Differences in the substrate specificities and active-site structures of two α-L-fucosidases (glycoside hydrolase family 29) from Bacteroides thetaiotaomicron

Biosci Biotechnol Biochem. 2012;76(5):1022-4. doi: 10.1271/bbb.111004. Epub 2012 May 7.

Abstract

Recent studies suggest that α-L-fucosidases of glycoside hydrolase family 29 can be divided into two subfamilies based on substrate specificity and phylogenetic clustering. To explore the validity of this classification, we enzymatically characterized two structure-solved α-L-fucosidases representing the respective subfamilies. Differences in substrate specificities are discussed in relation to differences in active-site structures between the two enzymes.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Bacteroides / enzymology*
  • Bacteroides / genetics
  • Carbohydrate Sequence
  • Catalytic Domain
  • Escherichia coli
  • Isoenzymes / chemistry
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Phylogeny
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Substrate Specificity
  • alpha-L-Fucosidase / chemistry*
  • alpha-L-Fucosidase / genetics
  • alpha-L-Fucosidase / metabolism

Substances

  • Bacterial Proteins
  • Isoenzymes
  • Recombinant Proteins
  • alpha-L-Fucosidase