Abstract
A remarkable tendency towards thermophilicity and thermostability seems to be a general trend of aspartate aminotrasferases (AspAT). This was first discovered by Jenkins et al. (1959) who introduced a vigourous heating step into their purification protocol for pig heart cytosolic enzyme. AspATs from different microorganisms living in different habitats are inactivated at temperatures 30–40° above the optimum growth temperature of the organism (Topt), as shown in Table I. Even AspAT from a Moraxella strain, which grows in the Antarctic, has a Tinact of 48°C where Tinact is the temperature at which after a 10 min incubation of the cell extracts, transaminase activity is 50% of the value before incubation.
This paper is dedicated to the memory of our very much missed friend and colleague Gianpaolo Nitti.
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References
Arnone, M. I., Birolo, L., Cubellis, M. V., Nitti, G., Marino, G. and Sannia, G., (1992) Expression of a hyperthermophilic aspartate aminotransferase in Escherichia coli. Biochem. Biophys. Acta 1160, 206–212.
Arnone, M. I., Birolo, L., Giamberini, M., Cubellis, M. V., Nitti, G., Sannia, G. and Marino, G., (1992) Limited proteolysis as a probe of conformational changes in aspartate aminotransferase from Sulfolobus solfataricus. Ear. J. Biochern., 204, 1183–1189.
Jenkins, W. T., Yphantis, D. A. and Sizer, I. W. (1959) Glutamic aspartic transaminase. I Assay, purification, and general properties. J. Biol. Chen,. 234, 51–58.
Marino, G., Arnone, M. I., Birolo, L., Cubellis, M. V., Nitti, G., Pucci, P., Zappacosta, F. and Sannia, G. (1991) Aspartate aminotransferase from Sulfolobvs solfataricus: a hyperthermophilic enzyme. In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds as Cofactors (Eds. Fukui, T., Kagamiyama, H., Soda, K. and Wada, H. ) pp. 43–55.
Metha, P. K., Hale, T. I. and Christen, P. (1993) Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur. J. Biochem., 214, 549–561.
Ratkowsky, D. A., Olley, J., McMeekin, T. A. and Ball, A. (1982) Relationships between temperature and growth rate of bacterial cultures. J. Bacteriol., 149, 1–5.
Zappacosta, F., Sannia, G., Savoy, L.A., Marino, G. and Pucci, P. (1994) Post-translational modifications in aspartate aminotransferase from Sulfolobus.solfataricus. Detection of N-smethyl lysine by mass spectrometry. Eur. J Biochem., 222, 761–767.
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© 1994 Birkhäuser Verlag Basel/Switzerland
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Marino, G., Birolo, L., Sannia, G. (1994). Aspartate aminotransferases like it hot. In: Marino, G., Sannia, G., Bossa, F. (eds) Biochemistry of Vitamin B6 and PQQ. Advances in Life Sciences. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7393-2_10
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DOI: https://doi.org/10.1007/978-3-0348-7393-2_10
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