The Enzyme Database

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EC 3.2.1.32     
Accepted name: endo-1,3-β-xylanase
Reaction: Random endohydrolysis of (1→3)-β-D-glycosidic linkages in (1→3)-β-D-xylans
Other name(s): xylanase (ambiguous); endo-1,3-β-xylosidase (misleading); 1,3-β-xylanase; 1,3-xylanase; β-1,3-xylanase; endo-β-1,3-xylanase; 1,3-β-D-xylan xylanohydrolase; xylan endo-1,3-β-xylosidase
Systematic name: 3-β-D-xylan xylanohydrolase
Comments: This enzyme is found mostly in marine bacteria, which break down the β(1,3)-xylan found in the cell wall of some green and red algae. The enzyme produces mainly xylobiose, xylotriose and xylotetraose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-55-2
References:
1.  Chen, W.P., Matsuo, M. and Tsuneo, Y. Purification and some properties of β-1,3-xylanase from Aspergillus terreus A-07. Agric. Biol. Chem. 50 (1986) 1183–1194.
2.  Aoki, T., Araki, T. and Kitamikado, M. Purification and characterization of an endo-β-1,3-xylanase from Vibrio species. Nippon Suisan Gakkaishi 54 (1988) 277–281.
3.  Araki, T., Tani, S., Maeda, K., Hashikawa, S., Nakagawa, H. and Morishita, T. Purification and characterization of β-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214. Biosci. Biotechnol. Biochem. 63 (1999) 2017–2019. [PMID: 10635569]
4.  Araki, T., Inoue, N. and Morishita, T. Purification and characterization of β-1,3-xylanase from a marine bacterium, Alcaligenes sp. XY-234. J. Gen. Appl. Microbiol. 44 (1998) 269–274. [PMID: 12501421]
5.  Okazaki, F., Shiraki, K., Tamaru, Y., Araki, T. and Takagi, M. The first thermodynamic characterization of β-1,3-xylanase from a marine bacterium. Protein J. 24 (2005) 413–421. [PMID: 16328734]
[EC 3.2.1.32 created 1965, modified 2011]
 
 


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