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Xylan endo-1,3-β-xylosidase

From Wikipedia, the free encyclopedia
endo-1,3-β-Xylanase
Identifiers
EC no.3.2.1.32
CAS no.9025-55-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

endo-1,3-β-Xylanase, EC 3.2.1.32 [xylanase (ambiguous), endo-1,3-β-xylosidase, 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 (misleading)] is an enzyme with systematic name 3-β-D-xylan xylanohydrolase.[1][2][3][4][5] It catalyses the following chemical reaction:

Random endohydrolysis of (1→3)-β-D-glycosidic linkages in (1→3)-β-D-xylans

The 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. It produces mainly xylobiose, xylotriose and xylotetraose.

References

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  1. ^ Chen, W.P.; Matsuo, M.; Tsuneo, Y. (1986). "Purification and some properties of β-1,3-xylanase from Aspergillus terreus A-07". Agric. Biol. Chem. 50 (5): 1183–1194. doi:10.1271/bbb1961.50.1183.
  2. ^ Aoki, T.; Araki, T.; Kitamikado, M. (1988). "Purification and characterization of an endo-β-1,3-xylanase from Vibrio species". Nippon Suisan Gakkaishi. 54 (2): 277–281. doi:10.2331/suisan.54.277.
  3. ^ Araki T, Tani S, Maeda K, Hashikawa S, Nakagawa H, Morishita T (November 1999). "Purification and characterization of β-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214". Bioscience, Biotechnology, and Biochemistry. 63 (11): 2017–9. doi:10.1271/bbb.63.2017. PMID 10635569.
  4. ^ Araki T, Inoue N, Morishita T (August 1998). "Purification and characterization of β-1,3-xylanase from a marine bacterium, Alcaligenes sp. XY-234". The Journal of General and Applied Microbiology. 44 (4): 269–274. doi:10.2323/jgam.44.269. PMID 12501421.
  5. ^ Okazaki F, Shiraki K, Tamaru Y, Araki T, Takagi M (November 2005). "The first thermodynamic characterization of β-1,3-xylanase from a marine bacterium". The Protein Journal. 24 (7–8): 413–21. doi:10.1007/s10930-005-7637-8. PMID 16328734.
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