G0535

Glycopeptidase A from almonds

buffered aqueous glycerol solution, ≥0.05 unit/mL

• Synonym(s): N-Glycosidase A, N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase, PNGase A
• CAS Number: 83534-39-8
• Enzyme Commission number: 3.5.1.52 (BRENDA, IUBMB)
• MDL number: MFCD00131222
• UNSPSC Code: 12352204
• NACRES: NA.32

Properties

• conjugate: (N-linked)
• Quality Level: 200
• form: buffered aqueous glycerol solution
• concentration: ≥0.05 unit/mL
• storage temp.: −20°C

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. These proteins cleave glycoproteins with asialocarbohydrate moieties at their β-aspartyl-glucosylamine linkages.

Application

Glycopeptidase A from almonds is used for deglycosylation. It catalyzes the removal of N-linked oligosaccharide chains and converts Asn residue to Asp.

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.

Safety Information

• Storage Class Code: 10 - Combustible liquids
• WGK: WGK 1
• Flash Point(F): No data available
• Flash Point(C): No data available