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Volumn 2, Issue 2, 2007, Pages 254-259

Involvement of alanine 103 residue in kinetic and physicochemical properties of glucose isomerases from Streptomyces species

Author keywords

Alanine 103; Glucose isomerase; Kinetic parameters; Site directed mutagenesis; Streptomyces

Indexed keywords

ALANINE; GLUCOSE; GLUCOSE ISOMERASE; GLYCINE;

EID: 34248348283     PISSN: 18606768     EISSN: None     Source Type: Journal    
DOI: 10.1002/biot.200600085     Document Type: Article
Times cited : (6)

References (25)
  • 1
    • 0029998291 scopus 로고    scopus 로고
    • Molecular and industrial aspects of glucose isomerase
    • Bhosale, S. H., Rao, M. B., Deshpande, V. V., Molecular and industrial aspects of glucose isomerase. Microbiol. Rev. 1996, 60, 280-300.
    • (1996) Microbiol. Rev , vol.60 , pp. 280-300
    • Bhosale, S.H.1    Rao, M.B.2    Deshpande, V.V.3
  • 2
    • 0025116430 scopus 로고
    • Catalytic mechanism of xylose (glucose) isomerase from Clostridium thermosulfurogenes
    • Lee, C., Bagdasarian, M., Meng, M., Zeikus, J. G., Catalytic mechanism of xylose (glucose) isomerase from Clostridium thermosulfurogenes. J. Biol. Chem. 1990, 265, 19082-19090.
    • (1990) J. Biol. Chem , vol.265 , pp. 19082-19090
    • Lee, C.1    Bagdasarian, M.2    Meng, M.3    Zeikus, J.G.4
  • 3
    • 0028225131 scopus 로고
    • X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis
    • Lavie, A., Allen, K. N., Petsko, G. A., Ringe, D., X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis. Biochemistry 1994, 33, 5469-5480.
    • (1994) Biochemistry , vol.33 , pp. 5469-5480
    • Lavie, A.1    Allen, K.N.2    Petsko, G.A.3    Ringe, D.4
  • 4
    • 0034334554 scopus 로고    scopus 로고
    • Asbóth, B., N ray-Szabó, G., Mechanism of action of D-xylose isomerase. Curr. Protein Pept. Sci. 2000, 1, 237-254.
    • Asbóth, B., N ray-Szabó, G., Mechanism of action of D-xylose isomerase. Curr. Protein Pept. Sci. 2000, 1, 237-254.
  • 5
    • 14744280673 scopus 로고
    • Enhancing the thermostability of glucose isomerase by protein engineering
    • Quax, W. J., Mrabet, N. T., Luiten, R. G. M., Schuurhuizen, P. W. et al., Enhancing the thermostability of glucose isomerase by protein engineering. Biotechnology 1991, 9, 738-742.
    • (1991) Biotechnology , vol.9 , pp. 738-742
    • Quax, W.J.1    Mrabet, N.T.2    Luiten, R.G.M.3    Schuurhuizen, P.W.4
  • 6
    • 0142215371 scopus 로고    scopus 로고
    • Directed evolution of Thermotoga neapolitana xylose isomerase: High activity on glucose at low temperature and low pH
    • Sriprapundh, D., Vieille, C., Zeikus, J. G., Directed evolution of Thermotoga neapolitana xylose isomerase: high activity on glucose at low temperature and low pH. Protein Eng. 2003, 16, 683-690.
    • (2003) Protein Eng , vol.16 , pp. 683-690
    • Sriprapundh, D.1    Vieille, C.2    Zeikus, J.G.3
  • 7
    • 0025765854 scopus 로고
    • Switching substrate preference of thermophilic xylose isomerase from D-xylose to D-glucose by redesigning the substrate binding pocket
    • Meng, M., Lee, C., Bagdasarian, M., Zeikus, J. G., Switching substrate preference of thermophilic xylose isomerase from D-xylose to D-glucose by redesigning the substrate binding pocket. Proc. Natl. Acad. Sci. USA 1991, 88, 4015-4019.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4015-4019
    • Meng, M.1    Lee, C.2    Bagdasarian, M.3    Zeikus, J.G.4
  • 8
    • 0034073503 scopus 로고    scopus 로고
    • Molecular determinants of xylose isomerase thermal stability and activity: Analysis of thermoenzymes by site-directed mutagenesis
    • Sriprapundh, D., Vieille, C., Zeikus, J. G., Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermoenzymes by site-directed mutagenesis. Protein Eng. 2000, 13, 259-265.
    • (2000) Protein Eng , vol.13 , pp. 259-265
    • Sriprapundh, D.1    Vieille, C.2    Zeikus, J.G.3
  • 9
    • 0031849115 scopus 로고    scopus 로고
    • A thermostable glucose isomerase having a relatively low optimum pH: Study of the activity and molecular cloning of the corresponding gene
    • Belghith, K. S., Bejar, S., A thermostable glucose isomerase having a relatively low optimum pH: study of the activity and molecular cloning of the corresponding gene. Biotechnol. Lett. 1998, 20, 553-556.
    • (1998) Biotechnol. Lett , vol.20 , pp. 553-556
    • Belghith, K.S.1    Bejar, S.2
  • 10
    • 4544294824 scopus 로고    scopus 로고
    • Glucose isomerase of the Streptomyces sp. SK strain: Purification, sequence analysis and implication of alanine 103 residue in the enzyme thermostability and acidotolerance
    • Borgi, M. A., Belghith, K. S, Ben Ali, M., Mezghani, M. et al., Glucose isomerase of the Streptomyces sp. SK strain: purification, sequence analysis and implication of alanine 103 residue in the enzyme thermostability and acidotolerance. Biochimie 2004, 86, 561-568.
    • (2004) Biochimie , vol.86 , pp. 561-568
    • Borgi, M.A.1    Belghith, K.S.2    Ben Ali, M.3    Mezghani, M.4
  • 11
    • 0028607332 scopus 로고
    • Construction of a new strain of Streptomyces violaceoniger, having strong, constitutive and stable glucose-isomerase activity
    • Bejar, S., Belghith, K., Gargouri, R., Ellouz, R., Construction of a new strain of Streptomyces violaceoniger, having strong, constitutive and stable glucose-isomerase activity. Biotechnol. Lett. 1994, 16, 1259-1264.
    • (1994) Biotechnol. Lett , vol.16 , pp. 1259-1264
    • Bejar, S.1    Belghith, K.2    Gargouri, R.3    Ellouz, R.4
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0346814641 scopus 로고
    • A new spectrophotometric method for the detection and determination of keto sugars and trioses
    • Dische, Z., Borenfreund, E., A new spectrophotometric method for the detection and determination of keto sugars and trioses. J. Biol. Chem. 1951, 192, 583-587.
    • (1951) J. Biol. Chem , vol.192 , pp. 583-587
    • Dische, Z.1    Borenfreund, E.2
  • 14
    • 0025912071 scopus 로고    scopus 로고
    • Smith, C. A., Rangarajan, M., Hartley, B. S., D-Xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. Biochem. J. 1991, 277, 255-261.
    • Smith, C. A., Rangarajan, M., Hartley, B. S., D-Xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. Biochem. J. 1991, 277, 255-261.
  • 15
    • 0025003703 scopus 로고
    • Comparative kinetics of D-xylose and D-glucose isomerase activities of the D-xylose isomerase from Thermus aquaticus HB8
    • Lehmacher, A., Bisswanger, H., Comparative kinetics of D-xylose and D-glucose isomerase activities of the D-xylose isomerase from Thermus aquaticus HB8. Biol. Chem. Hoppe-Seyler 1990, 371, 527-536.
    • (1990) Biol. Chem. Hoppe-Seyler , vol.371 , pp. 527-536
    • Lehmacher, A.1    Bisswanger, H.2
  • 16
    • 0026631355 scopus 로고
    • Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites
    • Jenkins, J., Janin, J., Rey, F., Chiadmi, M. et al., Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites. Biochemistry 1992, 31, 5449-5458.
    • (1992) Biochemistry , vol.31 , pp. 5449-5458
    • Jenkins, J.1    Janin, J.2    Rey, F.3    Chiadmi, M.4
  • 17
    • 0029143705 scopus 로고
    • Probing the role of active site residues in D-xylose isomerase
    • Whitaker, R. D., Cho, Y., Cha, J., Carrell, H. L. et al. Probing the role of active site residues in D-xylose isomerase. J. Biol. Chem. 1995, 270, 22895-22906.
    • (1995) J. Biol. Chem , vol.270 , pp. 22895-22906
    • Whitaker, R.D.1    Cho, Y.2    Cha, J.3    Carrell, H.L.4
  • 18
    • 2542578790 scopus 로고    scopus 로고
    • Xylose Isomerase in substrate and inhibitor Michaelis states: Atomic resolution studies of a metal-mediated hydride shift
    • Fenn, T. D., Ringe, D., Petsko, G. A., Xylose Isomerase in substrate and inhibitor Michaelis states: Atomic resolution studies of a metal-mediated hydride shift. Biochemistry 2004, 43, 6464-6474.
    • (2004) Biochemistry , vol.43 , pp. 6464-6474
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3
  • 19
    • 0034185559 scopus 로고    scopus 로고
    • Characterization of acid-stable glucose isomerase from Streptomyces sp. And development of single-step processes for high-fructose corn sweetener (HFCS) production
    • Kaneko, T., Takahashi, S., Saito, K., Characterization of acid-stable glucose isomerase from Streptomyces sp. And development of single-step processes for high-fructose corn sweetener (HFCS) production. Biosci. Biotechnol. Biochem. 2000, 64, 940-947.
    • (2000) Biosci. Biotechnol. Biochem , vol.64 , pp. 940-947
    • Kaneko, T.1    Takahashi, S.2    Saito, K.3
  • 20
    • 15944391627 scopus 로고    scopus 로고
    • Molecular cloning and expression of a thermostable xylose (glucose) isomerase gene. xylA, from Streptomyces chibaensis J-59
    • Joo, G. J., Shin, J. H., Heo, G. Y., Kim, Y. M. et al., Molecular cloning and expression of a thermostable xylose (glucose) isomerase gene. xylA, from Streptomyces chibaensis J-59. J. Microbiol. 2005, 43, 34-37.
    • (2005) J. Microbiol , vol.43 , pp. 34-37
    • Joo, G.J.1    Shin, J.H.2    Heo, G.Y.3    Kim, Y.M.4
  • 21
    • 0007914941 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable xylose (glucose) isomerase from Streptomyces chibaensis J-59
    • Joo, G. J., Shin, J. H., Heo, G. Y., Kwak Y. Y. et al., Purification and characterization of a thermostable xylose (glucose) isomerase from Streptomyces chibaensis J-59. Agric. Chem. Biotechnol. 2001, 44, 113-118.
    • (2001) Agric. Chem. Biotechnol , vol.44 , pp. 113-118
    • Joo, G.J.1    Shin, J.H.2    Heo, G.Y.3    Kwak, Y.Y.4
  • 22
    • 0034731512 scopus 로고    scopus 로고
    • Glucose isomerase: Insights into protein engineering for increased thermostability
    • Hartley, B. S., Hanlon, N., Robin, J. J., Rangarajan, M., Glucose isomerase: insights into protein engineering for increased thermostability. Biochim. Biophys. Acta 2000, 1543, 294-335.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 294-335
    • Hartley, B.S.1    Hanlon, N.2    Robin, J.J.3    Rangarajan, M.4
  • 23
    • 0005173568 scopus 로고
    • Purification and enzymatic properties of glucose isomerase from Streptomyces griseofuscus S-41
    • Kasumi, T., Hayashi, K., Tsumura, N., Purification and enzymatic properties of glucose isomerase from Streptomyces griseofuscus S-41. Agric. Biol. Chem. 1981, 45, 619-627.
    • (1981) Agric. Biol. Chem , vol.45 , pp. 619-627
    • Kasumi, T.1    Hayashi, K.2    Tsumura, N.3
  • 24
    • 34248363585 scopus 로고    scopus 로고
    • Pastinen, O., Thesis: Xylose isomerase from Streptomyces rubiginosus: stability, novel reactions and applications. Helsinki University of Technology, Helsinki, 2000.
    • Pastinen, O., Thesis: Xylose isomerase from Streptomyces rubiginosus: stability, novel reactions and applications. Helsinki University of Technology, Helsinki, 2000.
  • 25
    • 0028070761 scopus 로고
    • Perturbing the metal site in D-xylose isomerase, effect of mutations of His220 on enzyme stability
    • Cha, J. Cho, Y. Whitaker, R. D. Carrell, H. L. et al. Perturbing the metal site in D-xylose isomerase, effect of mutations of His220 on enzyme stability. J. Biol. Chem. 1994, 269, 2687-2694.
    • (1994) J. Biol. Chem , vol.269 , pp. 2687-2694
    • Cha, J.1    Cho, Y.2    Whitaker, R.D.3    Carrell, H.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.