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Volumn 165, Issue 7-8, 2011, Pages 1661-1673

Endo-inulinase stabilization by pyridoxal phosphate modification: A kinetics, thermodynamics, and simulation approach

Author keywords

Chemical modification; Endo inulinase; Molecular dynamics; Pyridoxal 5 phosphate; Thermostability

Indexed keywords

ENDO-INULINASE; ENZYME MODIFICATION; HALF LIVES; INACTIVATION PROCESS; INITIAL RATE; INTRAMOLECULAR INTERACTIONS; INULINASE; LYSINE RESIDUES; MODIFIED ENZYMES; MOLECULAR DOCKING; MOLECULAR DYNAMICS SIMULATIONS; PYRIDOXAL PHOSPHATES; RELATIVE ACTIVITIES; SIMULATION APPROACH; STRUCTURAL STABILITIES; SUBSTRATE SPECIFICITY; TEMPERATURE DEPENDENT; THERMODYNAMIC PARAMETER; THERMOSTABILITY; THERMOSTABILIZATION;

EID: 81955160685     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-011-9385-x     Document Type: Article
Times cited : (13)

References (36)
  • 1
    • 0001973467 scopus 로고    scopus 로고
    • H.J. Gilbert G.B. Davies S.B. Henrissat (eds). The Royal Society of Chemistry London
    • Coutinho, P. M., & Henrissat, B. (1999). In H. J. Gilbert, G. B. Davies, & S. B. Henrissat (Eds.), Recent advances in carbohydrate bioengineering (pp. 3-12). London: The Royal Society of Chemistry.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 5
    • 33646064714 scopus 로고    scopus 로고
    • 10.1016/j.jfoodeng.2005.05.052 1:CAS:528:DC%2BD28XnsVanur0%3D
    • PK Gill RK Manhas P Singh 2006 Journal of Food Engineering 76 369 375 10.1016/j.jfoodeng.2005.05.052 1:CAS:528:DC%2BD28XnsVanur0%3D
    • (2006) Journal of Food Engineering , vol.76 , pp. 369-375
    • Gill, P.K.1    Manhas, R.K.2    Singh, P.3
  • 14
    • 0031869580 scopus 로고    scopus 로고
    • Structural characteristics of brain glutamate decarboxylase in relation to its interaction and activation
    • DOI 10.1006/abbi.1997.0457
    • CH Chen SJ Wu DL Martin 1998 Archives of Biochemistry and Biophysics 349 175 182 10.1006/abbi.1997.0457 1:CAS:528:DyaK1cXjtVKnsw%3D%3D (Pubitemid 28368404)
    • (1998) Archives of Biochemistry and Biophysics , vol.349 , Issue.1 , pp. 175-182
    • Chen, C.-H.1    Wu, S.J.2    Martin, D.L.3
  • 15
    • 0344224216 scopus 로고    scopus 로고
    • Inactivation of betaine aldehyde dehydrogenase from amaranth leaves by pyridoxal 5'-phosphate
    • DOI 10.1016/S0168-9452(99)00021-7, PII S0168945299000217
    • M Vojtěchová R Rodríguez-Sotres RA Muñoz-Clares 1999 Plant Science 143 9 17 10.1016/S0168-9452(99)00021-7 (Pubitemid 29275284)
    • (1999) Plant Science , vol.143 , Issue.1 , pp. 9-17
    • Vojtechova, M.1    Rodriguez-Sotres, R.2    Munoz-Clares, R.A.3
  • 18
    • 0032053797 scopus 로고    scopus 로고
    • Chemical modification of the dihydropyridines binding sites by lysine reagent, pyridoxal 5'-phosphate
    • DOI 10.1016/S0197-0186(97)00100-9, PII S0197018697001009
    • B Costa L Giusti C Martini A Lucacchini 1998 Neurochemistry International 32 361 364 10.1016/S0197-0186(97)00100-9 1:CAS:528:DyaK1cXivV2hsbs%3D (Pubitemid 28174988)
    • (1998) Neurochemistry International , vol.32 , Issue.4 , pp. 361-364
    • Costa, B.1    Giusti, L.2    Martini, C.3    Lucacchini, A.4
  • 19
    • 2642543205 scopus 로고    scopus 로고
    • Involvement of lysine-193 of the conserved "K-T-G-G" motif in the catalysis of maize starch synthase IIa
    • DOI 10.1016/j.abb.2004.01.010, PII S000398610400027X
    • Z Gao P Keeling R Shibles 2004 Archives of Biochemistry and Biophysics 427 1 7 10.1016/j.abb.2004.01.010 1:CAS:528:DC%2BD2cXkslSjsr8%3D (Pubitemid 38725908)
    • (2004) Archives of Biochemistry and Biophysics , vol.427 , Issue.1 , pp. 1-7
    • Gao, Z.1    Keeling, P.2    Shibles, R.3    Guan, H.4
  • 20
    • 33747333106 scopus 로고
    • 10.1021/ac60147a030 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
    • GL Miller 1959 Analytical Chemistry 31 426 428 10.1021/ac60147a030 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
    • (1959) Analytical Chemistry , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 21
    • 0031026784 scopus 로고    scopus 로고
    • Thermodynamic stability of annexin V E17G: Equilibrium parameters from an irreversible unfolding reaction
    • DOI 10.1021/bi962163z
    • T Vogl C Jatzke HJ Hinz J Benz R Huber 1997 Biochemistry 36 1657 1668 10.1021/bi962163z 1:CAS:528:DyaK2sXhslyltr4%3D (Pubitemid 27086261)
    • (1997) Biochemistry , vol.36 , Issue.7 , pp. 1657-1668
    • Vogl, T.1    Jatzke, C.2    Hinz, H.-J.3    Benz, J.4    Huber, R.5
  • 22
    • 0345593605 scopus 로고    scopus 로고
    • A comparison of the energetics of annexin I and annexin v
    • DOI 10.1006/jmbi.1999.2732
    • A Rosengarth J Rösgen HJ Hinz V Gerke 1999 Journal of Molecular Biology 288 1013 1025 10.1006/jmbi.1999.2732 1:CAS:528:DyaK1MXjtVersLc%3D (Pubitemid 29248649)
    • (1999) Journal of Molecular Biology , vol.288 , Issue.5 , pp. 1013-1025
    • Rosengarth, A.1    Rosgen, J.2    Hinz, H.-J.3    Gerke, V.4
  • 23
    • 43049136627 scopus 로고    scopus 로고
    • Characterization of three-phase partitioned exo-polygalacturonase from Aspergillus sojae with unique properties
    • DOI 10.1016/j.bej.2007.08.008, PII S1369703X07002975
    • N Dogan C Tari 2008 Biochemical Engineering Journal 39 43 50 10.1016/j.bej.2007.08.008 1:CAS:528:DC%2BD1cXivVOmsL8%3D (Pubitemid 351625635)
    • (2008) Biochemical Engineering Journal , vol.39 , Issue.1 , pp. 43-50
    • Dogan, N.1    Tari, C.2
  • 26
    • 0032919227 scopus 로고    scopus 로고
    • Partial and complete alteration of surface charges of carboxymethylcellulase by chemical modification: Thermostabilization in water-miscible organic solvent
    • DOI 10.1016/S0141-0229(98)00170-7, PII S0141022998001707
    • KS Siddiqui AM Shamsi MA Anwar MH Rashid MI Rajoka 1999 Enzyme and Microbial Technology 24 599 608 10.1016/S0141-0229(98)00170-7 1:CAS:528:DyaK1MXjtVOjt74%3D (Pubitemid 29221082)
    • (1999) Enzyme and Microbial Technology , vol.24 , Issue.8-9 , pp. 599-608
    • Siddiqui, K.S.1    Shemsi, A.M.2    Anwar, M.A.3    Rashid, M.H.4    Rajoka, M.I.5
  • 27
    • 0032005090 scopus 로고    scopus 로고
    • Thermodynamic and kinetic study of stability of the native and chemically modified β-glucosidases from Aspergillus niger
    • DOI 10.1016/S0032-9592(97)00036-8, PII S0032959297000368
    • MH Rashid KS Siddiqui 1998 Process Biochemistry 33 109 115 10.1016/S0032-9592(97)00036-8 1:CAS:528:DyaK1cXhs1Ort7o%3D (Pubitemid 28128472)
    • (1998) Process Biochemistry , vol.33 , Issue.2 , pp. 109-115
    • Rashid, M.H.1    Siddiqui, K.S.2
  • 28
    • 0015235670 scopus 로고
    • 10.1021/bi00802a002 1:CAS:528:DyaE38XktlaqsA%3D%3D
    • KD Schnackerz EA Noltmann 1971 Biochemistry 10 4837 4842 10.1021/bi00802a002 1:CAS:528:DyaE38XktlaqsA%3D%3D
    • (1971) Biochemistry , vol.10 , pp. 4837-4842
    • Schnackerz, K.D.1    Noltmann, E.A.2
  • 33
    • 0000388705 scopus 로고    scopus 로고
    • 10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H 1:CAS:528:DyaK2sXlvV2nu7g%3D
    • B Hess J Bekker HJC Berendsen JGEM Fraaije 1997 Journal Comparative Chemistry 18 1463 1472 10.1002/(SICI)1096-987X(199709)18:12<1463::AID- JCC4>3.0.CO;2-H 1:CAS:528:DyaK2sXlvV2nu7g%3D
    • (1997) Journal Comparative Chemistry , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, J.2    Berendsen, H.J.C.3    Jgem, F.4
  • 36
    • 0034017055 scopus 로고    scopus 로고
    • 10.1093/protein/13.3.179 1:CAS:528:DC%2BD3cXjtlKmur8%3D
    • S Kumar CJ Tsai R Nussinov 2000 Protein Engineering 13 179 191 10.1093/protein/13.3.179 1:CAS:528:DC%2BD3cXjtlKmur8%3D
    • (2000) Protein Engineering , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.