Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi

Details

Serval ID
serval:BIB_FC6D84CC638B
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi
Journal
Biochemical Journal
Author(s)
Mouyna  I., Monod  M., Fontaine  T., Henrissat  B., Lechenne  B., Latge  J. P.
ISSN
0264-6021 (Print)
Publication state
Published
Issued date
05/2000
Volume
347
Number
3
Pages
741-747
Notes
Journal Article --- Old month value: May 1
Abstract
A new family of glycosylphosphatidylinositol-anchored beta(1-3)glucanosyltransferases (Gelp), recently identified and characterized in the filamentous fungus Aspergillus fumigatus, showed functional similarity to the Gas/Phr/Epd protein families, which are involved in yeast morphogenesis. Sequence comparisons and hydrophobic cluster analysis (HCA) showed that all the Gas/Phr/Epd/Gel proteins belong to a new family of glycosylhydrolases, family 72. We confirmed by site-directed mutagenesis and biochemical analysis that the two conserved glutamate residues (the putative catalytic residues of this family, as determined by HCA) are involved in the active site of this family of glycosylhydrolases.
Keywords
Amino Acid Sequence Aspergillus fumigatus/*enzymology Binding Sites Blotting, Western *Catalytic Domain Conserved Sequence/genetics Fungal Proteins/*chemistry/classification/genetics/*metabolism Glucan Endo-1,3-beta-D-Glucosidase/*chemistry/classification/genetics/*metabolism Glutamic Acid/genetics/metabolism Glycosylphosphatidylinositols/metabolism Molecular Sequence Data Multigene Family/genetics Mutation/genetics Protein Structure, Secondary Recombinant Proteins/chemistry/classification/genetics/metabolism Sequence Alignment
Pubmed
Web of science
Create date
25/01/2008 17:46
Last modification date
20/08/2019 17:27
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