메뉴 건너뛰기




Volumn 40, Issue 4, 2007, Pages 849-858

New combined kinetic and thermodynamic approach to model glucose-6-phosphate dehydrogenase activity and stability

Author keywords

Glucose 6 phosphate dehydrogenase; Kinetic properties; Liquid liquid extraction; Reverse micelles; Saccharomyces cerevisiae; Thermodynamic parameters

Indexed keywords

CELLS; ENTHALPY; FREE ENERGY; MICELLES; PHOSPHOLIPIDS; YEAST;

EID: 33847350336     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.06.017     Document Type: Article
Times cited : (19)

References (50)
  • 1
    • 0037223885 scopus 로고    scopus 로고
    • Aromatic stacking as a determinant of the thermal stability of CYP119 from Sulfolobus solfataricus
    • Puchkaev A.V., Koo L.S., and Montellano P.R.O. Aromatic stacking as a determinant of the thermal stability of CYP119 from Sulfolobus solfataricus. Arch Biochem Biophys 409 (2003) 52-58
    • (2003) Arch Biochem Biophys , vol.409 , pp. 52-58
    • Puchkaev, A.V.1    Koo, L.S.2    Montellano, P.R.O.3
  • 2
    • 0003099824 scopus 로고
    • Bermeyer H.U., Bergmeyer J., and Grasl M. (Eds), Verlag Chemie, Weinheim, Germany
    • Bergmeyer H.U. In: Bermeyer H.U., Bergmeyer J., and Grasl M. (Eds). Methods of enzymatic analysis. 3rd ed. vol. 2 (1984), Verlag Chemie, Weinheim, Germany 222-223
    • (1984) Methods of enzymatic analysis. 3rd ed. , vol.2 , pp. 222-223
    • Bergmeyer, H.U.1
  • 3
    • 0035047785 scopus 로고    scopus 로고
    • Kinetic properties of human placental glucose-6-phosphate dehydrogenase
    • Özer N., Aksoy Y., and Ögüs H.I. Kinetic properties of human placental glucose-6-phosphate dehydrogenase. Int J Biochem Cell Biol 33 (2001) 221-226
    • (2001) Int J Biochem Cell Biol , vol.33 , pp. 221-226
    • Özer, N.1    Aksoy, Y.2    Ögüs, H.I.3
  • 4
    • 0036176074 scopus 로고    scopus 로고
    • Dog liver glucose-6-phosphate dehydrogenase: purification and kinetic properties
    • Özer N., Bilgi C., and Ögüs H.I. Dog liver glucose-6-phosphate dehydrogenase: purification and kinetic properties. Int J Biochem Cell Biol 34 (2002) 253-262
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 253-262
    • Özer, N.1    Bilgi, C.2    Ögüs, H.I.3
  • 5
    • 0037413453 scopus 로고    scopus 로고
    • Kinetic and thermodynamic aspects of glucose-6-phosphate dehydrogenase activity and synthesis
    • Rossi F.G., Ribeiro M.Z., Converti A., Vitolo M., and Pessoa Jr. A. Kinetic and thermodynamic aspects of glucose-6-phosphate dehydrogenase activity and synthesis. Enzyme Microbial Technol 32 (2003) 107-113
    • (2003) Enzyme Microbial Technol , vol.32 , pp. 107-113
    • Rossi, F.G.1    Ribeiro, M.Z.2    Converti, A.3    Vitolo, M.4    Pessoa Jr., A.5
  • 6
    • 33847367565 scopus 로고    scopus 로고
    • Purification of glucose-6-phosphate dehydrogenase from buffalo (Bubalus bubalis) erythrocytes and investigation of some kinetic properties
    • Çifitçi M., Beydemir S., Yilmaz H., and Altikat S. Purification of glucose-6-phosphate dehydrogenase from buffalo (Bubalus bubalis) erythrocytes and investigation of some kinetic properties. Prot Exp Purif 5 (2003) 159-168
    • (2003) Prot Exp Purif , vol.5 , pp. 159-168
    • Çifitçi, M.1    Beydemir, S.2    Yilmaz, H.3    Altikat, S.4
  • 8
    • 0028014366 scopus 로고
    • Studies on red cell glucose-6-phosphate dehydrogenase. Evaluation of reference values
    • Yüregir G.T., Aksoy K., Arpaci A., Unlukurt I., and Tuli A. Studies on red cell glucose-6-phosphate dehydrogenase. Evaluation of reference values. Ann Clin Biochem 31 (1994) 50-55
    • (1994) Ann Clin Biochem , vol.31 , pp. 50-55
    • Yüregir, G.T.1    Aksoy, K.2    Arpaci, A.3    Unlukurt, I.4    Tuli, A.5
  • 9
    • 2642569196 scopus 로고    scopus 로고
    • Optimized extraction by cetyl trimethyl ammonium bromide reversed micelles of xylose reductase and xylitol dehydrogenase from Candida guilliermondii homogenate
    • Cortez E.V., Pessoa Jr. A., Felipe M.G.A., Roberto I.C., and Vitolo M. Optimized extraction by cetyl trimethyl ammonium bromide reversed micelles of xylose reductase and xylitol dehydrogenase from Candida guilliermondii homogenate. J Chromatogr B 807 (2004) 47-54
    • (2004) J Chromatogr B , vol.807 , pp. 47-54
    • Cortez, E.V.1    Pessoa Jr., A.2    Felipe, M.G.A.3    Roberto, I.C.4    Vitolo, M.5
  • 10
    • 3042782586 scopus 로고    scopus 로고
    • Optimization of beta-xylosidase recovery by reversed micelles using response surface methodology
    • Hasmann F.A., Cortez D.V., Roberto I.C., and Pessoa Jr. A. Optimization of beta-xylosidase recovery by reversed micelles using response surface methodology. Electr J Biotechnol 6 (2003) 153-160
    • (2003) Electr J Biotechnol , vol.6 , pp. 153-160
    • Hasmann, F.A.1    Cortez, D.V.2    Roberto, I.C.3    Pessoa Jr., A.4
  • 11
    • 33847393304 scopus 로고    scopus 로고
    • Purification of glucose-6-phosphate dehydrogenase from cell free extracts using biocompatible reversed micellar system
    • Hasmann F.A., Cortez D.V., Assis N., Roberto I.C., and Pessoa Jr. A. Purification of glucose-6-phosphate dehydrogenase from cell free extracts using biocompatible reversed micellar system. Braz Arch Biotechnol Technol 47 5 (2004) 187-194
    • (2004) Braz Arch Biotechnol Technol , vol.47 , Issue.5 , pp. 187-194
    • Hasmann, F.A.1    Cortez, D.V.2    Assis, N.3    Roberto, I.C.4    Pessoa Jr., A.5
  • 13
    • 2642558648 scopus 로고    scopus 로고
    • Liquid-liquid extraction of xylitol dehydrogenase from Candida guilliermondii homogenate by reversed micelles
    • Cortez E.V., Pessoa Jr. A., Felipe M.G.A., Roberto I.C., and Vitolo M. Liquid-liquid extraction of xylitol dehydrogenase from Candida guilliermondii homogenate by reversed micelles. J Chromatogr B 807 (2004) 55-60
    • (2004) J Chromatogr B , vol.807 , pp. 55-60
    • Cortez, E.V.1    Pessoa Jr., A.2    Felipe, M.G.A.3    Roberto, I.C.4    Vitolo, M.5
  • 14
    • 0030996992 scopus 로고    scopus 로고
    • Separation of inulinase from Kluyveromyces marxianus using reversed micellar extraction
    • Pessoa Jr. A., and Vitolo M. Separation of inulinase from Kluyveromyces marxianus using reversed micellar extraction. Biotechnol Techniques 11 (1997) 421-422
    • (1997) Biotechnol Techniques , vol.11 , pp. 421-422
    • Pessoa Jr., A.1    Vitolo, M.2
  • 15
    • 0029636923 scopus 로고
    • Extraction of lysozyme and ribonuclease-a using reversed micelles: limits to protein solubilization
    • Lye G.J., Asenjo J.A., and Pyle D.L. Extraction of lysozyme and ribonuclease-a using reversed micelles: limits to protein solubilization. Biotechnol Bioeng 47 (1995) 509-519
    • (1995) Biotechnol Bioeng , vol.47 , pp. 509-519
    • Lye, G.J.1    Asenjo, J.A.2    Pyle, D.L.3
  • 16
    • 0035004530 scopus 로고    scopus 로고
    • Screening of variables in β-xylosidase recovery using cetyl trimethyl ammonium bromide reversed micelles
    • Hasmann F.A., Pessoa Jr. A., and Roberto I.C. Screening of variables in β-xylosidase recovery using cetyl trimethyl ammonium bromide reversed micelles. Appl Biochem Biotechnol 91-93 (2001) 719-728
    • (2001) Appl Biochem Biotechnol , vol.91-93 , pp. 719-728
    • Hasmann, F.A.1    Pessoa Jr., A.2    Roberto, I.C.3
  • 17
    • 0030144987 scopus 로고    scopus 로고
    • Liquid-liquid extraction of protein with reversed micelles
    • Pires M.J., Aires-Barros M.R., and Cabral J.M.S. Liquid-liquid extraction of protein with reversed micelles. Biotechnol Prog 12 (1996) 290-301
    • (1996) Biotechnol Prog , vol.12 , pp. 290-301
    • Pires, M.J.1    Aires-Barros, M.R.2    Cabral, J.M.S.3
  • 18
    • 0029951623 scopus 로고    scopus 로고
    • Stability of a Fusarium solani pisi recombinant cutinase in phosphatidylcholine reversed micelles
    • Pinto-Sousa A.M., Cabral J.M.S., and Aires-Barros M.R. Stability of a Fusarium solani pisi recombinant cutinase in phosphatidylcholine reversed micelles. Biotechnol Lett 18 (1996) 583-586
    • (1996) Biotechnol Lett , vol.18 , pp. 583-586
    • Pinto-Sousa, A.M.1    Cabral, J.M.S.2    Aires-Barros, M.R.3
  • 19
    • 0032998733 scopus 로고    scopus 로고
    • Effect of hexanol as a cosolvent on partitioning and mass transfer rate of protein extraction using reversed micelles of CB-modified lecithin
    • Sun Y., Bai S., Gu I., Tong X.-D., Ichikawa S., and Furusaki S. Effect of hexanol as a cosolvent on partitioning and mass transfer rate of protein extraction using reversed micelles of CB-modified lecithin. Biochem Eng J 3 (1999) 9-16
    • (1999) Biochem Eng J , vol.3 , pp. 9-16
    • Sun, Y.1    Bai, S.2    Gu, I.3    Tong, X.-D.4    Ichikawa, S.5    Furusaki, S.6
  • 21
    • 0014640345 scopus 로고
    • Protein structure and enzymatic activity. II. Purification and properties of a crystalline glucose-6-phosphate dehydrogenase from Candida utilis
    • Engel H.J., Domschke W., and Alberti G.F. Protein structure and enzymatic activity. II. Purification and properties of a crystalline glucose-6-phosphate dehydrogenase from Candida utilis. Biochem Biophys Acta 191 (1969) 509-516
    • (1969) Biochem Biophys Acta , vol.191 , pp. 509-516
    • Engel, H.J.1    Domschke, W.2    Alberti, G.F.3
  • 22
    • 0015527226 scopus 로고
    • Human erythrocyte glucose 6-phosphate dehydrogenase: electron microscope studies on structure and interconversion of tetramers, dimers and monomers
    • Wrigley N.G., Heather J.V., Bonsignore A., and De Flora A. Human erythrocyte glucose 6-phosphate dehydrogenase: electron microscope studies on structure and interconversion of tetramers, dimers and monomers. J Mol Biol 68 (1972) 483-499
    • (1972) J Mol Biol , vol.68 , pp. 483-499
    • Wrigley, N.G.1    Heather, J.V.2    Bonsignore, A.3    De Flora, A.4
  • 23
    • 0002342645 scopus 로고
    • Modern enzymology: problems and trends
    • Kurganov B.I., Kochetov S.N., and Tishkov V.I. (Eds), Nova Science, London, New York
    • Zaitseva E.A., Chukhrai E.S., and Poltorak O.M. Modern enzymology: problems and trends. In: Kurganov B.I., Kochetov S.N., and Tishkov V.I. (Eds). Modern enzymology: problems and trends (1995), Nova Science, London, New York 585
    • (1995) Modern enzymology: problems and trends , pp. 585
    • Zaitseva, E.A.1    Chukhrai, E.S.2    Poltorak, O.M.3
  • 24
    • 33847404319 scopus 로고    scopus 로고
    • Stabilization mechanism of glucose-6-phosphate dehydrogenase
    • Zaitseva E.A., Chukhrai E.S., and Poltorak O.M. Stabilization mechanism of glucose-6-phosphate dehydrogenase. Vestn Mosk Univ Khimiya 41 Suppl 6 (2000) 127-129
    • (2000) Vestn Mosk Univ Khimiya , vol.41 , Issue.SUPPL. 6 , pp. 127-129
    • Zaitseva, E.A.1    Chukhrai, E.S.2    Poltorak, O.M.3
  • 25
    • 0037457697 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase partitioning in two-phase aqueous mixed (nonionic/cationic) micellar systems
    • Rangel-Yagui C.O.R., Lam H., Kamei D.T., Wang D.I.C., Pessoa Jr. A., and Blankschtein D. Glucose-6-phosphate dehydrogenase partitioning in two-phase aqueous mixed (nonionic/cationic) micellar systems. Biotechnol Bioeng 82 (2003) 445-456
    • (2003) Biotechnol Bioeng , vol.82 , pp. 445-456
    • Rangel-Yagui, C.O.R.1    Lam, H.2    Kamei, D.T.3    Wang, D.I.C.4    Pessoa Jr., A.5    Blankschtein, D.6
  • 26
    • 33746928305 scopus 로고    scopus 로고
    • Optimization of glucose-6-phosphate dehydrogenase releasing from Candida guilliermondii by disruption with glass beads
    • Gurpilhares D.B., Hasmann F.A., Pessoa Jr. A., and Roberto I.C. Optimization of glucose-6-phosphate dehydrogenase releasing from Candida guilliermondii by disruption with glass beads. Enzyme Microbial Technol 39 (2006) 591-595
    • (2006) Enzyme Microbial Technol , vol.39 , pp. 591-595
    • Gurpilhares, D.B.1    Hasmann, F.A.2    Pessoa Jr., A.3    Roberto, I.C.4
  • 28
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H., and Burk D. The determination of enzyme dissociation constants. J Am Chem Soc 56 (1934) 658-666
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 29
    • 2142746284 scopus 로고
    • The activated complex in chemical reactions
    • Eyring H.J. The activated complex in chemical reactions. J Chem Phys 3 (1935) 107-115
    • (1935) J Chem Phys , vol.3 , pp. 107-115
    • Eyring, H.J.1
  • 30
    • 0034694819 scopus 로고    scopus 로고
    • Threalose delays the reversible but not the irreversible thermal denaturation of cutinase
    • Baptista R.P., Cabral J.M.S., and Melo E.P. Threalose delays the reversible but not the irreversible thermal denaturation of cutinase. Biotechnol Bioeng 70 (2000) 699-703
    • (2000) Biotechnol Bioeng , vol.70 , pp. 699-703
    • Baptista, R.P.1    Cabral, J.M.S.2    Melo, E.P.3
  • 32
    • 0029158748 scopus 로고
    • Kinetics and heat-inactivation mechanisms of amino acid oxidase
    • Montes F.J., Battaner E., Catalán J., and Galán M.A. Kinetics and heat-inactivation mechanisms of amino acid oxidase. Proc Biochem 30 (1995) 217-224
    • (1995) Proc Biochem , vol.30 , pp. 217-224
    • Montes, F.J.1    Battaner, E.2    Catalán, J.3    Galán, M.A.4
  • 33
    • 0032005090 scopus 로고    scopus 로고
    • Thermodynamic and kinetic study of stability of the native and chemically modified β-glucosidases from Aspergillus niger
    • Rashid M.H., and Siddiqui K.S. Thermodynamic and kinetic study of stability of the native and chemically modified β-glucosidases from Aspergillus niger. Proc Biochem 33 (1998) 109-115
    • (1998) Proc Biochem , vol.33 , pp. 109-115
    • Rashid, M.H.1    Siddiqui, K.S.2
  • 34
    • 0002643399 scopus 로고
    • Minimizing protein inactivation
    • Creighton T.E. (Ed), IRL Press, Oxford
    • Volkin D.B., and Klibanov A.M. Minimizing protein inactivation. In: Creighton T.E. (Ed). Protein function: a practical approach (1989), IRL Press, Oxford 213-218
    • (1989) Protein function: a practical approach , pp. 213-218
    • Volkin, D.B.1    Klibanov, A.M.2
  • 37
    • 0037734154 scopus 로고    scopus 로고
    • Purification of glucose-6-phosphate dehydrogenase from baker's yeast in aqueous two-phase system with free triazine dyes as affinity ligands
    • Xu Y., Vitolo M., Albuquerque C.N., and Pessoa Jr. A. Purification of glucose-6-phosphate dehydrogenase from baker's yeast in aqueous two-phase system with free triazine dyes as affinity ligands. Appl Biochem Biotechnol 105-108 (2003) 853-865
    • (2003) Appl Biochem Biotechnol , vol.105-108 , pp. 853-865
    • Xu, Y.1    Vitolo, M.2    Albuquerque, C.N.3    Pessoa Jr., A.4
  • 38
    • 0032810627 scopus 로고    scopus 로고
    • A rapid method for the purification of glucose-6-phosphate dehydrogenase from bovine lens
    • Ulusu N.N., Kus M.S., Acan N.L., and Tezcan E.F. A rapid method for the purification of glucose-6-phosphate dehydrogenase from bovine lens. Int J Biochem Cell Biol 31 (1999) 787-796
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 787-796
    • Ulusu, N.N.1    Kus, M.S.2    Acan, N.L.3    Tezcan, E.F.4
  • 39
    • 31744446733 scopus 로고    scopus 로고
    • Purification and kinetics of sheep kidney cortex glucose-6-phosphate dehydrogenase
    • Ulusu N.N., and Tandogan B. Purification and kinetics of sheep kidney cortex glucose-6-phosphate dehydrogenase. Comp Biochem Physiol B: Biochem Mol Biol 143 (2006) 249-255
    • (2006) Comp Biochem Physiol B: Biochem Mol Biol , vol.143 , pp. 249-255
    • Ulusu, N.N.1    Tandogan, B.2
  • 40
    • 0033525539 scopus 로고    scopus 로고
    • Purification, localisation and characterisation of glucose-6-phosphate dehydrogenase of Trypanosoma brucei
    • Heise N., and Opperdoes F.R. Purification, localisation and characterisation of glucose-6-phosphate dehydrogenase of Trypanosoma brucei. Mol Biochem Parassitol 99 (1999) 21-32
    • (1999) Mol Biochem Parassitol , vol.99 , pp. 21-32
    • Heise, N.1    Opperdoes, F.R.2
  • 41
    • 16544380791 scopus 로고    scopus 로고
    • Purification and characterization of glucose-6-phosphate dehydrogenase from rat small intestine
    • Danisan A., Ceyhan D., Ögüs I.H., and Özer N. Purification and characterization of glucose-6-phosphate dehydrogenase from rat small intestine. Protein J 23 (2004) 317-324
    • (2004) Protein J , vol.23 , pp. 317-324
    • Danisan, A.1    Ceyhan, D.2    Ögüs, I.H.3    Özer, N.4
  • 42
    • 32644452910 scopus 로고    scopus 로고
    • Purification and properties of glucose-6-phosphate dehydrogenase from Aspergillus aculeatus
    • Ibraheem O., Adewale I.O., and Afolayan A. Purification and properties of glucose-6-phosphate dehydrogenase from Aspergillus aculeatus. J Biochem Mol Biol 38 (2005) 584-590
    • (2005) J Biochem Mol Biol , vol.38 , pp. 584-590
    • Ibraheem, O.1    Adewale, I.O.2    Afolayan, A.3
  • 43
    • 0026544585 scopus 로고
    • Heat inactivation of lipase from psychrotrophic P. fluorescens P38; activation parameters and enzyme stability at low or ultra-high temperatures
    • Owusu R.K., Makhzoum A., and Knapp J.S. Heat inactivation of lipase from psychrotrophic P. fluorescens P38; activation parameters and enzyme stability at low or ultra-high temperatures. Food Chem 44 (1992) 261-268
    • (1992) Food Chem , vol.44 , pp. 261-268
    • Owusu, R.K.1    Makhzoum, A.2    Knapp, J.S.3
  • 44
    • 58149209748 scopus 로고
    • Glucose-6-phosphate dehydrogenase from the blood cells of two Antarctic teleosts: correlation with cold adaptation
    • Ciardiello M.A., Camardella L., and di Prisco G. Glucose-6-phosphate dehydrogenase from the blood cells of two Antarctic teleosts: correlation with cold adaptation. Biochim Biophys Acta 1250 (1995) 76-82
    • (1995) Biochim Biophys Acta , vol.1250 , pp. 76-82
    • Ciardiello, M.A.1    Camardella, L.2    di Prisco, G.3
  • 45
    • 0031406893 scopus 로고    scopus 로고
    • Enzyme in Antarctic fish glucose-6-phosphate dehydrogenase and glutamate dehydrogenase
    • Ciardiello M.A., Camardella L., Carratore V., and di Prisco G. Enzyme in Antarctic fish glucose-6-phosphate dehydrogenase and glutamate dehydrogenase. Comp Biochem Physiol 118A (1997) 1031-1036
    • (1997) Comp Biochem Physiol , vol.118 A , pp. 1031-1036
    • Ciardiello, M.A.1    Camardella, L.2    Carratore, V.3    di Prisco, G.4
  • 50
    • 0014461737 scopus 로고
    • Temperature of compensation: significance for virus inactivation
    • Barnes R., Vogel H., and Gorden I. Temperature of compensation: significance for virus inactivation. Proc Natl Acad Sci 62 (1969) 263-270
    • (1969) Proc Natl Acad Sci , vol.62 , pp. 263-270
    • Barnes, R.1    Vogel, H.2    Gorden, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.