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Literature summary extracted from

  • Ray, R.R.
    Purification and characterization of extracellular beta-amylase of Bacillus megaterium B6 (2000), Acta Microbiol. Immunol. Hung., 47, 29-40.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.2 2-mercaptoethanol 1 mM, activates Priestia megaterium

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.2 AgNO3 1 mM, 94% inhibition Priestia megaterium
3.2.1.2 Al2(SO4)3 1 mM, 57% inhibition Priestia megaterium
3.2.1.2 Bi(NO3)3 1 mM, 54% inhibition Priestia megaterium
3.2.1.2 CuCl2 1 mM, 93% inhibition Priestia megaterium
3.2.1.2 FeCl3 1 mM, 16% inhibition Priestia megaterium
3.2.1.2 HgCl2 1 mM, 93% inhibition Priestia megaterium
3.2.1.2 N-ethylmaleimide remarkably reduces activity Priestia megaterium
3.2.1.2 p-chloromercuribenzoate 1 mM, 97% inhibition, exogenous thiols like dithiothreitol, 2-mercaptoethanol or cysteine HCl reactivate Priestia megaterium
3.2.1.2 sodium deoxycholate 0.001%, 15% inhibition Priestia megaterium
3.2.1.2 Sodium dodecyl sulfate 0.001%, 57% inhibition Priestia megaterium
3.2.1.2 Tween 20 0.001%, 16% inhibition Priestia megaterium
3.2.1.2 Tween 40 0.001%, 15% inhibition Priestia megaterium
3.2.1.2 ZnSO4 1 mM, 54% inhibition Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.2 additional information
-
 additional information Km for starch is 4.34 mg/ml at 60°C Priestia megaterium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.2 extracellular
-
 Priestia megaterium
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.2 BaCl2 1 mM, activates Priestia megaterium
3.2.1.2 CaCl2 1 mM, activates Priestia megaterium
3.2.1.2 CoCl2 1 mM, activates Priestia megaterium
3.2.1.2 MnCl2 1 mM, activates Priestia megaterium
3.2.1.2 SrCl2 1 mM, activates Priestia megaterium

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.2 102000
-
 1 * 102000, SDS-PAGE Priestia megaterium
3.2.1.2 105000
-
 gel filtration Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Priestia megaterium
-
-
-
3.2.1.2 Priestia megaterium B6
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.2 4100fold Priestia megaterium

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 additional information
-
-
 Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 amylopectin + H2O 88% of the activity with starch Priestia megaterium ?
-
 ?
3.2.1.2 amylopectin + H2O 88% of the activity with starch Priestia megaterium B6 ?
-
 ?
3.2.1.2 amylose + H2O 79% of the activity with starch Priestia megaterium ?
-
 ?
3.2.1.2 amylose + H2O 79% of the activity with starch Priestia megaterium B6 ?
-
 ?
3.2.1.2 dextrin + H2O 13% of the activity with starch Priestia megaterium ?
-
 ?
3.2.1.2 dextrin + H2O 13% of the activity with starch Priestia megaterium B6 ?
-
 ?
3.2.1.2 additional information not: xylan, pullulan, cellulose, carboxymethyl cellulose Priestia megaterium ?
-
 ?
3.2.1.2 additional information not: xylan, pullulan, cellulose, carboxymethyl cellulose Priestia megaterium B6 ?
-
 ?
3.2.1.2 starch + H2O best substrate, pure and low quality starches, maize starch, tapioca starch Priestia megaterium beta-maltose maltose is the major end product, traces of maltooligosaccharides, no glucose as product ?
3.2.1.2 starch + H2O best substrate, pure and low quality starches, maize starch, tapioca starch Priestia megaterium B6 beta-maltose maltose is the major end product, traces of maltooligosaccharides, no glucose as product ?

Subunits

EC Number Subunits Comment Organism
3.2.1.2 monomer 1 * 102000, SDS-PAGE Priestia megaterium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 60
-
 temperature optimum, but enzyme loses activity when exposed to 60°C, irreversible thermodenaturation Priestia megaterium

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.2 60
-
 temperature optimum, but enzyme loses activity when exposed to 60°C, irreversible thermodenaturation, thermodenaturation kinetics, Mn2+ and exogenous thiols like dithiothreitol, 2-mercaptoethanol or cysteine HCl play a remarkable role in reactivation of thermally denatured enzyme Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 6.9
-
-
 Priestia megaterium

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.2 6.5 7.5 90% stability between pH 6.5 and 7.5 Priestia megaterium