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Literature summary extracted from

  • Muslin, E.H.; Kanikula, A.M.; Clark, S.E.; Henson, C.A.
    Overexpression, purification, and characterization of a barley alpha-glucosidase secreted by Pichia pastoris (2000), Protein Expr. Purif., 18, 20-26.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.20 expression in Pichia pastoris Hordeum vulgare

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.20 maltose above 20 mM, substrate inhibition Hordeum vulgare

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.20 Hordeum vulgare
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.20
-
 Hordeum vulgare

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.20 0.807
-
-
 Hordeum vulgare

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.20 isomaltose + H2O
-
 Hordeum vulgare 2 alpha-D-glucose
-
 ?
3.2.1.20 maltose + H2O
-
 Hordeum vulgare alpha-D-glucose + D-glucose
-
 ?
3.2.1.20 nigerose + H2O
-
 Hordeum vulgare 2 alpha-D-glucose
-
 ?
3.2.1.20 trehalose + H2O low activity Hordeum vulgare alpha-D-glucose
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.20 30
-
 begins to denature at, at pH 4 Hordeum vulgare
3.2.1.20 45
-
 begins to denature at, at pH 5-6 Hordeum vulgare

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.20 3.5 4.5 hydrolysis of maltose, recombinant enzyme Hordeum vulgare

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.20 4
-
 most thermolabile at, high concentrations of sucrose protect from inactivation Hordeum vulgare