메뉴 건너뛰기




Volumn 86, Issue 3, 1998, Pages 324-331

The kinetics and mechanism of a reaction catalyzed by Bacillus stearothermphilus phosphoglucose isomerase

Author keywords

Fructose 6 phosphate; Glucose 6 phosphate; Kinetics; Mechanism; Phosphoglucose isomerase; Tetrameric enzyme

Indexed keywords

CATALYSIS; CHROMATOGRAPHIC ANALYSIS; ELECTROPHORESIS; ENZYMES; ISOMERIZATION; MOLECULAR WEIGHT; MOLECULES; PH; SUBSTRATES;

EID: 0031711001     PISSN: 0922338X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0922-338X(98)80138-4     Document Type: Article
Times cited : (7)

References (25)
  • 1
    • 0002340297 scopus 로고
    • Industrial application of adenosine 5′-triphosphate regeneration to synthesis of sugar phosphates
    • Mark, D., Bednarski, M. D., and Simon, E. S. (ed.). Am. Chem. Soc., Washington, DC
    • Nakajima, H., Kondo, H., Tsurutani, R., Dombou, M., Tomioka, I., and Tomita, K.: Industrial application of adenosine 5′-triphosphate regeneration to synthesis of sugar phosphates, p. 111-120. In Mark, D., Bednarski, M. D., and Simon, E. S. (ed.), Enzymes in carbohydrate synthesis. Am. Chem. Soc., Washington, DC (1991).
    • (1991) Enzymes in Carbohydrate Synthesis , pp. 111-120
    • Nakajima, H.1    Kondo, H.2    Tsurutani, R.3    Dombou, M.4    Tomioka, I.5    Tomita, K.6
  • 2
    • 0015240540 scopus 로고
    • Phosphoglucose isomerase from human erythrocyte
    • Tsuboi, K. K., Fukunaga, K., and Chervenka, C. H.: Phosphoglucose isomerase from human erythrocyte. J. Biol. Chem., 246, 7586-7594 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 7586-7594
    • Tsuboi, K.K.1    Fukunaga, K.2    Chervenka, C.H.3
  • 3
    • 0016169412 scopus 로고
    • A point mutation increasing the stability of human phosphoglucose isomerase
    • Tilley, B. E., Gracy, R. W., and Welch, S. G.: A point mutation increasing the stability of human phosphoglucose isomerase. J. Biol. Chem., 249, 4571-4579 (1974).
    • (1974) J. Biol. Chem. , vol.249 , pp. 4571-4579
    • Tilley, B.E.1    Gracy, R.W.2    Welch, S.G.3
  • 4
    • 0016192376 scopus 로고
    • Two isoenzymes of glucosephosphate isomerase from spinach leaves and their intracellular compartmentation
    • Schnarrenberger, C. and Oeser, A.: Two isoenzymes of glucosephosphate isomerase from spinach leaves and their intracellular compartmentation. Eur. J. Biochem., 45, 77-82 (1974).
    • (1974) Eur. J. Biochem. , vol.45 , pp. 77-82
    • Schnarrenberger, C.1    Oeser, A.2
  • 5
    • 0016170447 scopus 로고
    • Physical and chemical properties of yeast phosphoglucose isomerase isoenzymes
    • Kempe, T. D., Nakagawa, Y., and Noltmann, E. A.: Physical and chemical properties of yeast phosphoglucose isomerase isoenzymes. J. Biol. Chem., 249, 4617-4624 (1974).
    • (1974) J. Biol. Chem. , vol.249 , pp. 4617-4624
    • Kempe, T.D.1    Nakagawa, Y.2    Noltmann, E.A.3
  • 6
    • 0016430152 scopus 로고
    • The subunit structure of phosphoglucose isomerase from baker's yeast
    • Lowe, S. L. and Reithel, F. J.: The subunit structure of phosphoglucose isomerase from baker's yeast. J. Biol. Chem., 250, 94-99 (1975).
    • (1975) J. Biol. Chem. , vol.250 , pp. 94-99
    • Lowe, S.L.1    Reithel, F.J.2
  • 7
    • 0017227148 scopus 로고
    • Isolation of rabbit muscle glucosephosphate isomerase by a single-step substrate elution
    • Phillips, T. L., Talent, J. M., and Gracy, R. W.: Isolation of rabbit muscle glucosephosphate isomerase by a single-step substrate elution. Biochim. Biophys. Acta, 429, 624-628 (1976).
    • (1976) Biochim. Biophys. Acta , vol.429 , pp. 624-628
    • Phillips, T.L.1    Talent, J.M.2    Gracy, R.W.3
  • 8
    • 0019025915 scopus 로고
    • Purification and some properties of 6-phosphoglucose isomerase from Bacillus caldotenax
    • Takama, M. and Nosoh, Y.: Purification and some properties of 6-phosphoglucose isomerase from Bacillus caldotenax. J. Biochem., 87, 1821-1827 (1990).
    • (1990) J. Biochem. , vol.87 , pp. 1821-1827
    • Takama, M.1    Nosoh, Y.2
  • 9
    • 0015053163 scopus 로고
    • Purification and characterization of glucose 6-phosphate isomerase from Bacillus stearothermophilus
    • Muramatsu, N. and Nosoh, Y.: Purification and characterization of glucose 6-phosphate isomerase from Bacillus stearothermophilus. Arch. Biochem. Biophys., 144, 245-252 (1971).
    • (1971) Arch. Biochem. Biophys. , vol.144 , pp. 245-252
    • Muramatsu, N.1    Nosoh, Y.2
  • 10
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber, K. and Osborn, M.: The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem., 244, 4406-4412 (1969).
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 11
    • 25744461229 scopus 로고
    • The interaction of ribonuclease with purine and pyrimidine phosphates
    • Myer, Y. P. and Schellman, J. A.: The interaction of ribonuclease with purine and pyrimidine phosphates. Biochim. Biophys. Acta, 55, 361-373 (1962).
    • (1962) Biochim. Biophys. Acta , vol.55 , pp. 361-373
    • Myer, Y.P.1    Schellman, J.A.2
  • 12
    • 0002255136 scopus 로고
    • A colorimetric method for the determination of fructose in blood and urine
    • Roe, J. H.: A colorimetric method for the determination of fructose in blood and urine. J. Biol. Chem., 107, 15-22 (1934).
    • (1934) J. Biol. Chem. , vol.107 , pp. 15-22
    • Roe, J.H.1
  • 13
    • 84969001783 scopus 로고
    • The attractions of protein for small molecules and ions
    • Scatchard, G.: The attractions of protein for small molecules and ions. Ann. N. Y. Acad. Sci., 51, 660-672 (1949).
    • (1949) Ann. N. Y. Acad. Sci. , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 16
    • 0025166757 scopus 로고
    • Nucleotide regulation of Escherichia coli glycerol kinase
    • Pettigrew, D. W., Yu, G. J., and Lin, Y.: Nucleotide regulation of Escherichia coli glycerol kinase. Biochem., 29, 8620-8627 (1990).
    • (1990) Biochem. , vol.29 , pp. 8620-8627
    • Pettigrew, D.W.1    Yu, G.J.2    Lin, Y.3
  • 17
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J., and Changeux, J. P.: On the nature of allosteric transitions: a plausible model. J. Mol. Biol., 12, 88-118 (1965).
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 18
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland, D. E., Jr., Nemethy, G., and Filmer, D.: Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochem., 5, 365-385 (1966).
    • (1966) Biochem. , vol.5 , pp. 365-385
    • Koshland D.E., Jr.1    Nemethy, G.2    Filmer, D.3
  • 19
    • 0025996927 scopus 로고
    • Rates of reactions catalyzed by a dimeric enzyme. Effects of the reaction scheme and the kinetic parameters on co-operativity
    • Ishikawa, H., Ogino, H., and Oshida, H.: Rates of reactions catalyzed by a dimeric enzyme. Effects of the reaction scheme and the kinetic parameters on co-operativity. Biochem. J., 280, 131-137 (1991).
    • (1991) Biochem. J. , vol.280 , pp. 131-137
    • Ishikawa, H.1    Ogino, H.2    Oshida, H.3
  • 21
    • 0018178368 scopus 로고
    • Subunit structure of acetate kinase from Bacillus stearothermophilus as studied by hybridization and cross-linking experiments
    • Nakajima, H., Suzuki, K., and Imahori, K.: Subunit structure of acetate kinase from Bacillus stearothermophilus as studied by hybridization and cross-linking experiments. J. Biochem., 84, 1139-1146 (1978).
    • (1978) J. Biochem. , vol.84 , pp. 1139-1146
    • Nakajima, H.1    Suzuki, K.2    Imahori, K.3
  • 22
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme-catalyzed reactions
    • King, E. L. and Altman, C.: A schematic method of deriving the rate laws for enzyme-catalyzed reactions. J. Phys. Chem., 60, 1375-1378 (1956).
    • (1956) J. Phys. Chem. , vol.60 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 23
    • 0023989050 scopus 로고
    • The computerized derivation of rate equations for enzyme reactions on the basis of the pseudo-steady-state assumption and the rapid-equilibrium assumption
    • Ishikawa, H., Maeda, T., Hikita, H., and Miyatake, K.: The computerized derivation of rate equations for enzyme reactions on the basis of the pseudo-steady-state assumption and the rapid-equilibrium assumption. Biochem. J., 251, 175-181 (1988).
    • (1988) Biochem. J. , vol.251 , pp. 175-181
    • Ishikawa, H.1    Maeda, T.2    Hikita, H.3    Miyatake, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.