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Literature summary for 3.2.1.106 extracted from

  • Faridmoayer, A.; Scaman, C.H.
    An improved purification procedure for soluble processing alpha-glucosidase I from Saccharomyces cerevisiae overexpressing CWH41 (2004), Protein Expr. Purif., 33, 11-18.
    View publication on PubMed

General Stability

General Stability Organism
trypsin hydrolysis releases polypeptides containing the alpha-glucosidase I catalytic domain, with no loss of catalytic activity Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
98000
-
SDS-PAGE Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae regulates one of the key steps in asparagines-linked glycoprotein biosynthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
soluble form Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3130
-
-
Saccharomyces cerevisiae

Storage Stability

Storage Stability Organism
storage of the partially purified protein for 1 month at 4°C results in complete loss of the 98000 Da band, but the enzymatic activity remains, suggesting that either one or several of the peptides contain an active catalytic fragment that is resistant to further degradation Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Glc3Man9GlcNAc2 + H2O hydrolyses specifically terminal alpha1,2-linked glucose residue Saccharomyces cerevisiae D-glucose + Glc2Man9GlcNAc2
-
?
additional information regulates one of the key steps in asparagines-linked glycoprotein biosynthesis Saccharomyces cerevisiae ?
-
?