Dg. Naumoff, Conserved sequence motifs in levansucrases and bifunctional beta-xylosidases and alpha-L-arabinases, FEBS LETTER, 448(1), 1999, pp. 177-179
Comparison of the amino acid sequences of two families of glycosyl hydrolas
es reveals that they are related in a region in the central part of the seq
uences, One of these families (GH family 68) includes levansucrases acid th
e other one (glycosyl hydrolase family 43) includes bifunctional beta-xylos
idases and alpha-L-arabinofuranosidases. The similarity of the primary stru
cture of proteins from these families allows us to consider the invariant g
lutamate 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. (C) 1999 Federation of European
Biochemical Societies.