IUBMB Enzyme Nomenclature

EC 3.2.1.55

Accepted name: non-reducing end α-L-arabinofuranosidase

Reaction: Hydrolysis of terminal non-reducing α-L-arabinofuranoside residues in α-L-arabinosides.

Other name(s): arabinosidase (ambiguous); α-arabinosidase; α-L-arabinosidase; α-arabinofuranosidase; polysaccharide α-L-arabinofuranosidase; α-L-arabinofuranoside hydrolase; L-arabinosidase (ambiguous); α-L-arabinanase

Systematic name: α-L-arabinofuranoside non-reducing end α-L-arabinofuranosidase

Comments: The enzyme acts on α-L-arabinofuranosides, α-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Some β-galactosidases (EC 3.2.1.23) and β-D-fucosidases (EC 3.2.1.38) also hydrolyse α-L-arabinosides. cf. EC 3.2.1.185, non-reducing end β-L-arabinofuranosidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9067-74-7

References:

1. Tagawa, K. and Kaji, A. Preparation of L-arabinose-containing polysaccharides and the action of an α-L-arabinofuranosidase on these polysaccharides. Carbohydr. Res. 11 (1969) 293-301.

2. Kaji, A. and Tagawa, K. Purification, crystallization and amino acid composition of α-L-arabinofuranosidase from Aspergillus niger. Biochim. Biophys. Acta 207 (1970) 456-464. [PMID: 5452669]

3. Kaji, A. and Yoshihara, O. Properties of purified α-L-arabinofuranosidase from Corticium rolfsii. Biochim. Biophys. Acta 250 (1971) 367-371. [PMID: 5143344]

4. Margolles-Clark, E., Tenkanen, M., Nakari-Setala, T. and Penttila, M. Cloning of genes encoding α-L-arabinofuranosidase and β-xylosidase from Trichoderma reesei by expression in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 62 (1996) 3840-3846. [PMID: 8837440]

5. Inacio, J.M., Correia, I.L. and de Sa-Nogueira, I. Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in Bacillus subtilis. Microbiology 154 (2008) 2719-2729. [PMID: 18757805]

[EC 3.2.1.55 created 1972, modified 1976 (EC 3.2.1.79 created 1972, incorporated 1976), modified 2013]


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