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Literature summary for 3.2.1.20 extracted from

  • Stanley, D.; Rejzek, M.; Naested, H.; Smedley, M.; Otero, S.; Fahy, B.; Thorpe, F.; Nash, R.J.; Harwood, W.; Svensson, B.; Denyer, K.; Field, R.A.; Smith, A.M.
    The role of alpha-glucosidase in germinating barley grains (2011), Plant Physiol., 155, 932-943.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
1-deoxynojirimycin
-
Hordeum vulgare
4-O-alpha-glucosyl-moranoline weak inhibition Hordeum vulgare
acarbose
-
Hordeum vulgare
alpha-homonojirimycin strong inhibition Hordeum vulgare
australine
-
Hordeum vulgare
castanospermine
-
Hordeum vulgare
miglitol
-
Hordeum vulgare
additional information 1-deoxygalactonojirimycin, kifunensine, and isofagomine are poor inhibitors Hordeum vulgare
N-butyl-1-deoxy-nojirimycin
-
Hordeum vulgare
N-carboxypentyl-1-deoxynojirimycin
-
Hordeum vulgare
N-cyclohexylpropyl-1-deoxynojirimycin
-
Hordeum vulgare
N-nonyl-1-deoxy-nojirimycin
-
Hordeum vulgare
Nojirimycin strong inhibition Hordeum vulgare
valienamine
-
Hordeum vulgare

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
maltose + H2O Hordeum vulgare
-
2 D-glucose
-
?

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
endosperm
-
Hordeum vulgare
-
seed
-
Hordeum vulgare
-
seedling
-
Hordeum vulgare
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltose + H2O
-
Hordeum vulgare 2 D-glucose
-
?

General Information

General Information Comment Organism
malfunction inhibition of the enzyme affects seedling growth and starch degradation, phenotype, overview Hordeum vulgare
physiological function the alpha-glucosidase HvAGL97 is the major endosperm enzyme catalyzing the conversion of maltose to glucose but is not required for starch degradation Hordeum vulgare