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Literature summary extracted from

  • Liu, Y.H.; Lu, F.P.; Li, Y.; Yin, X.B.; Wang, Y.; Gao, C.
    Characterisation of mutagenised acid-resistant alpha-amylase expressed in Bacillus subtilis WB600 (2008), Appl. Microbiol. Biotechnol., 78, 85-94.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.1
-
 Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.1 L134R/S320A the mutagenised protein is more acid resistant than the native protein. The optimum pH and stable range of pH with the mutagenised protein is 4.5 and 4.0 to 6.5, respectively, compared with pH 6.5 and 5.5 to 7.0 as the favorite pH and pH stability range of the native protein Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 Ba2+ 1 mM, 23% inhibition of wild-type enzyme, 28% inhibition of mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 Cd2+ 1 mM, 33% inhibition of wild-type enzyme, 48% inhibition of mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 Cu2+ 1 mM, 55% inhibition of wild-type enzyme, 49% inhibition of mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 Hg2+ 1 mM, complete inhibition of wild-type enzyme and mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 Mg2+ 1 mM, 11% inhibition of wild-type enzyme, 5% inhibition of mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 Mn2+ 1 mM, 20% inhibition of wild-type enzyme, 15% inhibition of mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 Ni2+ 1 mM, 23% inhibition of wild-type enzyme, 24% inhibition of mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 Zn2+ 1 mM, 28% inhibition of wild-type enzyme, 37% inhibition of mutant enzyme L134R/S320A Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 Ca2+ 1 mM, 1.35fold activation of wild-type enzyme, 1.24fold activation of mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 Cs+ 1 mM, 1.13fold activation of wild-type enzyme Bacillus subtilis
3.2.1.1 Sr2+ 1 mM, 1.11fold activation of wild-type enzyme, no activation of mutant enzyme L134R/S320A Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 53000
-
 x * 53000, SDS-PAGE Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Bacillus subtilis
-
-
-
3.2.1.1 Bacillus subtilis WB600
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 recombinant wild-type and mutant enzyme L134R/S320A 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 dextrin
-
 ?
3.2.1.1 starch + H2O
-
 Bacillus subtilis WB600 dextrin
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 ? x * 53000, SDS-PAGE Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 4.5
-
 mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 6.5
-
 wild-type enzyme Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.1 3.5 7 pH 3.5: about 50% of maximal activity, pH 7.0: about 70% of maximal activity, mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 5 7 pH 5.0: about 70% of maximal activity, pH 7.0: about 90% of maximal activity, wild-type enzyme Bacillus subtilis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.1 4 6.5 70°C, 1 h, stable pH-range for mutant enzyme L134R/S320A Bacillus subtilis
3.2.1.1 5.5 7 70°C, 1 h, stable pH-range for wild-type enzyme Bacillus subtilis