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Literature summary for 3.2.1.1 extracted from

  • De, M.; Das, K.P.; Chakrabartty, P.K.
    Purification and characterization of alpha-amylase from Bacillus amyloliquefaciens NCIM 2829 (2005), Indian J. Biochem. Biophys., 42, 287-294.
    View publication on PubMed
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General Stability

General Stability Organism
Co2+ activates and enhances structural enzyme stability Bacillus amyloliquefaciens

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ strong inhibition Bacillus amyloliquefaciens
Hg2+ strong inhibition Bacillus amyloliquefaciens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Bacillus amyloliquefaciens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates and enhances structural enzyme stability Bacillus amyloliquefaciens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
67500
-
 x * 67500, SDS-PAGE Bacillus amyloliquefaciens

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
-
-
-
Bacillus amyloliquefaciens NCIM 2829
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme to homogeneity from strain NCIM 2829 culture filtrate Bacillus amyloliquefaciens

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
58
-
 purified enzyme Bacillus amyloliquefaciens

Subunits

Subunits Comment Organism
? x * 67500, SDS-PAGE Bacillus amyloliquefaciens
More loosly packed enzyme interior, secondary enzyme structure does not protect against aqueous environment, overview Bacillus amyloliquefaciens