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G0535

Sigma-Aldrich

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

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About This Item

CAS Number:
83534-39-8
Enzyme Commission number:
3.5.1.52 (BRENDA, IUBMB)
MDL number:
MFCD00131222
UNSPSC Code:
12352204
NACRES:
NA.32

conjugate

(N-linked)

Quality Level

200

form

buffered aqueous glycerol solution

concentration

≥0.05 unit/mL

storage temp.

−20°C

Related Categories

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.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

No data available

Flash Point(C)

No data available

Certificates of Analysis (COA)

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Karen G Welinder et al.
The Journal of biological chemistry, 284(15), 9764-9769 (2009-02-13)
Proteome data of potato (Solanum tuberosum) tuber juice and of purified potato tuber vacuoles indicated that mature patatins may perhaps lack a C-terminal propeptide. We have confirmed this by complete mass spectrometric sequencing of a number of patatin variants as
Asparagine-linked oligosaccharides in human placenta and umbilical cord as demonstrated by almond glycopeptidase.
N Takahashi et al.
FEBS letters, 146(1), 139-142 (1982-09-06)
T Takahashi et al.
Biochimica et biophysica acta, 657(2), 457-467 (1981-02-13)
The glycopeptidase preparation that has been isolated from almond emulsin and acts on beta-aspartylglycosylamine linkages in glycopeptides was separated into three active fractions by DEAE-cellulose column chromatography. The three discrete species of glycopeptidase (Groups A, B and C) have been
R P Miller et al.
Biochimica et biophysica acta, 954(1), 50-57 (1988-04-28)
The beta-subunit of dog kidney (Na+ + K+)-ATPase is a sialoglycoprotein and contains three potential N-glycosylation sites. In this study, the oligosaccharide chains of purified dog kidney beta-subunit were labeled with tritium by oxidation with sodium periodate or galactose oxidase
Amelie Croset et al.
Journal of biotechnology, 161(3), 336-348 (2012-07-21)
Glycosylation is one of the most common posttranslational modifications of proteins. It has important roles for protein structure, stability and functions. In vivo the glycostructures influence pharmacokinetics and immunogenecity. It is well known that significant differences in glycosylation and glycostructures
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Articles

N-Linked Glycan Strategies

N-Linked Glycan Strategies. Use of the endoglycosidic enzyme PNGase F (N-Glycosidase F) is the most effective method of removing virtually all N-linked oligosaccharides from glycoproteins.

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