Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Takagi, T.; Toda, H.; Isemura, T.
    Bacterial and mold amylases (1971), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 5, 235-271.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.1
-
 Bacillus subtilis
3.2.1.1
-
 Aspergillus oryzae

General Stability

EC Number General Stability Organism
3.2.1.1 pH 7, 20°C, stable against 6 M urea in presence of dialyzable Ca2+. In absence of dialyzable Ca2+, urea at less than 4 M denatures Aspergillus oryzae
3.2.1.1 stable against denaturation by SDS Aspergillus oryzae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 EDTA
-
 Bacillus subtilis
3.2.1.1 EDTA
-
 Geobacillus stearothermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 41000
-
-
 Geobacillus stearothermophilus
3.2.1.1 41000
-
 approach to equilibium method Bacillus subtilis
3.2.1.1 47000
-
 monomer, equilibrium sedimentation Bacillus subtilis
3.2.1.1 48000 52700 equilibrium sedimentation Geobacillus stearothermophilus
3.2.1.1 48900
-
 monomer, sedimentation and diffusion data Bacillus subtilis
3.2.1.1 49000
-
-
 Geobacillus stearothermophilus
3.2.1.1 49000
-
 gel filtration Aspergillus oryzae
3.2.1.1 50000 51000 sedimentation and diffusion data Aspergillus oryzae
3.2.1.1 52600
-
 equilibrium sedimentation Aspergillus oryzae
3.2.1.1 61000
-
 acid-stable and acid-unstable enzyme, equilibrium sedimentation Aspergillus niger
3.2.1.1 96900
-
 dimer, sedimentation and diffusion data Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Aspergillus niger
-
 acid-stable and acid-unstable enzyme
-
3.2.1.1 Aspergillus oryzae
-
-
-
3.2.1.1 Bacillus subtilis
-
-
-
3.2.1.1 Geobacillus stearothermophilus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.1 glycoprotein carbohydrate moiety is heterogeneous Aspergillus oryzae
3.2.1.1 glycoprotein acid-stable and acid-unstable alpha-amylase contains 24 mol and 7 mol of mannose, and 4 mol and 1 mol of hexosamine per mol protein, respectively Aspergillus niger

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1
-
 Bacillus subtilis
3.2.1.1
-
 Aspergillus oryzae

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.2.1.1 acid-denatured enzyme is able to regain the intact structure by neutralization, irreversible denaturation after exposure to an alkaline pH , denaturation under high pressure, reduced enzyme in 8 M urea or 6 M guanidine hydrochloride is completely denatured to a randomly coiled state, Ca2+ has a profound effect on the renaturation process Aspergillus oryzae
3.2.1.1 denaturation under high pressure, enzyme denatured by 8 M urea can refold to regain its activity. Rate and extent of reactivation increases in the presence of various other proteins, bovine serum albumin is most effective Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 starch + H2O
-
 Bacillus subtilis additional information
-
 ?
3.2.1.1 starch + H2O
-
 Geobacillus stearothermophilus additional information
-
 ?
3.2.1.1 starch + H2O
-
 Aspergillus niger additional information
-
 ?

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.1 5 10.5 stable Aspergillus oryzae