Intramolecular dynamics of structure of alkaline phosphatase from Escherichia coli

Vladimir M. Mazhul; Igor V. Mjakinnik; Alena N. Volkova

doi:10.1117/12.197414

2 January 1995 Intramolecular dynamics of structure of alkaline phosphatase from Escherichia coli

Vladimir M. Mazhul, Igor V. Mjakinnik, Alena N. Volkova

Proceedings Volume 2370, 5th International Conference on Laser Applications in Life Sciences; (1995) https://doi.org/10.1117/12.197414
Event: Laser Applications in Life Sciences: 5th International Conference, 1994, Minsk, Belarus

Abstract

The luminescent analysis with nano- and millisecond time resolution of intramolecular dynamics of Escherichia coli alkaline phosphatase was carried out. The effect of pH within the range 7.2 - 9.0, thermal inactivation, limited proteolysis by trypsin, binding of pyrophosphate, interconversion of enzyme and apoenzyme, the replacement of Zn²⁺ and Mg²⁺ in the active site by Cd²⁺ and Ni²⁺ on the spectral and kinetic parameters of luminescence was investigated. The essential changes of the level of nano- and millisecond dynamics of protein structure were found to correlate with the shift of enzymatic activity. The importance of small- and large-scale flexibility of protein structure for the act of enzymatic catalysis realization was shown.

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Vladimir M. Mazhul, Igor V. Mjakinnik, and Alena N. Volkova "Intramolecular dynamics of structure of alkaline phosphatase from Escherichia coli", Proc. SPIE 2370, 5th International Conference on Laser Applications in Life Sciences, (2 January 1995); https://doi.org/10.1117/12.197414

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