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Literature summary for 3.2.1.1 extracted from

  • Tsvetkov, V.T.; Emanuilova, E.I.
    Purification and properties of heat stable alpha-amylase from Bacillus brevis (1989), Appl. Microbiol. Biotechnol., 31, 246-248.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
Ag+ weak Brevibacillus brevis
Co2+ weak Brevibacillus brevis
Cu2+ weak Brevibacillus brevis
Fe2+ strong Brevibacillus brevis
Mg2+ weak Brevibacillus brevis
N-bromosuccinimide strong Brevibacillus brevis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Brevibacillus brevis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Brevibacillus brevis
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ stimulates Brevibacillus brevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27000
-
the difference between the value determined by gel filtration and by SDS-PAGE might be due to the affinity of this enzyme for Sephadex G-100, which might have substrate affinity for the enzyme Brevibacillus brevis

Organism

Organism UniProt Comment Textmining
Brevibacillus brevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Brevibacillus brevis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Brevibacillus brevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
-
Brevibacillus brevis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
pH 8.0, in presence of 5 mM CaCl2, half-life: 20 min Brevibacillus brevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 9
-
Brevibacillus brevis