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Literature summary extracted from

  • Beers, E.P.; Duke, S.H.
    Characterization of alpha-amylase from shoots and cotyledons of pea (Pisum sativum L.) seedlings (1990), Plant Physiol., 92, 1154-1163.
    View publication on PubMedView publication on EuropePMC

General Stability

EC Number General Stability Organism
3.2.1.1 29% loss of activity of shoot enzyme after treatment with Staphylococcus aureus V8 protease after 30 min at room temperature. 25% loss of activity of shoot enzyme after treatment with proteinase K after 30 min at room temperature. 20% loss of activity of shoot enzyme after treatment with trypsin/chymotrypsin after 30 min at room temperature Pisum sativum
3.2.1.1 Ca2+ partially stabilizes against heat inactivation Pisum sativum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 additional information
-
 additional information
-
 Pisum sativum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.1 chloroplast
-
 Pisum sativum 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 Ca2+ required Pisum sativum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 30000
-
 gel filtration at high ionic strength Pisum sativum
3.2.1.1 43500
-
 1 * 43500, SDS-PAGE Pisum sativum
3.2.1.1 45000
-
 gel filtration at low ionic strength Pisum sativum

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Pisum sativum
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.1 no modification enzyme is not a high-mannose-type glycoprotein Pisum sativum

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1
-
 Pisum sativum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.1 seedling shoot and cotyledon Pisum sativum
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.1 1190
-
 enzyme from shoots Pisum sativum
3.2.1.1 1190
-
 enzyme from cotyledons Pisum sativum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 amylopectin + H2O
-
 Pisum sativum additional information
-
 ?
3.2.1.1 amylose + H2O
-
 Pisum sativum additional information glucose + maltose ?
3.2.1.1 beta-limit dextrin + H2O
-
 Pisum sativum ?
-
 ?
3.2.1.1 maltoheptaose + H2O
-
 Pisum sativum additional information
-
 ?
3.2.1.1 maltohexaose + H2O
-
 Pisum sativum additional information
-
 ?
3.2.1.1 maltopentaose + H2O
-
 Pisum sativum additional information
-
 ?
3.2.1.1 maltotetraose + H2O
-
 Pisum sativum additional information
-
 ?
3.2.1.1 starch + H2O soluble starch Pisum sativum additional information
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 ? 1 * 43500, SDS-PAGE Pisum sativum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 additional information
-
 partial protection from heat inactivation by Ca2+, EGTA increases heat inactivation Pisum sativum
3.2.1.1 30
-
 15 min, in presence of 3 mM Ca2+, 9% loss of activity of the enzyme from shoot, 14% loss of activity of the enzyme from cotyledons. 15 min, without Ca2+, 63% loss of activity of the enzyme from shoot, 81% loss of activity of the enzyme from cotyledons Pisum sativum
3.2.1.1 70
-
 15 min, in presence of 3 mM Ca2+, 36% loss of activity of the enzyme from shoot, 23% loss of activity of the enzyme from cotyledons. 15 min, without Ca2+, 98% loss of activity of the enzyme from shoot, 99% loss of activity of the enzyme from cotyledons Pisum sativum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 5.5 6.5
-
 Pisum sativum