Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.1 extracted from

  • Brown, I.; Dafforn, T.R.; Fryer, P.J.; Cox, P.W.
    Kinetic study of the thermal denaturation of a hyperthermostable extracellular alpha-amylase from Pyrococcus furiosus (2013), Biochim. Biophys. Acta, 1834, 2600-2605.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Pyrococcus furiosus
-
-

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
106
-
denaturation of the enzyme is irreversible above a Tm of approximately 106°C and can be described by a one-step irreversible model Pyrococcus furiosus
117
-
t1/2: 10.1 min Pyrococcus furiosus
121
-
t1/2: 6.1 min, activation energy at 121°C is 316kJ/mol. Under an isothermal holding temperature of 121°C, the structure of the enzyme changes during denaturation from an alpha-helical structure, through a beta-sheet structure to an aggregated protein Pyrococcus furiosus
125
-
t1/2: 2.7 min Pyrococcus furiosus