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Literature summary extracted from

  • Sakano, Y.; Fukushima, J.; Kobayashi, T.
    Hydrolysis of alpha-1,4- and alpha-1,6-glucosidic linkages in trisaccharides by the Thermoactinomyces vulgaris alpha-amylase (1983), Agric. Biol. Chem., 47, 2211-2216.
No PubMed abstract available

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 15
-
 amylose short chain amylose, as anhydro-glucose units Thermoactinomyces vulgaris
3.2.1.1 20
-
 pullulan calculated as low molecular weight products Thermoactinomyces vulgaris

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Thermoactinomyces vulgaris
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 amylose + H2O
-
 Thermoactinomyces vulgaris ?
-
 ?
3.2.1.1 isopanose + H2O
-
 Thermoactinomyces vulgaris additional information at low substrate concentratins, 0.5%, equimolar maltose and glucose are produced, at high substrate concentrations, 4.0%, a small amount of isomaltoside + glucose + maltose is produced. The enzyme can hydrolyze alpha-1,6-glucosidic linkage as well as alpha-1,4-glucosidic linkage ?
3.2.1.1 maltotriose + H2O
-
 Thermoactinomyces vulgaris maltose + D-glucose
-
 ?
3.2.1.1 pullulan + H2O
-
 Thermoactinomyces vulgaris panose + ?
-
 ?
3.2.1.1 starch + H2O
-
 Thermoactinomyces vulgaris additional information
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 4.5
-
 hydrolysis of starch, pullulan, isopanose, maltotriose Thermoactinomyces vulgaris