From Wikipedia, the free encyclopedia
(Redirected from Xylan endo-1,3-b-xylosidase)
endo-1,3-β-Xylanase
Identifiers
EC no. 3.2.1.32
CAS no. 9025-55-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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

  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.
From Wikipedia, the free encyclopedia
(Redirected from Xylan endo-1,3-b-xylosidase)
endo-1,3-β-Xylanase
Identifiers
EC no. 3.2.1.32
CAS no. 9025-55-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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

  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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