title: Site-directed incorporation of non-natural amino acid into Streptomyces xylanase.
abstract: A key residue, W26G existing around the substrate-binding cleft of beta-1,4-xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A), was ascertained in this study. Several kinds of W266 mutants substituted by Trp analogs were synthesized by a site-directed incorporation method to elucidate the functional role of this aromatic residue. Significant decreases of hydrolytic activities were observed in all mutants, even though the substitution of the aromatic side chain was not so drastic, suggesting that the W266 residue had a fatal role in the hydrolytic activity of SoXyn10A.
authors.affiliation: School of Life and Environmental Science, Tsukuba University, 1-1-1 Tennoudai, Tsukuba 305-8577,Japan.
authors.forename: Takayuki
authors.initials: T
authors.lastname: Ichikawa
authors.forename: Atsushi
authors.initials: A
authors.lastname: Kuno
authors.forename: Masumi
authors.initials: M
authors.lastname: Taki
authors.forename: Takahiro
authors.initials: T
authors.lastname: Hohsaka
authors.forename: Masahiko
authors.initials: M
authors.lastname: Sisido
authors.forename: Satoshi
authors.initials: S
authors.lastname: Kaneko
authors.forename: Kazunari
authors.initials: K
authors.lastname: Taira
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Kobayashi
authors.forename: Tsunemi
authors.initials: T
authors.lastname: Hasegawa
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D004187:Disaccharides / Q000378:metabolism; D043364:Endo-1,4-beta Xylanases / Q000378:metabolism*; D006868:Hydrolysis; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D014364:Tryptophan / Q000031:analogs & derivatives / Q000737:chemistry
chemical_list: C414004:4-methylumbelliferyl-xylobioside; D000596:Amino Acids; D004187:Disaccharides; D014364:Tryptophan; D043364:Endo-1,4-beta Xylanases