Structural adaptation of serine hydroxymethyltransferase (SHMT), a pyridoxal-5'-phosphate dependent enzyme that catalyzes the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylene-tetrahydropteroylglutamate, synthesized by microorganisms adapted to low temperatures has been analyzed using a comparative approach. The variations of amino acid properties and frequencies among three temperature populations (psychrophilic, mesophilic, hyper- and thermophilic) of SHMT sequences have been tested. SHMTs display a general increase of polarity specially in the core, a more negatively charged surface, and enhanced flexibility. Subunit interface is more hydrophilic and less compact. Electrostatic potential of the tetrahydrofolate binding site has been compared. The enzyme from Psychromonas ingrahamii, the organism with the lowest adaptation temperatures, displayed the most positive potential. In general, the property variations show a coherent opposite trend in the hyper-thermophilic population: in particular, increase of hydrophobicity, packing and decrease of flexibility was observed. (C) 2009 Elsevier B.V. All rights reserved.

Structural adaptation of serine hydroxymethyltransferase to low temperatures / Siglioccolo, Alessandro; Bossa, Francesco; Pascarella, Stefano. - In: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES. - ISSN 0141-8130. - STAMPA. - 46:1(2010), pp. 37-46. [10.1016/j.ijbiomac.2009.09.009]

Structural adaptation of serine hydroxymethyltransferase to low temperatures

SIGLIOCCOLO, ALESSANDRO;BOSSA, Francesco;PASCARELLA, Stefano
2010

Abstract

Structural adaptation of serine hydroxymethyltransferase (SHMT), a pyridoxal-5'-phosphate dependent enzyme that catalyzes the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylene-tetrahydropteroylglutamate, synthesized by microorganisms adapted to low temperatures has been analyzed using a comparative approach. The variations of amino acid properties and frequencies among three temperature populations (psychrophilic, mesophilic, hyper- and thermophilic) of SHMT sequences have been tested. SHMTs display a general increase of polarity specially in the core, a more negatively charged surface, and enhanced flexibility. Subunit interface is more hydrophilic and less compact. Electrostatic potential of the tetrahydrofolate binding site has been compared. The enzyme from Psychromonas ingrahamii, the organism with the lowest adaptation temperatures, displayed the most positive potential. In general, the property variations show a coherent opposite trend in the hyper-thermophilic population: in particular, increase of hydrophobicity, packing and decrease of flexibility was observed. (C) 2009 Elsevier B.V. All rights reserved.
2010
electrostatic potential; flexibility; molecular evolution; polarity; psychrophile; pyridoxal-5 '-phosphate; pyridoxal-5′-phosphate; serine hydroxymethyltransferase
01 Pubblicazione su rivista::01a Articolo in rivista
Structural adaptation of serine hydroxymethyltransferase to low temperatures / Siglioccolo, Alessandro; Bossa, Francesco; Pascarella, Stefano. - In: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES. - ISSN 0141-8130. - STAMPA. - 46:1(2010), pp. 37-46. [10.1016/j.ijbiomac.2009.09.009]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/227859
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