title: Conserved sequence motifs in levansucrases and bifunctional beta-xylosidases and alpha-L-arabinases.
abstract: 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 beta-xylosidases and alpha-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.
authors.affiliation: State Institute for Genetics and Selection of Industrial Microorganisms, Moscow, Russia. lab2@vnigen.msk.su
authors.forename: D G
authors.initials: DG
authors.lastname: Naumoff
mesh_terms: D000595:Amino Acid Sequence; D017124:Conserved Sequence; D006026:Glycoside Hydrolases / Q000737:chemistry*; D006602:Hexosyltransferases / Q000737:chemistry*; D008969:Molecular Sequence Data; D014995:Xylosidases / Q000737:chemistry*
chemical_list: D006602:Hexosyltransferases; C021513:levansucrase; D006026:Glycoside Hydrolases; D014995:Xylosidases; C026579:exo-1,4-beta-D-xylosidase; C019713:alpha-N-arabinofuranosidase