Serine Hydroxymethyltransferase from the Cold Adapted Microorganism Psychromonas ingrahamii A Low Temperature Active Enzyme with Broad Substrate Specificity 英文参考文献.docVIP

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Serine Hydroxymethyltransferase from the Cold Adapted Microorganism Psychromonas ingrahamii A Low Temperature Active Enzyme with Broad Substrate Specificity 英文参考文献.doc

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Serine Hydroxymethyltransferase from the Cold Adapted Microorganism Psychromonas ingrahamii A Low Temperature Active Enzyme with Broad Substrate Specificity 英文参考文献

Int. J. Mol. Sci. 2012, 13, 1314-1326; doi:10.3390/ijmOPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 /journal/ijms Article Serine Hydroxymethyltransferase from the Cold Adapted Microorganism Psychromonas ingrahamii: A Low Temperature Active Enzyme with Broad Substrate Specificity Sebastiana Angelaccio *, Rita Florio, Valerio Consalvi, Guido Festa and Stefano Pascarella Department of Biochemical Sciences “A. Rossi Fanelli”, University of Rome “La Sapienza”, P.le Aldo Moro 5, Roma 00185, Italy; E-Mails: Rita.Florio@uniroma1.it (R.F.); Valerio.Consalvi@uniroma1.it (V.C.); festaguido@ (G.F.); Stefano.Pascarella@uniroma1.it (S.P.) * Author to whom correspondence should be addressed; E-Mail: Sebastiana.Angelaccio@uniroma1.it; Tel: +39-0649917686; Fax: +39-0649917566. Received: 30 November 2011; in revised form: 12 January 2012 / Accepted: 12 January 2012 / Published: 25 January 2012 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 (SHM