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Literature summary for 3.2.1.20 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)

Cloned (Comment) Organism
expression in Pichia pastoris Hordeum vulgare

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Hordeum vulgare

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Stability [°C]

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

pH Optimum

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

pH Stability

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