Article (Scientific journals)
Structural Similarities and Evolutionary Relationships in Chloride-Dependent Alpha-Amylases
D'Amico, Salvino; Gerday, Charles; Feller, Georges
2000In Gene, 253 (1), p. 95-105
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Abstract :
[en] The alpha-amylase sequences contained in databanks were screened for the presence of amino acid residues Arg195, Asn298 and Arg/Lys337 forming the chloride-binding site of several specialized alpha-amylases allosterically activated by this anion. This search provides 38 alpha-amylases potentially binding a chloride ion. All belong to animals, including mammals, birds, insects, acari, nematodes, molluscs, crustaceans and are also found in three extremophilic Gram-negative bacteria. An evolutionary distance tree based on complete amino acid sequences was constructed, revealing four distinct clusters of species. On the basis of multiple sequence alignment and homology modeling, invariable structural elements were defined, corresponding to the active site, the substrate binding site, the accessory binding sites, the Ca(2+) and Cl(-) binding sites, a protease-like catalytic triad and disulfide bonds. The sequence variations within functional elements allowed engineering strategies to be proposed, aimed at identifying and modifying the specificity, activity and stability of chloride-dependent alpha-amylases.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
D'Amico, Salvino ;  Université de Liège - ULiège > GIGA-Research
Gerday, Charles ;  Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences)
Feller, Georges ;  Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie
Language :
English
Title :
Structural Similarities and Evolutionary Relationships in Chloride-Dependent Alpha-Amylases
Publication date :
25 July 2000
Journal title :
Gene
ISSN :
0378-1119
eISSN :
1879-0038
Publisher :
Elsevier, Netherlands
Volume :
253
Issue :
1
Pages :
95-105
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 26 January 2010

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