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Int. J. Mol. Sci. 2012, 13(2), 1314-1326; doi:10.3390/ijms13021314
Article

Serine Hydroxymethyltransferase from the Cold Adapted Microorganism Psychromonas ingrahamii: A Low Temperature Active Enzyme with Broad Substrate Specificity

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Received: 30 November 2011 / Revised: 12 January 2012 / Accepted: 12 January 2012 / Published: 25 January 2012
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
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Abstract

Serine hydroxymethyltransferase from the psychrophilic microorganism Psychromonas ingrahamii was expressed in Escherichia coli and purified as a His-tag fusion protein. The enzyme was characterized with respect to its spectroscopic, catalytic, and thermodynamic properties. The properties of the psychrophilic enzyme have been contrasted with the characteristics of the homologous counterpart from E. coli, which has been structurally and functionally characterized in depth and with which it shares 75% sequence identity. Spectroscopic measures confirmed that the psychrophilic enzyme displays structural properties almost identical to those of the mesophilic counterpart. At variance, the P. ingrahamii enzyme showed decreased thermostability and high specific activity at low temperature, both of which are typical features of cold adapted enzymes. Furthermore, it was a more efficient biocatalyst compared to E. coli serine hydroxymethyltransferase (SHMT) particularly for side reactions. Many β-hydroxy-α-amino acids are SHMT substrates and represent important compounds in the synthesis of pharmaceuticals, agrochemicals and food additives. Thanks to these attractive properties, this enzyme could have a significant potential for biotechnological applications.
Keywords: cold adaptation; serine hydroxymethyltransferase; structural flexibility; temperature dependence of enzyme activity; catalytic promiscuity; pyridoxal-5′-phosphate; cofactor-mediated stabilization; psychrophiles; Psychromonas ingrahamii cold adaptation; serine hydroxymethyltransferase; structural flexibility; temperature dependence of enzyme activity; catalytic promiscuity; pyridoxal-5′-phosphate; cofactor-mediated stabilization; psychrophiles; Psychromonas ingrahamii
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Angelaccio, S.; Florio, R.; Consalvi, V.; Festa, G.; Pascarella, S. Serine Hydroxymethyltransferase from the Cold Adapted Microorganism Psychromonas ingrahamii: A Low Temperature Active Enzyme with Broad Substrate Specificity. Int. J. Mol. Sci. 2012, 13, 1314-1326.

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