Substrate specificity of alpha-L-arabinofuranosidase from Bacillus subtilis 3-6 toward arabinofurano-oligosaccharides.
The substrate specificity of alpha-L-arabinofuranosidase (EC 3.2.1.55) from Bacillus subtilis 3-6 was explored using methyl 2-O-, methyl 3-O-, and methyl 5-O-alpha-L-arabinofuranosyl-alpha-L-arabinofuranosides, and methyl 3,5-di-O-alpha-L-arabinofuranosyl-alpha-L-arabinofuranoside. The enzyme hydrolyzed the methyl alpha-L-arabinofuranobiosides to arabinose and methyl alpha-L-arabinofuranoside in the order of (1-->2)- > (1-->3)- > (1-->5)-linkages. The enzyme hydrolyzed the (1-->3)-linkage more than the (1-->5)-linkage of the methyl alpha-L-arabinofuranotrioside.
Kaneko
S
S
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Kusakabe
I
I
D001412:Bacillus subtilis / Q000201:enzymology*; D002240:Carbohydrate Sequence; D006026:Glycoside Hydrolases / Q000378:metabolism*; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000378:metabolism*; D013379:Substrate Specificity
D009844:Oligosaccharides; D006026:Glycoside Hydrolases; C019713:alpha-N-arabinofuranosidase