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Volumn 55, Issue 3, 2007, Pages 179-184

Mg2+ decreases arrhenius energies of activation for high temperature catalysis of phosphatases in Thermoactinomyces vulgaris

Author keywords

Acid phosphatase; Alkaline phosphatase; Arrhenius energy of activation; Arrhenius plots; Energy of activation; High temperature catalysis; Phosphatases; Thermoactinomyces vulgaris, Thermophilic actinomycete; Thermophilic phosphatases

Indexed keywords

ACID; ALKALINE PHOSPHATASE; CATION; EDETIC ACID; MAGNESIUM; MAGNESIUM CHLORIDE; PHOSPHATASE; ACID PHOSPHATASE; BACTERIAL PROTEIN;

EID: 34547782802     PISSN: 03438651     EISSN: 14320991     Source Type: Journal    
DOI: 10.1007/s00284-006-0539-y     Document Type: Article
Times cited : (4)

References (34)
  • 2
    • 0022397686 scopus 로고
    • Arrhenius plots of acetylcholine esterase activity in mammalian erythrocytes and in Torpedo electric organ: Effect of solubilization by proteinases and by a phosphatidylinositol
    • Barton PL, Futerman AH, Silman I (1985) Arrhenius plots of acetylcholine esterase activity in mammalian erythrocytes and in Torpedo electric organ: Effect of solubilization by proteinases and by a phosphatidylinositol. Biochem J 231:237-240
    • (1985) Biochem J , vol.231 , pp. 237-240
    • Barton, P.L.1    Futerman, A.H.2    Silman, I.3
  • 3
    • 0037805084 scopus 로고    scopus 로고
    • 2+-dependence and inhibition of transformation by trifluoperazine and chlorpromazine in Thermoactinomyces vulgaris
    • 2+-dependence and inhibition of transformation by trifluoperazine and chlorpromazine in Thermoactinomyces vulgaris. Curr Microbiol 46:265-269
    • (2003) Curr Microbiol , vol.46 , pp. 265-269
    • Bhatnagar, K.1    Singh, V.P.2
  • 4
    • 3142673470 scopus 로고    scopus 로고
    • 2+ -dependence and inhibitiory effects of trifluoperazine on plasma membrane ATPase of Thermoactinomyces vulgaris
    • 2+ -dependence and inhibitory effects of trifluoperazine on plasma membrane ATPase of Thermoactinomyces vulgaris. Curr Microbiol 49:28-31
    • (2004) Curr Microbiol , vol.49 , pp. 28-31
    • Bhatnagar, K.1    Singh, V.P.2
  • 6
    • 0035908887 scopus 로고    scopus 로고
    • 2+ binding to alkaline phosphatase correlates with slow changes in protein lability
    • 2+ binding to alkaline phosphatase correlates with slow changes in protein lability. Biochemistry 40:11,219-11,226
    • (2001) Biochemistry , vol.40 , pp. 11
    • Dirnbach, E.1    Stell, D.G.2    Gafni, A.3
  • 8
    • 0019298598 scopus 로고
    • Steroid hormone-induced alterations in endometrium: Part III. Arrhenius plot analysis of mitochondrial oxytocinase
    • Ganguly YS, Ghosh JJ (1980) Steroid hormone-induced alterations in endometrium: Part III. Arrhenius plot analysis of mitochondrial oxytocinase. Indian J Biochem Biophys 17:366-369
    • (1980) Indian J Biochem Biophys , vol.17 , pp. 366-369
    • Ganguly, Y.S.1    Ghosh, J.J.2
  • 10
    • 0035197087 scopus 로고    scopus 로고
    • Thermostable conidial and mycelial alkaline phosphatases from the thermophilic fungus Scytalidium thermophilum
    • Guimaraes LH, Terenzi HF, Jorge JA, Polizeli ML (2001) Thermostable conidial and mycelial alkaline phosphatases from the thermophilic fungus Scytalidium thermophilum. J Ind Microbiol Biotechnol 27:265-270
    • (2001) J Indian Microbiol Biotechnol , vol.27 , pp. 265-270
    • Guimaraes, L.H.1    Terenzi, H.F.2    Jorge, J.A.3    Polizeli, M.L.4
  • 11
    • 0008882853 scopus 로고
    • Transformation in Thermoactinomyces vulgaris
    • Hopwood DA, Wright HM (1972) Transformation in Thermoactinomyces vulgaris. J Gen Microbiol 71:383-398
    • (1972) J Gen Microbiol , vol.71 , pp. 383-398
    • Hopwood, D.A.1    Wright, H.M.2
  • 12
    • 0015221798 scopus 로고
    • Purification and properties of an alkaline phosphatase of Bacillus licheniformis
    • Hulett-Cowling FM, Campbell LL (1971). Purification and properties of an alkaline phosphatase of Bacillus licheniformis. Biochemistry 10:1364-1371
    • (1971) Biochemistry , vol.10 , pp. 1364-1371
    • Hulett-Cowling, F.M.1    Campbell, L.L.2
  • 13
    • 0037023912 scopus 로고    scopus 로고
    • Kinetic constant determinations of alkaline protease from Bacillus mojavensis using response surface methodology
    • Khalil BQ, Saxena RK, Gupta R (2002) Kinetic constant determinations of alkaline protease from Bacillus mojavensis using response surface methodology. Biotech Bioeng 78:289-295
    • (2002) Biotech Bioeng , vol.78 , pp. 289-295
    • Khalil, B.Q.1    Saxena, R.K.2    Gupta, R.3
  • 14
    • 0032844705 scopus 로고    scopus 로고
    • Community size and metabolic rates of psychrophilic sulfate-reducing bacteria in arctic marine sediments
    • Knoblauch C, Jorgesen BB, Harder J (1999) Community size and metabolic rates of psychrophilic sulfate-reducing bacteria in arctic marine sediments. Appl Environ Microbiol 65:4230-4233
    • (1999) Appl Environ Microbiol , vol.65 , pp. 4230-4233
    • Knoblauch, C.1    Jorgesen, B.B.2    Harder, J.3
  • 15
    • 0024844766 scopus 로고
    • Thermophilic organisms as source of thermostable enzymes
    • Kristjansson J (1989) Thermophilic organisms as source of thermostable enzymes. Trends Biotechnol 7:349-353
    • (1989) Trends Biotechnol , vol.7 , pp. 349-353
    • Kristjansson, J.1
  • 18
    • 0028812131 scopus 로고
    • The effect of low temperatures on enzyme activity
    • More N, Daniel RM, Petach HH (1995) The effect of low temperatures on enzyme activity. Biochem J 305:17-20
    • (1995) Biochem J , vol.305 , pp. 17-20
    • More, N.1    Daniel, R.M.2    Petach, H.H.3
  • 19
    • 0020084818 scopus 로고
    • Thermostabilty and turnover of phosphatases in an obligate thermophile-Thermoactinomyces vulgaris
    • Singh VP, Sinha U (1982) Thermostability and turnover of phosphatases in an obligate thermophile-Thermoactinomyces vulgaris. Indian J Exp Biol 20:26-30
    • (1982) Indian J Exp Biol , vol.20 , pp. 26-30
    • Singh, V.P.1    Sinha, U.2
  • 20
    • 0019129494 scopus 로고
    • Phosphate utilization and constitutive synthesis of phosphatases in Thermoactinomyces vulgaris Tsiklinsky
    • Sinha U, Singh VP (1980) Phosphate utilization and constitutive synthesis of phosphatases in Thermoactinomyces vulgaris Tsilinsky. Biochem J 190:457-460
    • (1980) Biochem J , vol.190 , pp. 457-460
    • Sinha, U.1    Singh, V.P.2
  • 21
    • 0542442933 scopus 로고
    • Regulation of phosphatases in Thermoactinomyces vulgaris
    • Sinha U, Singh VP (1981) Regulation of phosphatases in Thermoactinomyces vulgaris. Perspect Cytol Genet 3:107-111
    • (1981) Perspect Cytol Genet , vol.3 , pp. 107-111
    • Sinha, U.1    Singh, V.P.2
  • 22
    • 34547207701 scopus 로고
    • Cation-dependent activity and stability of phosphatases in Thermoactinomyces vulgaris
    • Sinha U, Singh VP, Srivastava S (1981) Cation-dependent activity and stability of phosphatases in Thermoactinomyces vulgaris. Indian J Exp Biol 19:553-557
    • (1981) Indian J Exp Biol , vol.19 , pp. 553-557
    • Sinha, U.1    Singh, V.P.2    Srivastava, S.3
  • 23
    • 0017387403 scopus 로고
    • Repressible alkaline phosphatase from Thermus aquaticus: Associated phosphodiesterase activity
    • Smile DH, Donohou M, Yeh M, Kenkel T, Trela JM (1977) Repressible alkaline phosphatase from Thermus aquaticus: associated phosphodiesterase activity. J Biol Chem 252:3399-3401
    • (1977) J Biol Chem , vol.252 , pp. 3399-3401
    • Smile, D.H.1    Donohou, M.2    Yeh, M.3    Kenkel, T.4    Trela, J.M.5
  • 24
    • 0023644488 scopus 로고
    • 2+ in rat hepatoma cells, accumulation of apoenzyme
    • 2+ in rat hepatoma cells, accumulation of apoenzyme. J Biol Chem 262:1535-1541
    • (1987) J Biol Chem , vol.262 , pp. 1535-1541
    • Sorimachi, K.1
  • 25
    • 0016905007 scopus 로고
    • Anaplerotic enzymes of acetate and pyruvate metabolism: Distinctive characteristics in Bacillus stearothermophilus
    • Birkhauser Verlag Basel
    • Sunderam TK, Libor S, Chell HM (1976) Anaplerotic enzymes of acetate and pyruvate metabolism: distinctive characteristics in Bacillus stearothermophilus. Pages 263-275 in H Zuber (ed) Enzymes and proteins from thermophilic microorganisms. Birkhauser Verlag, Basel
    • (1976) Enzymes and Proteins from Thermophilic Microorganisms , pp. 263-275
    • Sunderam, T.K.1    Libor, S.2    Chell, H.M.3    Zuber, H.4
  • 26
    • 0035970089 scopus 로고    scopus 로고
    • Convex Arrhenius plots and their interpretation
    • Truhlar DG, Kohen A (2001) Convex Arrhenius plots and their interpretation. Proc Natl Acad Sci USA 98:848-851
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 848-851
    • Truhlar, D.G.1    Kohen, A.2
  • 27
    • 0025829920 scopus 로고
    • Cytotoxic effect of 1,3 bis(2-chloroethyl)-N-nitrosourea at elevated temperatures: Arrhenius plot analysis and tumor response
    • Urano M, Majima H, Miller R, Kahn J (1991) Cytotoxic effect of 1,3 bis(2-chloroethyl)-N-nitrosourea at elevated temperatures: Arrhenius plot analysis and tumor response. Int J Hyperthermia 7:499-510
    • (1991) Int J Hyperthermia , vol.7 , pp. 499-510
    • Urano, M.1    Majima, H.2    Miller, R.3    Kahn, J.4
  • 28
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille C, Zeikus GJ (2001) Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1-43
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 30
    • 0016786229 scopus 로고
    • Differential effects of temperature on a membrane adenosine triphosphatase and associated phosphatase
    • Walker JA, Wheeler KP (1975) Differential effects of temperature on a membrane adenosine triphosphatase and associated phosphatase. Biochem J 151:439-442
    • (1975) Biochem J , vol.151 , pp. 439-442
    • Walker, J.A.1    Wheeler, K.P.2
  • 31
    • 0037184908 scopus 로고    scopus 로고
    • Altering the metal specificity of Escherichia coli alkaline phosphatase
    • Wojciechowski CL, Kantrowitz ER (2002) Altering the metal specificity of Escherichia coli alkaline phosphatase. J Biol Chem 277:50,476-50,481
    • (2002) J Biol Chem , vol.277 , pp. 50
    • Wojciechowski, C.L.1    Kantrowitz, E.R.2
  • 32
    • 0017127120 scopus 로고
    • Purification and characterization of a repressible alkaline phosphatase of Thermus aquaticus
    • Yeh M, Trela JM (1976) Purification and characterization of a repressible alkaline phosphatase of Thermus aquaticus. J Biol Chem 251:3134-3139
    • (1976) J Biol Chem , vol.251 , pp. 3134-3139
    • Yeh, M.1    Trela, J.M.2
  • 33
    • 17444434923 scopus 로고    scopus 로고
    • Role of conformational flexibility for enzymatic activity in NADH oxidase from Thermus thermophilus
    • Žoldak G, Šuták R, Antalîk M, Sprinzl M, Sedlák E (2003) Role of conformational flexibility for enzymatic activity in NADH oxidase from Thermus thermophilus. Eur J Biochem 270:4887-4897
    • (2003) Eur J Biochem , vol.270 , pp. 4887-4897
    • Žoldak, G.1    Šuták, R.2    Antalîk, M.3    Sprinzl, M.4    Sedlák, E.5


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