Alpha-glucuronidase GlcA67A (Cellvibrio japonicus) (GlcA67A)

Cellvibrio japonicus GlcA67A is an alpha-glucuronidase belonging to the glycoside hydrolase family 67 (GH67) (UniProt: P0C1X8). This enzyme is produced by the soil bacterium Cellvibrio japonicus, which serves as a model organism for the degradation of complex plant cell wall polysaccharides (DeBoy et al., J. Bacteriol. 2008). GlcA67A specifically catalyzes the hydrolysis of the alpha-1,2-glycosidic bond between 4-O-methyl-D-glucuronic acid and the xylose units in glucuronoxylan, a major component of hemicellulose (Nurizzo et al., J. Mol. Biol. 2002). By removing these side chains, GlcA67A facilitates the complete breakdown of the xylan backbone by other xylanolytic enzymes such as xylanases and beta-xylosidases (CAZy Database, 2024). While GlcA67A is not a target for human clinical therapeutics, it is highly relevant in industrial biotechnology for the conversion of lignocellulosic biomass into fermentable sugars for biofuel production (DeBoy et al., J. Bacteriol. 2008). Additionally, it is utilized in the enzymatic synthesis of specialized oligosaccharides with potential prebiotic applications (CAZy Database, 2024).

Other names

CjGlcA67AAlpha-glucuronidase AGH67 alpha-glucuronidaseGlucuronoxylan-glucuronohydrolase

Catalyzes the hydrolysis of the alpha-1,2-glycosidic linkage between 4-O-methyl-D-glucuronic acid and the xylose backbone of glucuronoxylan.