Description

• General description: Glycopeptidase found in almonds can be divided into three groups- A, B and C. the optimum pH value and the isoelectric point of glycopeptidase A is 6.0 and 7.7 respectively. It has a preference for glycopeptides with long chains. It is also capable of hydrolyzing intact glycoproteins such as, desialyted human transferrin, ovalbumin etc.[1] These proteins cleave glycoproteins with asialocarbohydrate moieties at their β-aspartyl-glucosylamine linkages.[2]
• Application: Glycopeptidase A from almonds is used for deglycosylation.[3] It catalyzes the removal of N-linked oligosaccharide chains and converts Asn residue to Asp.[4]
• Biochem/physiol Actions: Hydrolyzes an N4-(acetyl-β-D-glycosaminyl)asparagine in which the N-acetyl-D-glucosamine residue may be further glycosylated, yielding a (substituted) N-acetyl-β-D-glucoaminylamine and the peptide containing an aspartic residue.
• Unit Definition: One unit will hydrolyze 1.0 μmole of ovalbumin glycopeptide per min at pH 5.0 at 37°C.
• Physical form: Solution in 50% glycerol containing 50 mM citrate-phosphate buffer, pH 5.0, and BSA.