Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to form glycine and monocarbonic groups, essential in several biosynthetic pathways. The availability of crystallographic structures of SHMT from mesophilic organisms and information produced by the genomic projects, prompted the analysis of the adaptatgoin of SHMT to 'extreme' environments, such as high temperatures, by exploitation of structural data from thermophilic organisms.
Structural plasticity of thermophilic serine hydroxymethyltransferases / Paiardini, Alessandro; Gianese, Giulio; Bossa, Francesco; Pascarella, Stefano. - In: ITALIAN JOURNAL OF BIOCHEMISTRY. - ISSN 0021-2938. - 52:Supplement no. 1(2003), pp. 55-55. (Intervento presentato al convegno SIB-BIB 2003 tenutosi a Milano).
Structural plasticity of thermophilic serine hydroxymethyltransferases
Alessandro Paiardini;Giulio Gianese;Francesco Bossa;Stefano Pascarella
2003
Abstract
Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to form glycine and monocarbonic groups, essential in several biosynthetic pathways. The availability of crystallographic structures of SHMT from mesophilic organisms and information produced by the genomic projects, prompted the analysis of the adaptatgoin of SHMT to 'extreme' environments, such as high temperatures, by exploitation of structural data from thermophilic organisms.| File | Dimensione | Formato | |
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