Structure-function relationship of the xylanase from alkaliphilic Bacillus sp. strain 41M-1.
Xylanase J from alkaliphilic Bacillus sp. strain 41M-1 contains a family G catalytic domain at the N-terminus, followed by a linker sequence and a functionally-unknown C-terminal domain. The mutational analysis of xylanase J indicated that Glu-93, Glu-183, Trp-18, Trp-86, Tyr-84 and Tyr-95 play an important role in the catalytic activity. A deletion derivative of xylanase J lacking the C-terminal domain retained its activity, suggesting that the C-terminal domain does not directly involved in catalysis.
Nakamura
S
S
Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Nakai
R
R
Namba
K
K
Kubo
T
T
Wakabayashi
K
K
Aono
R
R
Horikoshi
K
K
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D001665:Binding Sites / Q000235:genetics; D002384:Catalysis; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion; D043325:Xylan Endo-1,3-beta-Xylosidase; D014995:Xylosidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D011994:Recombinant Proteins; D014995:Xylosidases; D043325:Xylan Endo-1,3-beta-Xylosidase