beta-fructosidase superfamily: homology with some alpha-L-arabinases and beta-D-xylosidases

Proteins. 2001 Jan 1;42(1):66-76. doi: 10.1002/1097-0134(20010101)42:1<66::aid-prot70>3.0.co;2-4.

Abstract

Comparison of the amino acid sequences of four families of glycosyl hydrolases reveals that they are homologous and have several common conserved regions. Two of these families contain beta-fructosidases (glycosyl hydrolase families GH32 and GH68) and the other two include alpha-L-arabinases and beta-xylosidases (families GH43 and GH62). The latter two families are proposed to be grouped together with the former two into the beta-fructosidase (furanosidase) superfamily. Several ORFs can be considered as a fifth family of the superfamily on the basis of sequence similarity. It is shown for the first time that a glycosyl hydrolase superfamily can include enzymes with both inversion and retention mechanism of action. Composition of the active center for enzymes of the superfamily is discussed.

MeSH terms

  • Catalytic Domain
  • Conserved Sequence
  • Glycoside Hydrolases / chemistry*
  • Glycoside Hydrolases / classification*
  • Molecular Sequence Data
  • Multigene Family*
  • Open Reading Frames
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Xylosidases / chemistry*
  • beta-Fructofuranosidase

Substances

  • Glycoside Hydrolases
  • Xylosidases
  • beta-Fructofuranosidase
  • exo-1,4-beta-D-xylosidase
  • alpha-N-arabinofuranosidase