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Literature summary for 3.2.1.1 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
Search for more literature for 3.2.1.1

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Aspergillus flavus

Localization

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

Metals/Ions

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

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Source Tissue

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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
48.1
-
 purified native enzyme, pH 7.0, 50°C Aspergillus flavus

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
alpha amylase
-
 Aspergillus flavus

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Aspergillus flavus

pH Range

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

pH Stability

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

pI Value

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

General Information

General Information Comment Organism
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
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