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Literature summary extracted from

  • Laderman, K.A.; Davis, B.R.; Krutzsch, H.C.; Lewis, M.S.; Griko, Y.V.; Privalov, P.L.; Anfinsen, C.B.
    The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus (1993), J. Biol. Chem., 268, 24394-24401.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.2.1.1 free Ca2+, slight stabilization Pyrococcus furiosus
3.2.1.1 guanidine HCl, 1 M, 27% loss of activity, significant decrease in activity at 2 M Pyrococcus furiosus
3.2.1.1 moderate protease susceptibility Pyrococcus furiosus
3.2.1.1 urea, 1 M, 13% loss of activity, significant decrease in activity at 2 M Pyrococcus furiosus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 Co2+
-
 Pyrococcus furiosus
3.2.1.1 Cr2+
-
 Pyrococcus furiosus
3.2.1.1 Cu2+
-
 Pyrococcus furiosus
3.2.1.1 Fe2+
-
 Pyrococcus furiosus
3.2.1.1 Mg2+
-
 Pyrococcus furiosus
3.2.1.1 Zn2+
-
 Pyrococcus furiosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 additional information
-
 additional information
-
 Pyrococcus furiosus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.1 intracellular
-
 Pyrococcus furiosus 5622
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 66000
-
 2 * 66000, intracellular enzyme, electrophoresis in presence of 8 M urea Pyrococcus furiosus
3.2.1.1 129000
-
 non-denaturing PAGE Pyrococcus furiosus
3.2.1.1 130500
-
 equilibrium ultracentrifugation Pyrococcus furiosus
3.2.1.1 157000
-
 gel filtration Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Pyrococcus furiosus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1
-
 Pyrococcus furiosus

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.2.1.1 heat denaturation is irreversible Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 maltoheptaose + H2O
-
 Pyrococcus furiosus additional information
-
 ?
3.2.1.1 maltohexaose + H2O
-
 Pyrococcus furiosus additional information
-
 ?
3.2.1.1 maltotriose the final optimum also mirrors the reverse reaction Pyrococcus furiosus maltose + glucose + maltotetraose + maltopentaose + maltohexaose
-
 r
3.2.1.1 maltotriose + H2O
-
 Pyrococcus furiosus maltose + D-glucose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 dimer 2 * 66000, intracellular enzyme, electrophoresis in presence of 8 M urea Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 100
-
-
 Pyrococcus furiosus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.1 70 115 70°C: about 30% of maximal activity, 115°C: about 75% of maximal activity Pyrococcus furiosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 additional information
-
 the process of heat denaturation is complex and includes at least three stages, indicating that the protein structure consists of three domains, heat denaturation is irreversible Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 6.5 7.5
-
 Pyrococcus furiosus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.1 6 8 pH 6.0: about 50% of maximal activity, pH 8.0: about 60% of maximal activity Pyrococcus furiosus