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

BRENDA support

Literature summary extracted from

  • Erlkamp, M.; Grobelny, S.; Winter, R.
    Crowding effects on the temperature and pressure dependent structure, stability and folding kinetics of Staphylococcal nuclease (2014), Phys. Chem. Chem. Phys., 16, 5965-5976.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.31.1 16800
-
-
 Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
3.1.31.1 Staphylococcus aureus P00644
-
-

Subunits

EC Number Subunits Comment Organism
3.1.31.1 monomer 1 * 16800 Staphylococcus aureus
3.1.31.1 More the enzyme contains 26.2% alpha-helices, 24.8% beta-sheets, 26.8% beta-turns, 8.7% unordered chains and 7.4% extended chains (6.1% is uncertain), PDB ID: 1STN Staphylococcus aureus

Synonyms

EC Number Synonyms Comment Organism
3.1.31.1 SNase
-
 Staphylococcus aureus
3.1.31.1 staphylococcal nuclease
-
 Staphylococcus aureus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.31.1 additional information
-
 temperature- and pressure-dependent stability diagram, thermodynamic properties, and folding reaction kinetics of the small, single-domain monomeric staphylococcal nuclease in presence or absence of macromolecular crowder agent Ficoll PM 70, which behaves as a semi-rigid spheroid with a hydrodynamic radius of about 5 nm, detailed overview. Increasing the temperature from 25°C to 57°C exhibits no change of the size of the crowder particles within the experimentalerror. No significant changes in particle size are detected by raising the pressure up to 2.5 kbar. The measured translational diffusion times indicate that, depending on the size of the protein, themicroviscosity of Ficoll PM70 is only about 4-6 times larger than the microviscosity of pure water Staphylococcus aureus