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Literature summary extracted from

  • Santorelli, M.; Maurelli, L.; Pocsfalvi, G.; Fiume, I.; Squillaci, G.; La Cara, F.; Del Monaco, G.; Morana, A.
    Isolation and characterisation of a novel alpha-amylase from the extreme haloarchaeon Haloterrigena turkmenica (2016), Int. J. Biol. Macromol., 92, 174-184 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.1 additional information poor effects by PEG 1500, PEG 3350, and PEG 8000 Haloterrigena turkmenica
3.2.1.1 Triton X-100 activates 21.2% at 1.0% v/v Haloterrigena turkmenica

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.1 gene htur2110, sequence comparisons Haloterrigena turkmenica

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate CHAPS, 39.2% inhibition at 1% v/v Haloterrigena turkmenica
3.2.1.1 Tween 20 89.4% inhibition at 1% v/v Haloterrigena turkmenica

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.1 extracellular
-
 Haloterrigena turkmenica
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 additional information when the enzyme is assayed in the presence of CaCl2 or EDTA at 5, 10, and 25 mM, neither increase nor decrease of activity is observed suggesting that Ca2+ is not required for the enzyme action, and EDTA is not inhibitory Haloterrigena turkmenica
3.2.1.1 NaCl activates, optimal at 2 M for highest enzyme activity, profile overview Haloterrigena turkmenica

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 54000
-
 gel filtration Haloterrigena turkmenica

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 Haloterrigena turkmenica
-
 ?
-
 ?
3.2.1.1 starch + H2O Haloterrigena turkmenica ATCC 51198
-
 ?
-
 ?
3.2.1.1 starch + H2O Haloterrigena turkmenica NCIMB 13204
-
 ?
-
 ?
3.2.1.1 starch + H2O Haloterrigena turkmenica DSM 5511
-
 ?
-
 ?
3.2.1.1 starch + H2O Haloterrigena turkmenica VKM B-1734
-
 ?
-
 ?

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.2.1.1 Acetone at 20% v/v, loss of 96.8% activity Haloterrigena turkmenica
3.2.1.1 chloroform at 20% v/v, activates by 5.7% activity Haloterrigena turkmenica
3.2.1.1 Ethanol at 20% v/v, loss of 88.3% activity Haloterrigena turkmenica
3.2.1.1 Methanol at 20% v/v, loss of 89.8% activity Haloterrigena turkmenica
3.2.1.1 n-Butanol at 20% v/v, loss of 70.8% activity Haloterrigena turkmenica
3.2.1.1 n-hexane at 20% v/v, activates by 9.5% activity Haloterrigena turkmenica
3.2.1.1 n-propanol at 20% v/v, loss of 87.5% activity Haloterrigena turkmenica

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Haloterrigena turkmenica D2RTP2 catalytic region of the alpha-amylase; i.e. Halococcus turkmenicus
-
3.2.1.1 Haloterrigena turkmenica ATCC 51198 D2RTP2 catalytic region of the alpha-amylase; i.e. Halococcus turkmenicus
-
3.2.1.1 Haloterrigena turkmenica DSM 5511 D2RTP2 catalytic region of the alpha-amylase; i.e. Halococcus turkmenicus
-
3.2.1.1 Haloterrigena turkmenica NCIMB 13204 D2RTP2 catalytic region of the alpha-amylase; i.e. Halococcus turkmenicus
-
3.2.1.1 Haloterrigena turkmenica VKM B-1734 D2RTP2 catalytic region of the alpha-amylase; i.e. Halococcus turkmenicus
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 native enzyme from culture supernatant 33.1fold by centrifugation at 55000 rpm, dialysis, ultrafiltration, anion exchange chromatography, dialysis, and gel filtration Haloterrigena turkmenica

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.1 additional information culture is grown in medium containing potato starch at 0.2% w/v Haloterrigena turkmenica
-

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
-
 one enzyme unit is defined as the amount of enzyme that hydrolyses 1 mg of starch in 1 min Haloterrigena turkmenica
3.2.1.1 79.8
-
 purified enzyme, pH 8.5, 55°C Haloterrigena turkmenica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 additional information the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan Haloterrigena turkmenica ?
-
 ?
3.2.1.1 additional information the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan Haloterrigena turkmenica ATCC 51198 ?
-
 ?
3.2.1.1 additional information the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan Haloterrigena turkmenica NCIMB 13204 ?
-
 ?
3.2.1.1 additional information the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan Haloterrigena turkmenica DSM 5511 ?
-
 ?
3.2.1.1 additional information the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan Haloterrigena turkmenica VKM B-1734 ?
-
 ?
3.2.1.1 potato starch + H2O 1% w/v potato starch Haloterrigena turkmenica ?
-
 ?
3.2.1.1 potato starch + H2O 1% w/v potato starch Haloterrigena turkmenica ATCC 51198 ?
-
 ?
3.2.1.1 potato starch + H2O 1% w/v potato starch Haloterrigena turkmenica NCIMB 13204 ?
-
 ?
3.2.1.1 potato starch + H2O 1% w/v potato starch Haloterrigena turkmenica DSM 5511 ?
-
 ?
3.2.1.1 potato starch + H2O 1% w/v potato starch Haloterrigena turkmenica VKM B-1734 ?
-
 ?
3.2.1.1 starch + H2O
-
 Haloterrigena turkmenica ?
-
 ?
3.2.1.1 starch + H2O
-
 Haloterrigena turkmenica ATCC 51198 ?
-
 ?
3.2.1.1 starch + H2O
-
 Haloterrigena turkmenica NCIMB 13204 ?
-
 ?
3.2.1.1 starch + H2O
-
 Haloterrigena turkmenica DSM 5511 ?
-
 ?
3.2.1.1 starch + H2O
-
 Haloterrigena turkmenica VKM B-1734 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 monomer 1 * 66000, SDS-PAGE, 1 * 49800, catalytic region of the enzyme, SDS-PAGE Haloterrigena turkmenica

Synonyms

EC Number Synonyms Comment Organism
3.2.1.1 AmyA
-
 Haloterrigena turkmenica
3.2.1.1 endo-1,4-alpha-D-glucan glucanohydrolase
-
 Haloterrigena turkmenica
3.2.1.1 htur2110
-
 Haloterrigena turkmenica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 55
-
-
 Haloterrigena turkmenica

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.1 30 65 activity range, profile overview. 55% of maximal activity at 60°C Haloterrigena turkmenica

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 50 55 purified enzyme, 2 M NaCl, pH 8.5, 84% residual activity after 1 h, highly stable also in presence of 3 M NaCl. The enzyme retains 65% activity after 24 h at 50°C, and its half-life is 5 h and 25 min at 55°C, and 12 min at 60°C Haloterrigena turkmenica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 8.5
-
-
 Haloterrigena turkmenica

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.1 6 10 over 50% of maximal activity within this range, inactive at pH 5.0, profile overview Haloterrigena turkmenica

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.1 8.5
-
 purified enzyme, 2 M NaCl, 55°C, 84% residual activity after 1 h Haloterrigena turkmenica

General Information

EC Number General Information Comment Organism
3.2.1.1 evolution the enzyme belongs to the glycosyl hydrolase family 13, GH13. The enzyme has the characteristic structure of alpha-amylases belonging to the GH family 13 with a single polypeptide chain folded into the three domains A-C Haloterrigena turkmenica
3.2.1.1 physiological function alpha-amylases randomly cleave the internal glycosidic bond of the starch chain producing shorter oligosaccharides Haloterrigena turkmenica