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Literature summary extracted from

  • Karim, K.M.R.; Husaini, A.; Sing, N.N.; Sinang, F.M.; Roslan, H.A.; Hussain, H.
    Purification of an alpha amylase from Aspergillus flavus NSH9 and molecular characterization of its nucleotide gene sequence (2018), 3 Biotech, 8, 204 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.1 DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression Aspergillus flavus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 Cu2+ 54% inhibition at 1 mM, 76% at 5 mM Aspergillus flavus
3.2.1.1 Fe2+ 8% inhibition at 1 mM, 27% at 5 mM Aspergillus flavus
3.2.1.1 K+ 11% inhibition at 1 mM, 21% at 5 mM Aspergillus flavus
3.2.1.1 Mg2+ 23% inhibition at 1 mM, 24% at 5 mM Aspergillus flavus
3.2.1.1 Na+ 12% inhibition at 1 mM, 28% at 5 mM Aspergillus flavus
3.2.1.1 Zn2+ 26% inhibition at 1 mM, 73% at 5 mM Aspergillus flavus

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 kinetics Aspergillus flavus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.1 extracellular the first 21 amino acids of the enzyme sequence are presumed to be a signal peptide Aspergillus flavus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 Ca2+ activates slightly at 1-5 mM Aspergillus flavus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Aspergillus flavus A0A1L6Z980 isolated from sago humus
-
3.2.1.1 Aspergillus flavus NSH9 A0A1L6Z980 isolated from sago humus
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.1 glycoprotein the enzyme sequence contains two putative asparagine-linked N-glycosylation sites (Asn-X-Ser/Thr) at the 218th and 422nd amino acid residue Aspergillus flavus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 native enzyme 3.4fold by ammonium sulfate fractionation and anion exchange chromatography Aspergillus flavus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.1 mycelium the culture is grown on raw sago starch Aspergillus flavus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.1 additional information
-
 alpha-amylase activity of crude enzyme is 2.87 U/ml after 5 days of incubation in medium containing raw sago starch Aspergillus flavus
3.2.1.1 48.1
-
 purified native enzyme, pH 7.0, 50°C Aspergillus flavus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 starch + H2O hydrolysis of alpha-1,4-glucosidic bonds Aspergillus flavus ?
-
 ?
3.2.1.1 starch + H2O hydrolysis of alpha-1,4-glucosidic bonds Aspergillus flavus NSH9 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 ? x * 54000, SDS-PAGE, x * 52500, sequence calculation, mature enzyme Aspergillus flavus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.1 alpha amylase
-
 Aspergillus flavus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 50
-
-
 Aspergillus flavus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.1 20 90 over 60% of maximal activity within this range Aspergillus flavus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 50
-
 purified enzyme, pH 5.0, 87% activity remaining after 60 min Aspergillus flavus
3.2.1.1 60
-
 purified enzyme, pH 5.0, over 70% activity remaining after 30 min Aspergillus flavus
3.2.1.1 70
-
 purified enzyme, pH 5.0, over 70% activity remaining after 15 min Aspergillus flavus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 7
-
-
 Aspergillus flavus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.1 3 9 activity range, profile overview Aspergillus flavus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.1 3
-
 purified enzyme, 25°C, 24 h, 40% activity remaining Aspergillus flavus
3.2.1.1 6 7 purified enzyme, 25°C, 24 h, completely stable at Aspergillus flavus
3.2.1.1 9
-
 purified enzyme, 25°C, 24 h, 40% activity remaining Aspergillus flavus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.1 Aspergillus flavus sequence calculation, mature enzyme
-
 4.62

General Information

EC Number General Information Comment Organism
3.2.1.1 evolution the enzyme belongs to glycosyl hydrolase family 13, GH13, capable of acting on alpha-1,4-bonds only. The peptide sequence (residues 22-399) is homologous to glycoside hydrolase superfamily (IPR017853) containing glycosyl hydrolase, family 13, catalytic domain (residues 34-390) (IPR006047-Interpro), and alpha-amylase catalytic domain, AmyAc_euk_AmyA (residues 26-395) (cd11319-CDD NCBI). Near the C-terminal (residues 407-496), the deduced peptide sequence also contains an alpha-amylase domain DUF1966 (IPR015340, pfam09260) Aspergillus flavus
3.2.1.1 additional information presence of three conserved catalytic residues of alpha-amylase, two Ca2+-binding sites, and seven conserved peptide sequences. The enzyme also carries two potential surface/secondary-binding site (SBS) residues (Trp 237 and Tyr 409) that might be playing crucial roles in both the enzyme activity and also the binding of starch granules. Enzyme structure homology modelling using the structure of alpha-amylase from Aspergillus oryzae strain RIB40 (PDB ID 2TAA) Aspergillus flavus