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

BRENDA support

Literature summary extracted from

  • Betzel, C.; Teplyakov, A.V.; Harutyunyan, E.H.; Saenger, W.; Wilson, K.S.
    Thermitase and proteinase K: a comparison of the refined three-dimensional structures of the native enzymes (1990), Protein Eng., 3, 161-172.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.64 three-dimensional structure at 1.48 A resolution Parengyodontium album
3.4.21.66 comparison of the refined three-dimensional structure Thermoactinomyces vulgaris

General Stability

EC Number General Stability Organism
3.4.21.64 Relatively stable towards heat and denaturing agents Parengyodontium album

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.64 Calcium required for folding of the polypeptide chain Parengyodontium album
3.4.21.64 Calcium the second more mobile Ca2+ site bridges 2 loops close to the amino and the carboxy termini Parengyodontium album
3.4.21.64 Calcium 2 calcium ions are bound to the native enzyme, activity drops by 70% if this Ca2+ is removed by EDTA Parengyodontium album
3.4.21.64 Calcium the first calcium site is formed by the loop of the residues 174-178 and Asp200 Parengyodontium album
3.4.21.66 Ca2+ three calcium binding sites, two of these are tight binding sites, and removal of calcium causes unfolding and autolysis to occur. The third calcium is more weakly bound, its removal reduces the activity of the enzyme by 10%, the reduction being reversible Thermoactinomyces vulgaris

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.64 Parengyodontium album
-
-
-
3.4.21.66 Thermoactinomyces vulgaris
-
-
-

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.64 additional information
-
 Ca2+ contributes to the overal stability of the surface regions and improves the thermal stability Parengyodontium album
3.4.21.66 additional information
-
 calcium ions contribute to the overall stability of the surface regions and improve the thermal stability of the enzyme Thermoactinomyces vulgaris