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Literature summary extracted from

  • Gai, Y.; Chen, J.; Zhang, S.; Zhu, B.; Zhang, D.
    Property improvement of alpha-amylase from Bacillus stearothermophilus by deletion of amino acid residues arginine 179 and glycine 180 (2018), Food Technol. Biotechnol., 56, 58-64 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.1 gene ami, recombinant expression of wild-type enzyme and deletion mutant in Bacillus subtilis strain 1A751 Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.1 additional information construction of a dexadletion mutant AmySDELTAR179-G180 by deleting Arg179 and Gly180 through site-directed mutagenesis. The thermostability of mutant AmySDELTAR179-G180 is enhanced and the half-life at 100°C significantly increased from 24 to 33 min. In addition, AmySDELTAR179-G180 exhibits greatxader acid resistance and lower calcium requirements to maintain alpha-amylase activity compared to the wild-type enzyme AmyS. The sexadcretory capacity of the recombinant strain is evaluated by fed-batch fermentation in a 7.5-litre fermenter in which high alpha-amylase activity is obtained. The highest activity reaches 3300 U/ml with a high productivity of 45.8 U/(ml*h). Structural comparison of the AmyS model with that of the AmySDELTAR179-G180 mutant model shows that the deletion of R179-G180 causes a slight structural rearrangement and a decrease in AmySDELTAR179-G180 calcium requirements Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.1 starch + H2O Geobacillus stearothermophilus alpha-amylases are classical calcium-binding enzymes, which randomly hydrolyze internal alpha-1,4-glucosidic linkages in starch to produce smaller molecular mass maltodextrins, maltooligosaccharides and glucose ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Geobacillus stearothermophilus O31193 i.e. Bacillus stearothermophilus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 starch + H2O
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 Geobacillus stearothermophilus ?
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 ?
3.2.1.1 starch + H2O alpha-amylases are classical calcium-binding enzymes, which randomly hydrolyze internal alpha-1,4-glucosidic linkages in starch to produce smaller molecular mass maltodextrins, maltooligosaccharides and glucose Geobacillus stearothermophilus ?
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 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 ? x * 58000, recombinant wild-type enzyme, SDS-PAGE Geobacillus stearothermophilus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.1 1,4-alpha-D-glucan glucanohydrolase
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 Geobacillus stearothermophilus
3.2.1.1 ami
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 Geobacillus stearothermophilus
3.2.1.1 AmyS
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 Geobacillus stearothermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 100
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 purified recombinant wild-type enzyme AmyS, half-life is 24 min, for the purified recombinant mutant AmySxadDELTAR179-G180 half-life is 33 min Geobacillus stearothermophilus

General Information

EC Number General Information Comment Organism
3.2.1.1 additional information homology modeling of native AmyS and mutant AmySxadDELTAR179-G180 structures are created using the wild-type BStA (PDB ID 1HVX) as a template. A small extra loop containing residues Arg179-Gly180 is located in domain B of AmyS Geobacillus stearothermophilus
3.2.1.1 physiological function alpha-amylases are classical calcium-binding enzymes, which randomly hydrolyze internal alpha-1,4-glucosidic linkages in starch to produce smaller molecular mass maltodextrins, maltooligosaccharides and glucose Geobacillus stearothermophilus