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Literature summary extracted from

  • Channale, S.M.; Bhide, A.J.; Yadav, Y.; Kashyap, G.; Pawar, P.K.; Maheshwari, V.L.; Ramasamy, S.; Giri, A.P.
    Characterization of two coleopteran alpha-amylases and molecular insights into their differential inhibition by synthetic alpha-amylase inhibitor, acarbose (2016), Insect Biochem. Mol. Biol., 74, 1-11 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.1 sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21 Star (DE3) Callosobruchus chinensis
3.2.1.1 sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21 Star (DE3) in inclusion bodies Tribolium castaneum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 acarbose enzyme binding and docking study Callosobruchus chinensis
3.2.1.1 acarbose enzyme binding and docking study Tribolium castaneum
3.2.1.1 wheat amylase inhibitor a proteinaceous inhibitor Callosobruchus chinensis
3.2.1.1 wheat amylase inhibitor a proteinaceous inhibitor Tribolium castaneum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 additional information
-
additional information Michaelis-Menten kinetic analysis Callosobruchus chinensis
3.2.1.1 additional information
-
additional information Michaelis-Menten kinetic analysis Tribolium castaneum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.1 extracellular the enzyme contains a signal peptide Callosobruchus chinensis
-
-
3.2.1.1 extracellular the enzyme contains a signal peptide Tribolium castaneum
-
-

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 Callosobruchus chinensis
-
D-glucose + maltose + maltotriose
-
?
3.2.1.1 starch + H2O Tribolium castaneum
-
maltose + maltotriose + maltotetraose
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Callosobruchus chinensis A0A168VCK5 i.e. Pachymerus chinensis
-
3.2.1.1 Tribolium castaneum P09107
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 recombinant His6-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography Callosobruchus chinensis
3.2.1.1 recombinant solubilized and refolded His6-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography Tribolium castaneum

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.2.1.1 recombinant His6-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21 Star (DE3) inclusion bodies using solubilization of the enzyme protein in denaturing buffer containing 20 mM Tris, pH 8.5, 8 M urea, 100 mM NaCl, 1 mM 2-mercaptoethanol, followed by a on-column refolding method Tribolium castaneum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 amylopectin + H2O
-
Tribolium castaneum ?
-
?
3.2.1.1 amylopectin + H2O preferred substrate Callosobruchus chinensis ?
-
?
3.2.1.1 starch + H2O
-
Callosobruchus chinensis D-glucose + maltose + maltotriose
-
?
3.2.1.1 starch + H2O
-
Tribolium castaneum maltose + maltotriose + maltotetraose
-
?
3.2.1.1 starch + H2O preferred substrate Tribolium castaneum maltose + maltotriose + maltotetraose
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 More three-dimensional enzyme structure modelling Callosobruchus chinensis
3.2.1.1 More three-dimensional enzyme structure modelling Tribolium castaneum

Synonyms

EC Number Synonyms Comment Organism
3.2.1.1 CcAmy
-
Callosobruchus chinensis
3.2.1.1 TcAmy
-
Tribolium castaneum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 40
-
recombinant enzyme Tribolium castaneum
3.2.1.1 50
-
recombinant enzyme Callosobruchus chinensis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.1 0.92
-
starch pH 5.0, 37°C, recombinant enzyme Callosobruchus chinensis
3.2.1.1 1.1
-
amylopectin pH 5.0, 37°C, recombinant enzyme Callosobruchus chinensis
3.2.1.1 1.13
-
starch pH 5.0, 37°C, recombinant enzyme Tribolium castaneum
3.2.1.1 1.4
-
amylopectin pH 5.0, 37°C, recombinant enzyme Tribolium castaneum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 5
-
recombinant enzyme Callosobruchus chinensis
3.2.1.1 5
-
recombinant enzyme Tribolium castaneum

General Information

EC Number General Information Comment Organism
3.2.1.1 evolution phylogenetic tree of coleopteran alpha-amylases Callosobruchus chinensis
3.2.1.1 evolution phylogenetic tree of coleopteran alpha-amylases Tribolium castaneum
3.2.1.1 additional information homology modeling and molecular docking of alpha-amylase from Callosobruchus chinensis and comparison to the alpha-amylase from Tribolium castaneum showing structural differences between these two enzymes, overview Callosobruchus chinensis
3.2.1.1 additional information homology modeling and molecular docking of alpha-amylase from Callosobruchus chinensis and comparison to the alpha-amylase from Tribolium castaneum showing structural differences between these two enzymes, overview Tribolium castaneum