메뉴 건너뛰기




Volumn 275, Issue 17, 2008, Pages 4317-4328

The role of group bulkiness in the catalytic activity of psychrophile cold-active protein tyrosine phosphatase

Author keywords

Catalytic efficiency; Cold active protein tyrosine phosphatase; Crystal structure; Group bulkiness; Psychrophile

Indexed keywords

ACID; AMINO ACID; COLD ACTIVE PROTEIN TYROSINE PHOSPHATASE; ENZYME; PROTEIN TYROSINE PHOSPHATASE;

EID: 49349112976     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06575.x     Document Type: Article
Times cited : (8)

References (44)
  • 10
    • 0034646605 scopus 로고    scopus 로고
    • Structural, kinetic, and calorimetric characterization of the cold-active phosphoglycerate kinase from the Antarctic Pseudomonas sp TACII18
    • Bentahir M, Feller G, Aittaleb M, Lamotte-Brasseur J, Himri T, Chessa JP Gerday C (2000) Structural, kinetic, and calorimetric characterization of the cold-active phosphoglycerate kinase from the Antarctic Pseudomonas sp TACII18. J Biol Chem 275, 11147 11153.
    • (2000) J Biol Chem , vol.275 , pp. 11147-11153
    • Bentahir, M.1    Feller, G.2    Aittaleb, M.3    Lamotte-Brasseur, J.4    Himri, T.5    Chessa, J.P.6    Gerday, C.7
  • 11
    • 0034736285 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility
    • Lonhienne T, Gerday C Feller G (2000) Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim Biophys Acta 1543, 1 10.
    • (2000) Biochim Biophys Acta , vol.1543 , pp. 1-10
    • Lonhienne, T.1    Gerday, C.2    Feller, G.3
  • 13
    • 0037302213 scopus 로고    scopus 로고
    • Catalytic efficiency and some structural properties of cold-active protein-tyrosine-phosphatase
    • Tsuruta H Aizono Y (2003) Catalytic efficiency and some structural properties of cold-active protein-tyrosine-phosphatase. J Biochem 133, 225 230.
    • (2003) J Biochem , vol.133 , pp. 225-230
    • Tsuruta, H.1    Aizono, Y.2
  • 14
    • 0032930543 scopus 로고    scopus 로고
    • Enzymatical properties of psychrophilic phosphatase I
    • Tsuruta H Aizono Y (1999) Enzymatical properties of psychrophilic phosphatase I. J Biochem 125, 690 695.
    • (1999) J Biochem , vol.125 , pp. 690-695
    • Tsuruta, H.1    Aizono, Y.2
  • 15
    • 0033962396 scopus 로고    scopus 로고
    • Cloning of phosphatase I gene from a psychrophile, Shewanella sp., and some properties of the recombinant enzyme
    • Tsuruta H Aizono Y (2000) Cloning of phosphatase I gene from a psychrophile, Shewanella sp., and some properties of the recombinant enzyme. J Biochem 127, 143 149.
    • (2000) J Biochem , vol.127 , pp. 143-149
    • Tsuruta, H.1    Aizono, Y.2
  • 16
    • 17044370905 scopus 로고    scopus 로고
    • Crystal structure of cold-active protein-tyrosine phosphatase from a psychrophile, Shewanella sp
    • Tsuruta H, Mikami B Aizono Y (2005) Crystal structure of cold-active protein-tyrosine phosphatase from a psychrophile, Shewanella sp. J Biochem 137, 69 77.
    • (2005) J Biochem , vol.137 , pp. 69-77
    • Tsuruta, H.1    Mikami, B.2    Aizono, Y.3
  • 17
    • 0030976053 scopus 로고    scopus 로고
    • Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: Role of two new phosphoprotein phosphatases PrpA and PrpB
    • Missiakas D Raina S (1997) Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: role of two new phosphoprotein phosphatases PrpA and PrpB. EMBO J 16, 1670 1685.
    • (1997) EMBO J , vol.16 , pp. 1670-1685
    • Missiakas, D.1    Raina, S.2
  • 18
    • 0024970557 scopus 로고
    • Discovery of a protein phosphatase activity encoded in the genome of bacteriophage λ. Probable identity with open reading frame 221
    • Cohen PT Cohen P (1989) Discovery of a protein phosphatase activity encoded in the genome of bacteriophage λ. Probable identity with open reading frame 221. Biochem J 260, 931 934.
    • (1989) Biochem J , vol.260 , pp. 931-934
    • Cohen, P.T.1    Cohen, P.2
  • 19
    • 0031857515 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a protein-serine/threonine phosphatase from the hyperthermophilic archaeon Pyrodictium abyssi TAG11
    • Mai B, Frey G, Swanson RV, Mathur EJ Stetter K (1998) Molecular cloning and functional expression of a protein-serine/threonine phosphatase from the hyperthermophilic archaeon Pyrodictium abyssi TAG11. J Bacteriol 180, 4030 4035.
    • (1998) J Bacteriol , vol.180 , pp. 4030-4035
    • Mai, B.1    Frey, G.2    Swanson, R.V.3    Mathur, E.J.4    Stetter, K.5
  • 21
    • 0034687659 scopus 로고    scopus 로고
    • Structure of the bacteriophage λ Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes
    • Voegtli WC, White DJ, Reiter NJ, Rusnak F Rosenzweig AC (2000) Structure of the bacteriophage λ Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes. Biochemistry 39, 15365 15374.
    • (2000) Biochemistry , vol.39 , pp. 15365-15374
    • Voegtli, W.C.1    White, D.J.2    Reiter, N.J.3    Rusnak, F.4    Rosenzweig, A.C.5
  • 23
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg J, Huang HB, Kwon YG, Greengard P, Narin AC Kuriyan J (1995) Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 376, 745 753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.B.2    Kwon, Y.G.3    Greengard, P.4    Narin, A.C.5    Kuriyan, J.6
  • 24
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • Egloff MP, Cohen PT, Reinemer P Barford D (1995) Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J Mol Biol 254, 942 959.
    • (1995) J Mol Biol , vol.254 , pp. 942-959
    • Egloff, M.P.1    Cohen, P.T.2    Reinemer, P.3    Barford, D.4
  • 25
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • Rusnak F Mertz P (2000) Calcineurin: form and function. Physiol Rev 80, 1483 1521.
    • (2000) Physiol Rev , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 26
    • 0030596529 scopus 로고    scopus 로고
    • Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures
    • Klabunde T, Sträter N, Fröhlich R, Witzel H Krebs B (1996) Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures. J Mol Biol 259, 737 748.
    • (1996) J Mol Biol , vol.259 , pp. 737-748
    • Klabunde, T.1    Sträter, N.2    Fröhlich, R.3    Witzel, H.4    Krebs, B.5
  • 27
    • 0032915156 scopus 로고    scopus 로고
    • X-ray structure of the Escherichia coli periplasmic 5′-nucleotidase containing a dimetal catalytic site
    • Knöfel T Sträter N (1999) X-ray structure of the Escherichia coli periplasmic 5′-nucleotidase containing a dimetal catalytic site. Nature Struct Biol 6, 448 453.
    • (1999) Nature Struct Biol , vol.6 , pp. 448-453
    • Knöfel, T.1    Sträter, N.2
  • 29
    • 0020170339 scopus 로고
    • Evidence for a spin-coupled binuclear iron unit at the active site of the purple acid phosphatase from beef spleen
    • Davis JC Averill BA (1982) Evidence for a spin-coupled binuclear iron unit at the active site of the purple acid phosphatase from beef spleen. Proc Natl Acad Sci USA 79, 4623 4627.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4623-4627
    • Davis, J.C.1    Averill, B.A.2
  • 33
    • 0035946945 scopus 로고    scopus 로고
    • Mechanism of hydrolysis of phosphate esters by the dimetal center of 5′-nucleotidase based on crystal structures
    • Knöfel T Sträter N (2001) Mechanism of hydrolysis of phosphate esters by the dimetal center of 5′-nucleotidase based on crystal structures. J Mol Biol 309, 239 254.
    • (2001) J Mol Biol , vol.309 , pp. 239-254
    • Knöfel, T.1    Sträter, N.2
  • 35
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia C (1975) Structural invariants in protein folding. Nature 254, 304 308.
    • (1975) Nature , vol.254 , pp. 304-308
    • Chothia, C.1
  • 36
    • 0025914068 scopus 로고
    • A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction
    • Ito W, Ishiguro H Kurosawa Y (1991) A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction. Gene 102, 67 70.
    • (1991) Gene , vol.102 , pp. 67-70
    • Ito, W.1    Ishiguro, H.2    Kurosawa, Y.3
  • 37
    • 0022321627 scopus 로고
    • Crystallization of macromolecules: General principles
    • McPherson A (1985) Crystallization of macromolecules: general principles. Methods Enzymol 114, 112 120.
    • (1985) Methods Enzymol , vol.114 , pp. 112-120
    • McPherson, A.1
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromol Crystallogr A 276, 307 326.
    • (1997) Macromol Crystallogr a , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 84943920736 scopus 로고
    • Phase annealing in SHELX-90: Direct methods for larger structures
    • Sheldrick GM (1990) Phase annealing in SHELX-90: direct methods for larger structures. Acta Crystallogr A 46, 467 473.
    • (1990) Acta Crystallogr a , vol.46 , pp. 467-473
    • Sheldrick, G.M.1
  • 40
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallog 26, 283 291.
    • (1993) J Appl Crystallog , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 41
    • 0028057108 scopus 로고
    • Raster3D Version 2.0. a program for photorealistic molecular graphics
    • Merritt EA Murphy ME (1994) Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr D 50, 869 873.
    • (1994) Acta Crystallogr D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2
  • 42
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf RM (1997) An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph Model 15, 132 134.
    • (1997) J Mol Graph Model , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 43
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallog 24, 946 950.
    • (1991) J Appl Crystallog , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.