1us3
From Proteopedia
Contents |
NATIVE XYLANASE10C FROM CELLVIBRIO JAPONICUS
Template:ABSTRACT PUBMED 14670951
Function
[Q59675_9GAMM] Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is able to hydrolyze oat spelt xylan, the arabinoxylans from wheat and rye, and glucuronoxylan. Also displays very low activity against xylooligosaccharides. During the xylan degradation process, Xyn10C may act on the soluble xylans and long xylooligosaccharides products released by the secreted xylanases Xyn11A, Xyn11B and Xyn10A.[1] [2]
About this Structure
1us3 is a 1 chain structure with sequence from Cellvibrio japonicus. Full crystallographic information is available from OCA.
Reference
- Pell G, Szabo L, Charnock SJ, Xie H, Gloster TM, Davies GJ, Gilbert HJ. Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases. J Biol Chem. 2004 Mar 19;279(12):11777-88. Epub 2003 Dec 11. PMID:14670951 doi:10.1074/jbc.M311947200
- ↑ Millward-Sadler SJ, Davidson K, Hazlewood GP, Black GW, Gilbert HJ, Clarke JH. Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus. Biochem J. 1995 Nov 15;312 ( Pt 1):39-48. PMID:7492333
- ↑ Pell G, Szabo L, Charnock SJ, Xie H, Gloster TM, Davies GJ, Gilbert HJ. Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases. J Biol Chem. 2004 Mar 19;279(12):11777-88. Epub 2003 Dec 11. PMID:14670951 doi:10.1074/jbc.M311947200
