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Literature summary extracted from

  • Wu, X.Q.; Wang, J.; Lue, Z.R.; Tang, H.M.; Park, D.; Oh, S.H.; Bhak, J.; Shi, L.; Park, Y.D.; Zou, F.
    Alpha-glucosidase folding during urea denaturation: enzyme kinetics and computational prediction (2010), Appl. Biochem. Biotechnol., 160, 1341-1355.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.2.1.20 enzyme denaturation, inactivated in a dose-dependent manner, after 2 h of incubation at 25°C with 2000 mM urea only 90% relative enzyme activity, after 2 h of incubation at 25°C with 5000 mM urea enzyme inactive Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.20 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.20 p-nitrophenyl alpha-D-glucopyranoside + H2O assay at pH 6.8, 37°C, reaction stopped by adding Na2CO3 Saccharomyces cerevisiae 4-nitrophenol + D-glucose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.20 alpha-glucosidase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.20 37
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.20 6.8
-
 assay at Saccharomyces cerevisiae