Open AccessThe NodB domain of a multidomain xylanase from Cellulomonas fimi deacetylates acetylxylan
Author(s) -
Laurie Judith I,
Clarke Jonathan H,
Ciruela Antonio,
Faulds Craig B,
Williamson Gary,
Gilbert Harry J,
Rixon Jane E,
MillwardSadler Jane,
Hazlewood Geoffrey P
Publication year - 1997
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.1574-6968.1997.tb10298.x
Subject(s) - xylanase , chemistry , biochemistry , acetylation , mucor , microbiology and biotechnology , biology , enzyme , gene , aspergillus
The NodB‐like domain from Cellulomonas fimi xylanase D is a member of a small family of structurally homologous proteins which includes a chitin deacetylase from Mucor rouxii , an acetylxylan esterase from Streptomyces lividans and the NodB protein from rhizobia . Functional analysis of the xylanase D NodB domain suggests that, like other members of the family, it is a deacetylase, whose function is to remove acetyl groups from acetylated xylan.