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Volumn 239, Issue 1, 1996, Pages 138-143

A site-directed mutagenesis study of Saccharomyces cerevisiae pyrophosphatase. Functional conservation of the active site of soluble inorganic pyrophosphatases

Author keywords

Genetic engineering; Pyrophosphatase; Yeast

Indexed keywords

INORGANIC PYROPHOSPHATASE;

EID: 0029941861     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0138u.x     Document Type: Article
Times cited : (54)

References (47)
  • 1
    • 0026563457 scopus 로고
    • Two pathways of pyrophosphate hydrolysis and synthesis by yeast inorganic pyrophosphatase
    • Baykov, A. & Shestakov, A. (1492) Two pathways of pyrophosphate hydrolysis and synthesis by yeast inorganic pyrophosphatase. Eur. J. Biochem. 206, 463 - 470.
    • (1492) Eur. J. Biochem. , vol.206 , pp. 463-470
    • Baykov, A.1    Shestakov, A.2
  • 2
    • 0025616098 scopus 로고
    • Kinetics and thermodynamics of catalysis by the inorganic pyrophosphatase of Escherichia Coli in both directions
    • Baykov, A. A., Shestakov, A. S., Kasho, V. N., Vener, A. V. & Ivanov, A. H. (1990) Kinetics and thermodynamics of catalysis by the inorganic pyrophosphatase of Escherichia Coli in both directions. Eur. J. Biochem. 194, 879 - 887.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 879-887
    • Baykov, A.A.1    Shestakov, A.S.2    Kasho, V.N.3    Vener, A.V.4    Ivanov, A.H.5
  • 3
    • 13344279410 scopus 로고
    • Dissociation of hexameric Escherichia coli inorganic pyrophosphatase into trimers on His136→Gln or His 140→Gln substitution and its effect on enzyme catalytic properties
    • Baykov, A. A., Dudarenkov, V. Y., Kasho, V. N., Käpylä, J., Salminen, T., Hyytiä, T., Cooperman, B., Goldman, A. & Lahti, R. (1995) Dissociation of hexameric Escherichia coli inorganic pyrophosphatase into trimers on His136→Gln or His 140→Gln substitution and its effect on enzyme catalytic properties, J. Biol. Chem. 270, 30804 - 30812.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30804-30812
    • Baykov, A.A.1    Dudarenkov, V.Y.2    Kasho, V.N.3    Käpylä, J.4    Salminen, T.5    Hyytiä, T.6    Cooperman, B.7    Goldman, A.8    Lahti, R.9
  • 5
    • 0019319062 scopus 로고
    • Identification of an arginine important for enzymatic activity within the covalent structure of yeast inorganic pyrohosphatase
    • Bond, M. W., Chiu, N. Y. & Cooperman, B. S. (1980) Identification of an arginine important for enzymatic activity within the covalent structure of yeast inorganic pyrohosphatase, Biochemistry 19, 94 - 102.
    • (1980) Biochemistry , vol.19 , pp. 94-102
    • Bond, M.W.1    Chiu, N.Y.2    Cooperman, B.S.3
  • 8
    • 0020345921 scopus 로고
    • The mechanism of action of yeast inorganic pyrophosphatase
    • Cooperman, B. S. (1982) The mechanism of action of yeast inorganic pyrophosphatase, Methods Enzymol. 87, 526 - 548.
    • (1982) Methods Enzymol. , vol.87 , pp. 526-548
    • Cooperman, B.S.1
  • 9
    • 0026628087 scopus 로고
    • Evolutionary conservation of the active site of soluble inorganic pyrophosphatase
    • Cooperman, B. S., Baykov, A. A. & Lahti, R. (1992) Evolutionary conservation of the active site of soluble inorganic pyrophosphatase, Trends Biol. Sci. 17, 262 - 266.
    • (1992) Trends Biol. Sci. , vol.17 , pp. 262-266
    • Cooperman, B.S.1    Baykov, A.A.2    Lahti, R.3
  • 10
    • 0000474852 scopus 로고
    • Biased codon usage: An exploration of its role in optimization of translation
    • (Reznikoff, W. & Gold, L., eds) Buttler-worths, London
    • De Boer, H. A. & Kastelein, R. A. (1986) Biased codon usage: an exploration of its role in optimization of translation, in Maximizing gene expression (Reznikoff, W. & Gold, L., eds) pp. 225 - 285, Buttler-worths, London.
    • (1986) Maximizing Gene Expression , pp. 225-285
    • De Boer, H.A.1    Kastelein, R.A.2
  • 11
    • 0022993780 scopus 로고
    • Glutamic acid-149 is important for enzymatic activity of yeast inorganic pyrophosphatase
    • Gonzalez, M. A. & Cooperman, B. S. (1986) Glutamic acid-149 is important for enzymatic activity of yeast inorganic pyrophosphatase, Biochemistry 25, 7179 - 7185.
    • (1986) Biochemistry , vol.25 , pp. 7179-7185
    • Gonzalez, M.A.1    Cooperman, B.S.2
  • 12
    • 0021772127 scopus 로고
    • Evidence that catalysis by yeast inorganic pyrophosphatase proceeds by direct phosphoryl transfer to water and not via phosphoryl enzymc intermediate
    • Gonzalez, M. A., Webb, M. R., Welsh, K. M. & Cooperman, B. S. (1984) Evidence that catalysis by yeast inorganic pyrophosphatase proceeds by direct phosphoryl transfer to water and not via phosphoryl enzymc intermediate, Biochemistry 23, 797 - 801.
    • (1984) Biochemistry , vol.23 , pp. 797-801
    • Gonzalez, M.A.1    Webb, M.R.2    Welsh, K.M.3    Cooperman, B.S.4
  • 13
    • 0019830545 scopus 로고
    • A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase
    • Heinonen, J. & Lahti, R. (1981) A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase, Anal. Biochem. 113, 313 - 317.
    • (1981) Anal. Biochem. , vol.113 , pp. 313-317
    • Heinonen, J.1    Lahti, R.2
  • 14
    • 0025313531 scopus 로고
    • Catalysis of the hydrolysis of phosphorylated pyridines by Mg(OH) - A possible model for enzymatic phosphoryl transfer
    • Herschlag, D. & Jencks, W. P. (1990) Catalysis of the hydrolysis of phosphorylated pyridines by Mg(OH) - a possible model for enzymatic phosphoryl transfer, Biochemistry 29, 5172 - 5179.
    • (1990) Biochemistry , vol.29 , pp. 5172-5179
    • Herschlag, D.1    Jencks, W.P.2
  • 15
  • 16
    • 77956910470 scopus 로고
    • Inorganic pyrophosphatase of Escherichia coli
    • Josse, J. & Wong, S. C. K. (1971) Inorganic pyrophosphatase of Escherichia coli, Enzymes 4, 499 - 527.
    • (1971) Enzymes , vol.4 , pp. 499-527
    • Josse, J.1    Wong, S.C.K.2
  • 18
    • 0029918891 scopus 로고    scopus 로고
    • Crystallographic identification of metal-binding sites in E. coli inorganic pyrophosphatase
    • Kankare, J., Salminen, T., Lahti, R., Cooperman, B. S., Baykov, A. A. & Goldman, A. (1996a) Crystallographic identification of metal-binding sites in E. coli inorganic pyrophosphatase, Biochemistry 35, 4670 - 4677.
    • (1996) Biochemistry , vol.35 , pp. 4670-4677
    • Kankare, J.1    Salminen, T.2    Lahti, R.3    Cooperman, B.S.4    Baykov, A.A.5    Goldman, A.6
  • 21
    • 0028948711 scopus 로고
    • Effect of D97E substitution on the kinetic and thermodynamic properties of Escherichia coli inorganic pyrophosphatase
    • Käpylä, J., Hyytiä, T., Lahti, R., Goldman, A., Baykov, A. A. & Cooperman, B. S. (1995) Effect of D97E substitution on the kinetic and thermodynamic properties of Escherichia coli inorganic pyrophosphatase, Biochemistry 34, 792 - 800.
    • (1995) Biochemistry , vol.34 , pp. 792-800
    • Käpylä, J.1    Hyytiä, T.2    Lahti, R.3    Goldman, A.4    Baykov, A.A.5    Cooperman, B.S.6
  • 22
    • 0018881742 scopus 로고
    • Enzyme-catalyzed phosphoryl transfer reactions
    • Knowles, J. R. (1980) Enzyme-catalyzed phosphoryl transfer reactions, Annu. Rev. Biochem. 49, 877 - 919.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 877-919
    • Knowles, J.R.1
  • 24
    • 0023775270 scopus 로고
    • Cloning, molecular characterization and chromosome localization of the inorganic pyrophosphatase (PPA) gene from S. cerevisiae
    • Kolakowski, L. F., Schlösser, M. & Cooperman, B. S. (1988) Cloning, molecular characterization and chromosome localization of the inorganic pyrophosphatase (PPA) gene from S. cerevisiae, Nucleic Acids Res. 16, 10441 - 10452.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10441-10452
    • Kolakowski, L.F.1    Schlösser, M.2    Cooperman, B.S.3
  • 25
    • 8944250113 scopus 로고
    • Functionally important lysine residue of inorganic pyrophosphatase from baker's yeast
    • Komissarov, A. A., Makarova, I. V., Sklyankina, V. A. & Avaeva, S. M. (1985) Functionally important lysine residue of inorganic pyrophosphatase from baker's yeast, Bioorg. Khim. 11, 1504 - 1509.
    • (1985) Bioorg. Khim. , vol.11 , pp. 1504-1509
    • Komissarov, A.A.1    Makarova, I.V.2    Sklyankina, V.A.3    Avaeva, S.M.4
  • 26
    • 0002677837 scopus 로고
    • On the metabolic significance of phosphorolytic and pyrophosphorolytic reactions
    • (Kasha, M. & Pullman. B., eds) Academic Press, New York.
    • Kornberg, A. (1962) On the metabolic significance of phosphorolytic and pyrophosphorolytic reactions, in Horizons in biochemistry (Kasha, M. & Pullman. B., eds) p. 251, Academic Press, New York.
    • (1962) Horizons in Biochemistry , pp. 251
    • Kornberg, A.1
  • 27
    • 0026244229 scopus 로고
    • MolScript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MolScript: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946 - 950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 28
    • 0000092367 scopus 로고
    • Crystalline inorganic pyrophosphatase isolated from baker's yeast
    • Kunitz, M. (1952) Crystalline inorganic pyrophosphatase isolated from baker's yeast. J. Gen. Physiol. 35, 423 - 450.
    • (1952) J. Gen. Physiol. , vol.35 , pp. 423-450
    • Kunitz, M.1
  • 29
    • 0023613953 scopus 로고
    • Rapid and efficient site-specfic mutagenesis without phenotypic selection
    • Kunkel, T. A., Roberts, J. D. & Zakour, R. A. (1987) Rapid and efficient site-specfic mutagenesis without phenotypic selection. Methods Enzymol. 154, 367 - 382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 30
    • 0000279670 scopus 로고
    • Structure of the active center of yeast inorganic pyrophosphatase on the basis of the results of an X-ray structural study
    • Kuranova, I. P., Terzyan, S. S., Voronova, A. A., Smirnova, E. A., Vainshtein, B. K., Höhne, W. & Hansen, G. (1983) Structure of the active center of yeast inorganic pyrophosphatase on the basis of the results of an X-ray structural study. Bioorg. Khim. 9, 1611 - 1619.
    • (1983) Bioorg. Khim. , vol.9 , pp. 1611-1619
    • Kuranova, I.P.1    Terzyan, S.S.2    Voronova, A.A.3    Smirnova, E.A.4    Vainshtein, B.K.5    Höhne, W.6    Hansen, G.7
  • 31
    • 0024233964 scopus 로고
    • Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12
    • Lahti, R., Pitkäranta, T., Valve, E., Ilta, I., Kukko-Kalske, E. & Heinonen, J. (1988) Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12, J. Bacteriol. 170, 5901 - 5907.
    • (1988) J. Bacteriol. , vol.170 , pp. 5901-5907
    • Lahti, R.1    Pitkäranta, T.2    Valve, E.3    Ilta, I.4    Kukko-Kalske, E.5    Heinonen, J.6
  • 32
    • 0025301144 scopus 로고
    • A site-directed mutagenesis study on Escherichia coli inorganic pyrophosphatase. Glutamic acid-98 and lysine-104 are important for structural integrity, whereas aspartic acids-97 and -102 are essential tor catalytic activity
    • Lahti, R., Pohjanoksa, K., Pitkäranta, T., Heikinheimo, P., Salminen, T., Meyer, P. & Heinonen, J. (1990a) A site-directed mutagenesis study on Escherichia coli inorganic pyrophosphatase. Glutamic acid-98 and lysine-104 are important for structural integrity, whereas aspartic acids-97 and -102 are essential tor catalytic activity, Biochemistry 29, 5761 - 5766.
    • (1990) Biochemistry , vol.29 , pp. 5761-5766
    • Lahti, R.1    Pohjanoksa, K.2    Pitkäranta, T.3    Heikinheimo, P.4    Salminen, T.5    Meyer, P.6    Heinonen, J.7
  • 34
    • 0025906827 scopus 로고
    • Genetic engineering of Escheriehia coli inorganic pyrophosphatase; Tyr55 and Tyr141 are important for the structural integrity
    • Lahti, R., Salminen, T., Latonen, S., Heikinheimo, P., Pohjanoksa, K. & Heinonen, J. (1991) Genetic engineering of Escheriehia coli inorganic pyrophosphatase; Tyr55 and Tyr141 are important for the structural integrity, Eur. J. Biochem. 198, 293 - 297.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 293-297
    • Lahti, R.1    Salminen, T.2    Latonen, S.3    Heikinheimo, P.4    Pohjanoksa, K.5    Heinonen, J.6
  • 35
    • 0025912666 scopus 로고
    • Yeast PPA2 gene encodes a mitochondrial inorganic pyrophosphatase that is essential for mitochondrial function
    • Lundin, M., Baltscheffsky, H. & Ronne, H. (1991) Yeast PPA2 gene encodes a mitochondrial inorganic pyrophosphatase that is essential for mitochondrial function. J. Biol. Chem. 266, 12168 - 12172.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12168-12172
    • Lundin, M.1    Baltscheffsky, H.2    Ronne, H.3
  • 36
    • 0020645043 scopus 로고
    • New M13-vectors for cloning
    • Messing, J. (1983) New M13-vectors for cloning, Methods Enzymol. 101, 20 - 78.
    • (1983) Methods Enzymol. , vol.101 , pp. 20-78
    • Messing, J.1
  • 37
    • 0026769965 scopus 로고
    • Tyrosine-89 is important for enzymatic activity of S. cerevisiae inorganic pyrophosphatase
    • Raznikov, A. V., Sklyankina, V. A. & Avaeva, S. M. (1992) Tyrosine-89 is important for enzymatic activity of S. cerevisiae inorganic pyrophosphatase, FEBS Lett. 308, 62-64.
    • (1992) FEBS Lett. , vol.308 , pp. 62-64
    • Raznikov, A.V.1    Sklyankina, V.A.2    Avaeva, S.M.3
  • 39
    • 0028957740 scopus 로고
    • Structure and function analysis of Escherichia coli inorganic pyrophosphatase: Is a hydroxide ion the key to catalysis?
    • Salminen, T., Käpylä, J., Heikinheimo, P., Goldman, A., Heinonen, J., Baykov, A. A., Cooperman, B. S. & Lahti, R. (1995) Structure and function analysis of Escherichia coli inorganic pyrophosphatase: is a hydroxide ion the key to catalysis? Biochemistry 34, 782 - 791.
    • (1995) Biochemistry , vol.34 , pp. 782-791
    • Salminen, T.1    Käpylä, J.2    Heikinheimo, P.3    Goldman, A.4    Heinonen, J.5    Baykov, A.A.6    Cooperman, B.S.7    Lahti, R.8
  • 40
    • 0029896617 scopus 로고    scopus 로고
    • An unusual route to thermostability disclosed by the comparison of Thermus thermophilus and Escherichia coli inorganic pyrophosphatases
    • in the press
    • Salminen, T., Teplyakov, A., Kankare, J., Cooperman, B. S., Lahti, R. & Goldman, A. (1996) An unusual route to thermostability disclosed by the comparison of Thermus thermophilus and Escherichia coli inorganic pyrophosphatases, Protein Sci., in the press.
    • (1996) Protein Sci.
    • Salminen, T.1    Teplyakov, A.2    Kankare, J.3    Cooperman, B.S.4    Lahti, R.5    Goldman, A.6
  • 42
    • 0019889782 scopus 로고
    • Thermodynamics, kinetics, and mechanism in yeast inorganic pyrophosphatase catalysis of inorganic pyrophosphate: Inorganic phosphate equilibration
    • Springs, B., Welsh, K. M. & Cooperman, B. S. (1981) Thermodynamics, kinetics, and mechanism in yeast inorganic pyrophosphatase catalysis of inorganic pyrophosphate: inorganic phosphate equilibration, Biochemistry 20, 6384 - 6391.
    • (1981) Biochemistry , vol.20 , pp. 6384-6391
    • Springs, B.1    Welsh, K.M.2    Cooperman, B.S.3
  • 45
  • 46
    • 0014940060 scopus 로고
    • Constitutive inorganic pyrophosphatase of Escherichia coli III. Molecular mass and physical properties of the enzyme and its subunits
    • Wong, S. C. K., Hall, D. C. & Josse, J. (1970) Constitutive inorganic pyrophosphatase of Escherichia coli III. Molecular mass and physical properties of the enzyme and its subunits. J. Biol. Chem. 245, 4335 - 4345.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4335-4345
    • Wong, S.C.K.1    Hall, D.C.2    Josse, J.3
  • 47
    • 0024967767 scopus 로고
    • Complementary DNA coding click beetle luciterases can elicit bioluminescence of different colors
    • Wood, K. V., Lam, Y. A., Seliger, H. H. & McElroy, W. D. (1989) Complementary DNA coding click beetle luciterases can elicit bioluminescence of different colors, Science 244, 700 - 702.
    • (1989) Science , vol.244 , pp. 700-702
    • Wood, K.V.1    Lam, Y.A.2    Seliger, H.H.3    McElroy, W.D.4


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