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Conserved sequence motifs in levansucrases and bifunctional β‐xylosidases and α‐ l ‐arabinases
Author(s) -
Naumoff Daniil G
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00369-5
Subject(s) - glycosyl , peptide sequence , protein primary structure , sequence alignment , amino acid residue , glycoside hydrolase , biochemistry , hydrolase , residue (chemistry) , amino acid , bifunctional , chemistry , biology , enzyme , gene , catalysis
Comparison of the amino acid sequences of two families of glycosyl hydrolases reveals that they are related in a region in the central part of the sequences. One of these families (GH family 68) includes levansucrases and the other one (glycosyl hydrolase family 43) includes bifunctional β‐xylosidases and α‐ l ‐arabinofuranosidases. The similarity of the primary structure of proteins from these families allows us to consider the invariant glutamate residue as a component of their active center. It is shown for the first time that glycosyl hydrolases recognizing different glycofuranoside residues can have a common sequence motif.