Thermal inactivation and conformational lock studies on horse liver alcohol dehydrogenase: Structural mechanism

International Journal of Biological Macromolecules

Volumn 58, Issue , 2013, Pages 66-72

  Moosavi Movahedi, Faezeh ^a   Saboury, Ali A ^b   Alijanvand, H Hadi ^b   Bohlooli, M ^b   Salami, M ^b   Moosavi Movahedi, Ali A ^b  

^a ISLAMIC AZAD UNIVERSITY   (Iran)

^b UNIVERSITY OF TEHRAN   (Iran)

Author keywords

Aggregation mechanism; Conformational locks; Dynamic light scattering; Horse liver alcohol dehydrogenase; Thermal inactivation

Indexed keywords

ALCOHOL DEHYDROGENASE;

ARTICLE; BETA SHEET; BINDING SITE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME MECHANISM; FLUORESCENCE SPECTROSCOPY; HORSE; HYDRODYNAMICS; LIGHT SCATTERING; MATHEMATICAL COMPUTING; PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION; TEMPERATURE SENSITIVITY; THERMAL ANALYSIS; THERMAL STIMULATION; ULTRAVIOLET SPECTROSCOPY;

EQUIDAE;

EID: 84876695857     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2013.03.038     Document Type: Article

References (27)

1. Eklund H. Pharmacology Biochemistry and Behavior 1983, 18:73-81.
2. Nakamura K., Matsuda T. Current Organic Chemistry 2006, 10:1217-1246.
3. Ehrenberg A., Dalziel K. Acta Chemica Scandinavica 1958, 12:465-469.
4. Schneider G., Eklund H., Cedergren-Zeppezauer E., Zeppezauer M. The EMBO Journal 1983, 2:685-689.
5. Eklund H., Nordström B., Zeppezauer E., Soderlund G., Ohlsson I., Boiwe T., Soderberg B.O., Tapia O., Brändén C.I., Åkeson Å. Journal of Molecular Biology 1976, 102:27-59.
6. Eklund H., Nordström B., Zeppezauer E., Söderlund G., Ohlsson I., Boiwe T., Brändén C.I. FEBS Letters 1974, 44:200-204.
7. Brändén C.I., Eklund H., Nordström B., Boiwe T., Söderlund G., Zeppezauer E., Ohlsson I., Åkeson Å. Proceedings of the National Academy of Sciences 1973, 70:2439-2442.
8. Moosavi-Nejad S.Z., Moosavi-Movahedi A.A., Rezaei-Tavirani M., Floris G., Medda R. Journal of Biochemistry and Molecular Biology 2003, 36:167-172.
9. Berezovsky I.N., Trifonov E.N. Journal of Molecular Biology 2001, 307:1419-1426.
10. Poltorak O., Chukhray E., Torshin I., Atyaksheva L., Trevan M., Chaplin M. Journal of Molecular Catalysis B: Enzymatic 1999, 7:165-172.
11. Poltorak O., Chukhrai E., Kozlenkov A., Chaplin M., Trevan M. Journal of Molecular Catalysis B: Enzymatic 1999, 7:157-163.
12. Kurganov B.I., Kornilaev B.A., Chebotareva N.A., Malikov V.P., Orlov V.N., Lyubarev A.E., Livanova N.B. Biochemistry 2000, 39:13144-13152.
13. Hong J., Moosavi-Movahedi A.A., Ghourchian H., Amani M., Amanlou M., Chilaka F. Journal of Biochemistry and Molecular Biology 2005, 38:533-538.
14. Amani M., Moosavi-Movahedi A.A., Floris G., Longu S., Mura A., Moosavi-Nejad S.Z., Saboury A.A., Ahmad F. The Protein Journal 2005, 24:183-191.
15. Alaei L., Moosavi-Movahedi A.A., Hadi H., Saboury A.A., Amani M. Protein and Peptide Letters 2012, 19:852-858.
16. Z. Sattari, H. Pourfaizi, G. Dehghan, M. Amani, A.A. Moosavi-Movahedi, Structural Chemistry, , in press. doi:10.1007/s11224-11012-10136-11226.
17. Segel I.H. Effects of pH and temperature. Enzyme Kinetics 1995, 926-942. John Wiley & Sons press, New York, USA.
18. Haynes D.H., Staerk H. Journal of Membrane Biology 1974, 17:313-340.
19. Wallace A.C., Laskowski R.A., Thornton J.M. Protein Engineering 1995, 8:127-134.
20. Guex N., Peitsch M. Protein Data Bank Quaterly Newsletter 1996, 77.
21. Tsodikov O.V., Record M.T., Sergeev Y.V. Journal of Computational Chemistry 2002, 23:600-609.
22. Krissinel E., Henrick K. Journal of Molecular Biology 2007, 372:774-797.
23. Poltorak O., Chukhray E., Torshin I.Y. Biochemistry (Moscow) 1998, 63:303-311.
24. Eklund H., Brändén C. Journal of Biological Chemistry 1979, 254:3458-3461.
25. Siepen J.A., Radford S.E., Westhead D.R. Protein Science 2003, 12:2348-2359.
26. Nesloney C.L., Kelly J.W. Bioorganic and Medicinal Chemistry 1996, 4:739-766.
27. Richardson J.S., Richardson D.C. Proceedings of the National Academy of Sciences 2002, 99:2754-2759.