Structural transformations in the dynamics of Michaelis complex formation in lactate dehydrogenase

Biophysical Journal

Volumn 89, Issue 1, 2005, Pages

  McClendon, Sebastian ^a   Vu, Dung M ^b   Clinch, Keith ^c   Callender, Robert ^a   Dyer, R Brian ^b  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

^c CALLAGHAN INNOVATION   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

LACTATE DEHYDROGENASE; NICOTINAMIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; BINDING KINETICS; CHEMICAL STRUCTURE; COMPLEX FORMATION; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE; LASER; LASER INDUCED TEMPERATURE JUMP RELAXATION SPECTROSCOPY; MICHAELIS COMPLEX; MICHAELIS MENTEN KINETICS; MOLECULAR DYNAMICS; PROTEIN DYNAMICS; PROTEIN FUNCTION; SPECTROSCOPY; TEMPERATURE;

EID: 23244446437     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.064675     Document Type: Article

References (6)

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2. Burgner, J. W., and W. J. Ray. 1984. On the origin of lactate dehydrogenase induced rate effect. Biochemistry. 23:3636-3648.
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4. McClendon, S., N. Zhadin, and R. Callender. 2005. The approach to the Michaelis complex in lactate dehydrogenase: the substrate binding pathway. Biophys. J. In press.
5. Deng, H., J. Zheng, A. Clarke, J. J. Holbrook, R. Callender, and J. W. Burgner. 1994. Source of catalysis in the lactate dehydrogenase system. Ground state interactions in the enzyme-substrate complex. Biochemistry. 33:2297-2305.
6. Dunn, C. R., H. M. Wilks, D. J. Halsall, T. Atkinson, A. R. Clarke, H. Muirhead, and J. J. Holbrook. 1991. Design and synthesis of new enzymes based upon the lactate dehydrogenase framework. Philos. Trans. R. Soc. Lond. B. Biol Sci. 332: p. 177-185.