enhanced phoshorylation and enzymatic activity of phosphoglucomutase by the Btk29A tyrosine kinase in Drosophila. Arch. Biochem. Biophys. 413:207-212.
    • (2003) Arch. Biochem. Biophys. , vol.413 , pp. 207-212
    • Inoue, H.1    Kondo, S.2    Hinohara, Y.3    Juni, N.4    Yamamoto, D.5
  • 19
    • 0036064282 scopus 로고    scopus 로고
    • Tκ-PTP, a protein tyrosine/serine phosphatase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1: Enzymatic characteristics and identification of its substrate proteins
    • Jeon, S.-J., S. Fujiwara, M. Takagi, T. Tanaka, and T. Imanaka. 2002. Tκ-PTP, a protein tyrosine/serine phosphatase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1: enzymatic characteristics and identification of its substrate proteins. Biochem. Biophys. Res. Commun. 295:508-514.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 508-514
    • Jeon, S.-J.1    Fujiwara, S.2    Takagi, M.3    Tanaka, T.4    Imanaka, T.5
  • 23
    • 0037335790 scopus 로고    scopus 로고
    • Archaeal protein kinases and protein phosphatases - Insights from genomics and biochemistry
    • Kennelly, P. J. 2003. Archaeal protein kinases and protein phosphatases - insights from genomics and biochemistry. Biochem. J. 370:373-389.
    • (2003) Biochem. J. , vol.370 , pp. 373-389
    • Kennelly, P.J.1
  • 24
    • 0020463405 scopus 로고
    • Glycogen in thermoacidophilic archaebacteria of the genera Sulfolobus, Thermoproteus, Desulfurococcus, and Thermococcus
    • Konig, H., R. Skorko, W. Zillig, and W.-F. Reiter. 1982. Glycogen in thermoacidophilic archaebacteria of the genera Sulfolobus, Thermoproteus, Desulfurococcus, and Thermococcus. Arch. Microbiol. 132:297-303.
    • (1982) Arch. Microbiol. , vol.132 , pp. 297-303
    • Konig, H.1    Skorko, R.2    Zillig, W.3    Reiter, W.-F.4
  • 25
    • 0033564594 scopus 로고    scopus 로고
    • Comparison of the in vivo and in vitro phosphorylation of exocytosis-sensitive protein PP63/perfusin by differential MALDI mass spectrometric peptide mapping
    • Kussmann, M., K. Hauser, R. Kissmehl, J. Breed, H. Plattner, and P. Roepstorff. 1999. Comparison of the in vivo and in vitro phosphorylation of exocytosis-sensitive protein PP63/perfusin by differential MALDI mass spectrometric peptide mapping. Biochemistry 38:7780-7790.
    • (1999) Biochemistry , vol.38 , pp. 7780-7790
    • Kussmann, M.1    Hauser, K.2    Kissmehl, R.3    Breed, J.4    Plattner, H.5    Roepstorff, P.6
  • 26
    • 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
  • 27
  • 28
    • 0346725952 scopus 로고    scopus 로고
    • Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A
    • Lee, H., N. Rezai-Zadeh, and E. Seto. 2004. Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A. Mol. Cell. Biol. 24:765-773.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 765-773
    • Lee, H.1    Rezai-Zadeh, N.2    Seto, E.3
  • 29
    • 0346655237 scopus 로고    scopus 로고
    • A phosphoprotein from the archaeon Suifolobus solfataricus with protein-serine kinase activity
    • Lower, B. H., M. B. Potters, and P. J. Kennelly. 2004. A phosphoprotein from the archaeon Suifolobus solfataricus with protein-serine kinase activity. J. Bacteriol. 186:463-472.
    • (2004) J. Bacteriol. , vol.186 , pp. 463-472
    • Lower, B.H.1    Potters, M.B.2    Kennelly, P.J.3
  • 30
    • 0037515708 scopus 로고    scopus 로고
    • Open reading frame sso2387 from the archaeon Sulfolobus solfataricus encodes a polypeptide with protein-serine kinase activity
    • Lower, B. H., and P. J. Kennelly. 2003. Open reading frame sso2387 from the archaeon Sulfolobus solfataricus encodes a polypeptide with protein-serine kinase activity. J. Bacteriol. 185:3436-3445.
    • (2003) J. Bacteriol. , vol.185 , pp. 3436-3445
    • Lower, B.H.1    Kennelly, P.J.2
  • 32
    • 0034710280 scopus 로고    scopus 로고
    • Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: Identification of the amino acid residues essential for catalysis
    • Mio, T., T. Yamada-Okabe, M. Arisawa, and H. Yamada-Okabe. 2000. Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for catalysis. Biochim. Biophys. Acta 1492:369-376.
    • (2000) Biochim. Biophys. Acta , vol.1492 , pp. 369-376
    • Mio, T.1    Yamada-Okabe, T.2    Arisawa, M.3    Yamada-Okabe, H.4
  • 33
    • 0035584063 scopus 로고    scopus 로고
    • Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase
    • Naught, L. E., and P. A. Tipton. 2001. Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase. Arch. Biochem. Biophys. 396:111-118.
    • (2001) Arch. Biochem. Biophys. , vol.396 , pp. 111-118
    • Naught, L.E.1    Tipton, P.A.2
  • 34
    • 0042974219 scopus 로고    scopus 로고
    • Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase
    • Naught, L. E., C. Regni, L. J. Beamer, and P. A. Tipton. 2003. Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/ phosphoglucomutase. Biochemistry 42:9946-9951.
    • (2003) Biochemistry , vol.42 , pp. 9946-9951
    • Naught, L.E.1    Regni, C.2    Beamer, L.J.3    Tipton, P.A.4
  • 36
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • Posewitz, M. C., and P. Tempst. 1999. Immobilized gallium(III) affinity chromatography of phosphopeptides. Anal. Biochem. 71:2883-2892.
    • (1999) Anal. Biochem. , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 38
    • 1642452663 scopus 로고    scopus 로고
    • Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa
    • Regni, C., L. Naught, P. A. Tipton, and L. J. Beamer. 2004. Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa. Structure 12:55-63.
    • (2004) Structure , vol.12 , pp. 55-63
    • Regni, C.1    Naught, L.2    Tipton, P.A.3    Beamer, L.J.4
  • 39
    • 0036174748 scopus 로고    scopus 로고
    • Crystal structure of PMM/PGM: An enzyme in the biosynthetic pathway of P. aeruginosa virulence factors
    • Regni, C., P. A. Tipton, and L. J. Beamer. 2002. Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors. Structure 10:269-279.
    • (2002) Structure , vol.10 , pp. 269-279
    • Regni, C.1    Tipton, P.A.2    Beamer, L.J.3
  • 40
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali, A., and T. L. Blundell. 1993. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 41
    • 3342884205 scopus 로고    scopus 로고
    • Evolutionary trace analysis of the α-D-phosphohexomutase family
    • Shackelford, G. S., C. A. Regni, and L. A. Beamer. 2004. Evolutionary trace analysis of the α-D-phosphohexomutase family. Protein Sci. 13:2130-2138.
    • (2004) Protein Sci. , vol.13 , pp. 2130-2138
    • Shackelford, G.S.1    Regni, C.A.2    Beamer, L.A.3
  • 43
    • 0030013766 scopus 로고    scopus 로고
    • BCM search launcher - An integrated interface to molecular biology data base search and analysis services available on the World Wide Web
    • Smith, R. F., B. A. Wiese, M. K. Wojzynski, D. B. Davidson, and K. C. Worley. 1996. BCM search launcher - an integrated interface to molecular biology data base search and analysis services available on the World Wide Web. Genome Res. 6:454-462.
    • (1996) Genome Res. , vol.6 , pp. 454-462
    • Smith, R.F.1    Wiese, B.A.2    Wojzynski, M.K.3    Davidson, D.B.4    Worley, K.C.5
  • 44
    • 0031594123 scopus 로고    scopus 로고
    • Archaeal phosphoproteins. Identification of a hexosephosphate mutase and the α-subunit of succinyl-CoA synthetase in the extreme acidothermophile Sulfolobus solfataricus
    • Solow, B., K. M. Bischoff, M. J. Zylka, and P. J. Kennelly. 1998. Archaeal phosphoproteins. Identification of a hexosephosphate mutase and the α-subunit of succinyl-CoA synthetase in the extreme acidothermophile Sulfolobus solfataricus. Protein Sci. 7:105-111.
    • (1998) Protein Sci. , vol.7 , pp. 105-111
    • Solow, B.1    Bischoff, K.M.2    Zylka, M.J.3    Kennelly, P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.