Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.

The statistical coupling analysis of 768 β-glucosidases from the GH1 family revealed 23 positions in which the amino acid frequencies are coupled. The roles of these covariant positions in terms of the properties of β-glucosidases were investigated by alanine-screening mutagenesis using the fall arm...

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Autores principales:	Fábio K Tamaki, Larissa C Textor, Igor Polikarpov, Sandro R Marana
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e6912e8aa6554dbaaa5cc7c75985a4b2
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spelling	oai:doaj.org-article:e6912e8aa6554dbaaa5cc7c75985a4b22021-11-18T08:20:24ZSets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.1932-620310.1371/journal.pone.0096627https://doaj.org/article/e6912e8aa6554dbaaa5cc7c75985a4b22014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24804841/?tool=EBIhttps://doaj.org/toc/1932-6203The statistical coupling analysis of 768 β-glucosidases from the GH1 family revealed 23 positions in which the amino acid frequencies are coupled. The roles of these covariant positions in terms of the properties of β-glucosidases were investigated by alanine-screening mutagenesis using the fall armyworm Spodoptera frugiperda β-glycosidase (Sfβgly) as a model. The effects of the mutations on the Sfβgly kinetic parameters (kcat/Km) for the hydrolysis of three different p-nitrophenyl β-glycosides and structural comparisons of several β-glucosidases showed that eleven covariant positions (54, 98, 143, 188, 195, 196, 203, 398, 451, 452 and 460 in Sfβgly numbering) form a layer surrounding the active site of the β-glucosidases, which modulates their catalytic activity and substrate specificity via direct contact with the active site residues. Moreover, the influence of the mutations on the transition temperature (Tm) of Sfβgly indicated that nine of the coupled positions (49, 62, 143, 188, 223, 278, 309, 452 and 460 in Sfβgly numbering) are related to thermal stability. In addition to being preferentially occupied by prolines, structural comparisons indicated that these positions are concentrated at loop segments of the β-glucosidases. Therefore, due to these common biochemical and structural properties, these nine covariant positions, even without physical contacts among them, seem to jointly modulate the thermal stability of β-glucosidases.Fábio K TamakiLarissa C TextorIgor PolikarpovSandro R MaranaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 5, p e96627 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Fábio K Tamaki Larissa C Textor Igor Polikarpov Sandro R Marana Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.
description	The statistical coupling analysis of 768 β-glucosidases from the GH1 family revealed 23 positions in which the amino acid frequencies are coupled. The roles of these covariant positions in terms of the properties of β-glucosidases were investigated by alanine-screening mutagenesis using the fall armyworm Spodoptera frugiperda β-glycosidase (Sfβgly) as a model. The effects of the mutations on the Sfβgly kinetic parameters (kcat/Km) for the hydrolysis of three different p-nitrophenyl β-glycosides and structural comparisons of several β-glucosidases showed that eleven covariant positions (54, 98, 143, 188, 195, 196, 203, 398, 451, 452 and 460 in Sfβgly numbering) form a layer surrounding the active site of the β-glucosidases, which modulates their catalytic activity and substrate specificity via direct contact with the active site residues. Moreover, the influence of the mutations on the transition temperature (Tm) of Sfβgly indicated that nine of the coupled positions (49, 62, 143, 188, 223, 278, 309, 452 and 460 in Sfβgly numbering) are related to thermal stability. In addition to being preferentially occupied by prolines, structural comparisons indicated that these positions are concentrated at loop segments of the β-glucosidases. Therefore, due to these common biochemical and structural properties, these nine covariant positions, even without physical contacts among them, seem to jointly modulate the thermal stability of β-glucosidases.
format	article
author	Fábio K Tamaki Larissa C Textor Igor Polikarpov Sandro R Marana
author_facet	Fábio K Tamaki Larissa C Textor Igor Polikarpov Sandro R Marana
author_sort	Fábio K Tamaki
title	Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.
title_short	Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.
title_full	Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.
title_fullStr	Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.
title_full_unstemmed	Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.
title_sort	sets of covariant residues modulate the activity and thermal stability of gh1 β-glucosidases.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/e6912e8aa6554dbaaa5cc7c75985a4b2
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Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.

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