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...
Main Authors: | Fábio K Tamaki, Larissa C Textor, Igor Polikarpov, Sandro R Marana |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2014-01-01
|
Series: | PLoS ONE |
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24804841/?tool=EBI |
Similar Items
-
Mutations close to a hub residue affect the distant active site of a GH1 β-glucosidase.
by: Valquiria P Souza, et al.
Published: (2018-01-01) -
Structural and biochemical data of Trichoderma harzianum GH1 β-glucosidases
by: Renata N. Florindo, et al.
Published: (2017-12-01) -
In Silico Approach to Elucidate Factors Associated with GH1 β-Glucosidase Thermostability
by: Amer Ahmed, et al.
Published: (2019-12-01) -
Search for independent (β/α)4 subdomains in a (β/α)8 barrel β-glucosidase.
by: Vitor M Almeida, et al.
Published: (2018-01-01) -
Structural and Functional Insights Into CmGH1, a Novel GH39 Family β-Glucosidase From Deep-Sea Bacterium
by: Yanfang Shen, et al.
Published: (2019-12-01)