The first thermodynamic characterization of beta-1,3-xylanase from a marine bacterium.
Sequence analysis of beta-1,3-xylanase (TxyA) from a marine bacterium, Alcaligenes sp. strain XY-234 implied that an xylan-binding module belonging to carbohydrate-binding module family 31 (TxyA-CBM) is separated from a catalytic module belonging to glycosyl hydrolase family 26 (TxyA-CM) by a putative glycine-rich linker [Okazaki, F., et al. (2002) J. Bacteriol. 184: 2399-2403]. In order to reveal the role of these structural features of TxyA, two modules, TxyA-CBM and TxyA-CM, were constructed, and those modules and full-length TxyA were characterized by thermodynamic studies. TxyA-CBM and TxyA-CM showed full reversible folding from denaturant-induced unfolded forms, exhibited higher thermodynamic stabilities. The conformational stability of both truncated modules is industrially desirable, as well as aiding the understanding of the enzymatic characterization of the two modules of beta-1,3-xylanase separated by a long linker.
Okazaki
Fumiyoshi
F
School of Materials Science, Japan Advanced Institute of Science and Technology (JAIST), 1-1 Asahidai, Nomi, Ishikawa 923-1292, Japan.
Shiraki
Kentaro
K
Tamaru
Yutaka
Y
Araki
Toshiyoshi
T
Takagi
Masahiro
M
D000421:Alcaligenes / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D002241:Carbohydrates / Q000737:chemistry; D002942:Circular Dichroism; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry* / Q000378:metabolism; D019791:Guanidine / Q000737:chemistry; D009792:Oceans and Seas; D011487:Protein Conformation; D011489:Protein Denaturation; D013816:Thermodynamics
D001426:Bacterial Proteins; D002241:Carbohydrates; D043364:Endo-1,4-beta Xylanases; D019791:Guanidine