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

BRENDA support

Literature summary for 3.2.1.17 extracted from

  • Kyomuhendo, P.; Myrnes, B.; Brandsdal, B.O.; Smalas, A.O.; Nilsen, I.W.; Helland, R.
    Thermodynamics and structure of a salmon cold active goose-type lysozyme (2010), Comp. Biochem. Physiol. B, 156, 254-263.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme, hanging drop vapour diffusion method, 0.001 ml of 8 mg/ml protein in 150 mM NaCl and 50 mM HEPES, pH 7.25, is mixed with 0.001 ml of reservoir solutions containing 43-45% ammonium sulfate, 0.01 M cobalt chloride, and 0.1 M MES, pH 6.25-6.5, 22°C, 3 weeks, X-ray diffraction structure determination and analysis at 1.75 A resolution Salmo salar

Organism

Organism UniProt Comment Textmining
Salmo salar A6PZ97
-
-

Renatured (Commentary)

Renatured (Comment) Organism
unfolding and potential refolding analysis due to cold adaptation and heat treatment, differential scanning calorimetry. Recombinant SalG has a melting temperature of 36.8°C under thermal denaturation conditions and regains activity after returning to permissive (low) temperature. Refolding is dramatically reduced in solutions with high SalG concentrations, coupled with significant protein precipitation. Rapid and irreversible inactivation takes place during heating at high enzyme concentration Salmo salar

Subunits

Subunits Comment Organism
More structure homology modeling, overview Salmo salar

Synonyms

Synonyms Comment Organism
Goose-type lysozyme
-
Salmo salar
SalG
-
Salmo salar

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
unfolding and potential refolding analysis due to cold adaptation and heat treatment, differential scanning calorimetry. Recombinant SalG has a melting temperature of 36.8°C under thermal denaturation conditions and regains activity after returning to permissive (low) temperature. Rapid and irreversible inactivation takes place during heating at high enzyme concentration Salmo salar