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Molecular cloning, nucleotide sequence and characteristics of a xylanase gene ( xyn A) from Ruminococcus albus 7
Author(s) -
NAKAMURA Mutsumi,
NAGAMINE Takafumi,
TAKENAKA Akio,
AMINOV Rustem I.,
OGATA Koretsugu,
TAJIMA Kiyoshi,
MATSUI Hiroki,
BENNO Yoshimi,
ITABASHI Hisao
Publication year - 2002
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1046/j.1344-3941.2002.00048.x
Subject(s) - xylanase , nucleic acid sequence , ruminococcus , gene , biology , peptide sequence , cloning (programming) , biochemistry , genetics , bacteria , enzyme , computer science , programming language
ABSTRACT A 2.6‐kb DNA fragment encoding a xylanase gene ( xyn A) was cloned from the rumen hemicellulolytic bacterium Ruminococcus albus 7. The deduced primary structure of the protein (XynA) was divided into a signal peptide region and 3 domains. Domain A was identified as a family 11 (G) catalytic domain, but one amino acid residue was replaced by another in an active site signature 1 of family 11. Domain B is a stabilizing domain for the catalytic domains of families 10 and 11. Deletion of domain B reduced stability of the xylanase at high temperature and at high and low pH. Domain B may be useful for protein engineering of xylanase. Domain C has sequence similarity to deacetylases and NodB proteins.