α-L-Arabinofuranosidase (EC 3.2.1.55, arabinosidase, α-arabinosidase, α-L-arabinosidase, α-arabinofuranosidase, polysaccharide α-L-arabinofuranosidase, α-L-arabinofuranoside hydrolase, L-arabinosidase, α-L-arabinanase) is an enzyme with systematic name α-L-arabinofuranoside arabinofuranohydrolase.[1][2][3] It catalyses the hydrolysis of terminal non-reducing α-L-arabinofuranoside residues in α-L-arabinosides
| α-L-Arabinofuranosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.55 | ||||||||
| CAS no. | 9067-74-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
The enzyme acts on α-L-arabinofuranosides, α-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans.
References
edit- ^ Kaji A, Tagawa K (June 1970). "Purification, crystallization and amino acid composition of α-L-arabinofuranosidase from Aspergillus niger". Biochimica et Biophysica Acta (BBA) - Protein Structure. 207 (3): 456–64. doi:10.1016/s0005-2795(70)80008-3. PMID 5452669.
- ^ Kaji A, Yoshihara O (November 1971). "Properties of purified -L-arabinofuranosidase from Corticium rolfsii". Biochimica et Biophysica Acta. 250 (2): 367–71. doi:10.1016/0005-2744(71)90193-8. PMID 5143344.
- ^ Tagawa, K.; Kaji, A. (1969). "Preparation of L-arabinose-containing polysaccharides and the action of an α-L-arabinofuranosidase on these polysaccharides". Carbohydr. Res. 11 (3): 293–301. doi:10.1016/s0008-6215(00)80570-4.
External links
edit- Alpha-L-arabinofuranosidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
