Characterization of a Neocallimastix patriciarum xylanase gene and its product.
A xylanase gene (xynC) isolated from the anaerobic ruminal fungus Neocallimastix patriciarum was characterized. The gene consists of an N-terminal catalytic domain that exhibited homology to family 11 of glycosyl hydrolases, a C-terminal cellulose binding domain (CBD) and a putative dockerin domain in between. Each domain was linked by a short linker domain rich in proline and alanine. Deletion analysis demonstrated that the CBD was essential for optimal xylanase activity of the enzyme, while the putative dockerin domain may not be required for enzyme function.
Liu
J H
JH
Institute of BioAgricultural Sciences, Academia Sinica, Taipei, Taiwan, ROC.
Selinger
B L
BL
Tsai
C F
CF
Cheng
K J
KJ
D000595:Amino Acid Sequence; D001483:Base Sequence; D008969:Molecular Sequence Data; D020088:Neocallimastix / Q000201:enzymology / Q000235:genetics*; D016415:Sequence Alignment; D043325:Xylan Endo-1,3-beta-Xylosidase; D014995:Xylosidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D014995:Xylosidases; D043325:Xylan Endo-1,3-beta-Xylosidase