Open AccessNucleotide sequence of arfB of Clostridium stercorarium , and prediction of catalytic residues of α‐ l ‐arabinofuranosidases based on local similarity with several families of glycosyl hydrolases 1
Author(s) -
Zverlov Vladimir V,
Liebl Wolfgang,
Bachleitner Marianne,
Schwarz Wolfgang H
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb13107.x
Subject(s) - glycosyl , hydrolase , nucleic acid sequence , glycoside hydrolase , peptide sequence , sequence alignment , consensus sequence , sequence (biology) , nucleotide , biochemistry , biology , conserved sequence , genetics , chemistry , enzyme , gene
The nucleotide sequence of the α‐ l ‐arabinofuranosidase gene arfB from Clostridium stercorarium was determined. The deduced protein has a molecular mass of 56.2 kDa with an amino terminus identical to the N‐terminal sequence of the purified mature enzyme from C. stercorarium . Its sequence is homologous to arabinofuranosidases of glycosyl hydrolase family 51. Sequence alignment and cluster analysis reveal three new members of glycosyl hydrolase family 51, allowing for the definition of highly conserved regions. Two of these regions are remarkably similar to the most conserved regions within several other families of glycosyl hydrolases, which have in common a (β/α) 8 ‐barrel as the core super‐secondary structure, and allow to predict the acid/base catalyst and the nucleophile of the active site.