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Literature summary for 3.2.1.1 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

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

Inhibitors

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

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus furiosus

Renatured (Commentary)

Renatured (Comment) Organism
heat denaturation is irreversible Pyrococcus furiosus

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7.5
-
Pyrococcus furiosus

pH Range

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