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Literature summary extracted from

  • Yamasaki, Y.
    beta-Amylase in germinating millet seeds (2003), Phytochemistry, 64, 935-939.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.2 Cu2+ 5 mM, 37°C, 30 min, about 80% inhibition Panicum miliaceum
3.2.1.2 Hg2+ 5 mM, 37°C, 30 min, about 80% inhibition Panicum miliaceum
3.2.1.2 Mn2+ 5 mM, 37°C, 30 min, about 80% inhibition Panicum miliaceum
3.2.1.2 p-chloromercuribenzoate 0.01 mM, 100% inhibition Panicum miliaceum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.2 58000
-
gel filtration Panicum miliaceum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.2 starch + H2O Panicum miliaceum beta-amylase should be a key enzyme in starch degradation during the germination of millet seeds, enzyme activity increases during days 1-4 of germination ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Panicum miliaceum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.2
-
Panicum miliaceum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.2 seed germinating Panicum miliaceum
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.2 103.9
-
pH 4.5, 37°C, soluble starch Panicum miliaceum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 amylopectin + H2O 114.6% of the activity with amylose, soluble starch, amylose and amylopectin are the most suitable substrates, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered Panicum miliaceum ?
-
?
3.2.1.2 amylose + H2O EX-I, soluble starch, amylose and amylopectin are the most suitable substrates, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered Panicum miliaceum ?
-
?
3.2.1.2 glycogen + H2O 49.4% of the activity with amylose Panicum miliaceum ?
-
?
3.2.1.2 maltoheptaose + H2O 34.6% of the activity with amylose Panicum miliaceum ?
-
?
3.2.1.2 maltohexaose + H2O 23.3% of the activity with amylose Panicum miliaceum ?
-
?
3.2.1.2 maltooligosaccharide + H2O beta-amylase hydrolyzes maltooligosaccharides more readily as their degree of polymerization increases, this being strongest for maltooligosaccharides larger than 13 glucose residues and very weakly for maltotriose, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered Panicum miliaceum ?
-
?
3.2.1.2 maltopentaose + H2O 13.8% of the activity with amylose Panicum miliaceum ?
-
?
3.2.1.2 maltotetraose + H2O 7.6% of the activity with amylose Panicum miliaceum ?
-
?
3.2.1.2 maltotriose + H2O very poor substrate Panicum miliaceum ?
-
?
3.2.1.2 starch + H2O beta-amylase should be a key enzyme in starch degradation during the germination of millet seeds, enzyme activity increases during days 1-4 of germination Panicum miliaceum ?
-
?
3.2.1.2 starch + H2O 106.9% of the activity with amylose, soluble starch, amylose and amylopectin are the most suitable substrates, some activity against native starch, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered Panicum miliaceum ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.2 monomer 1 * 58000, SDS-PAGE Panicum miliaceum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 55
-
optimum temperature after 30 min incubation Panicum miliaceum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.2 55
-
15 min, 50 mM NaOAc buffer, pH 6, stable up to Panicum miliaceum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 5.5 6
-
Panicum miliaceum

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.2 3.5 9 15 h, 20°C, 50 mM McIlvaine’s buffer and sodium carbonate-boric acid buffer, stable in the range Panicum miliaceum

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.2 Panicum miliaceum isoelectric focusing
-
4.9