一个家庭的结构和功能10 beta-xylanase嵌合体的链霉菌属olivaceoviridis e - 86 FXYN和纤维菌属fimi Cex。
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金子,Ichinose H,藤本Z, Kuno, Yura呢K、M,美津浓H, Kusakabe我,小林H
一个家庭的结构和功能10 beta-xylanase嵌合体的链霉菌属olivaceoviridis e - 86 FXYN和纤维菌属fimi Cex。
生物化学杂志。2004年6月18日;279(25):26619 - 26所示。Epub 2004年4月12日。
- PubMed ID
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15078885 (在PubMed]
- 文摘
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木聚糖酶的催化领域属于糖苷水解酶家族10 (GH10)可分为22个模块(M1锰;佐藤,Y。Niimura, Y。Yura呢,K。去,m(1999)基因(Amst)。238年,93 - 101)。检验的晶体结构GH10木聚糖酶从链霉菌属olivaceoviridis e - 86 (SoXyn10A)显示催化域的GH10木聚糖酶可以切割成两个部分,一个氨基端更大的区域和c端小区域,由衬底绑定崩裂,对应模块M14 M15边境。有人建议,石穴底物结合的拓扑GH10木聚糖酶并不守恒(Charnock, s·J。、Spurway t D。谢,H。Beylot, m . H。Virden, R。、沃伦·r·a·J。、Hazlewood g P。吉尔伯特,h . j .(1998)生物。273年化学,32187 - 32199)。 To facilitate a greater understanding of the structure-function relationship of the substrate binding cleft of GH10 xylanases, a chimeric xylanase between SoXyn10A and Xyn10A from Cellulomonas fimi (CfXyn10A) was constructed, and the topology of the hybrid substrate binding cleft established. At the three-dimensional level, SoXyn10A and CfXyn10A appear to possess 5 subsites, with the amino acid residues comprising subsites -3 to +1 being well conserved, although the +2 subsites are quite different. Biochemical analyses of the chimeric enzyme along with SoXyn10A and CfXyn10A indicated that differences in the structure of subsite +2 influence bond cleavage frequencies and the catalytic efficiency of xylooligosaccharide hydrolysis. The hybrid enzyme constructed in this study displays fascinating biochemistry, with an interesting combination of properties from the parent enzymes, resulting in a low production of xylose.