title: The endoxylanases from family 11: computer analysis of protein sequences reveals important structural and phylogenetic relationships.
abstract: Eighty-two amino acid sequences of the catalytic domains of mature endoxylanases belonging to family 11 have been aligned using the programs MATCHBOX and CLUSTAL. The sequences range in length from 175 to 233 residues. The two glutamates acting as catalytic residues are conserved in all sequences. A very good correlation is found between the presence (at position 100) of an asparagine in the so-called 'alkaline' xylanases, or an aspartic acid in those with a more acidic pH optimum. Four boxes defining segments of highest similarity were detected; they correspond to regions of defined secondary structure: B5, B6, B8 and the carboxyl end of the alpha helix, respectively. Cysteine residues are not common in these sequences (0.7% of all residues), and disulfide bridges are not important in explaining the stability of several thermophilic xylanases. The alignment allows the classification of the enzymes in groups according to sequence similarity. Fungal and bacterial enzymes were found to form mostly separate clusters of higher similarity.
authors.affiliation: Laboratorio de Bioquímica, Departamento de Genética Molecular y Microbiología, Pontificia Universidad Católica de Chile, Casilla 114-D, Santiago, Chile.
authors.forename: Amalia
authors.initials: A
authors.lastname: Sapag
authors.forename: Johan
authors.initials: J
authors.lastname: Wouters
authors.forename: Christophe
authors.initials: C
authors.lastname: Lambert
authors.forename: Pablo
authors.initials: P
authors.lastname: de Ioannes
authors.forename: Jaime
authors.initials: J
authors.lastname: Eyzaguirre
authors.forename: Eric
authors.initials: E
authors.lastname: Depiereux
mesh_terms: D000143:Acids; D000595:Amino Acid Sequence; D020134:Catalytic Domain; D017124:Conserved Sequence; D043364:Endo-1,4-beta Xylanases; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D005810:Multigene Family; D010802:Phylogeny; D017433:Protein Structure, Secondary; D014995:Xylosidases / Q000737:chemistry / Q000145:classification / Q000235:genetics*
chemical_list: D000143:Acids; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases