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Literature summary for 1.14.99.54 extracted from

  • Tanghe, M.; Danneels, B.; Last, M.; Beerens, K.; Stals, I.; Desmet, T.
    Disulfide bridges as essential elements for the thermostability of lytic polysaccharide monooxygenase LPMO10C from Streptomyces coelicolor (2017), Protein Eng. Des. Sel., 30, 401-408.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A143C/P183C/S73C/A115C introduction of two additional disulfide bridges, mutant displays a 12°C increase in melting temperature and is able to retain 60% of its activity after heat treatment Streptomyces coelicolor
additional information introduction of additional disulfide bridges. Four out of 16 variants display an improvement in melting temperature, ranging from 2°C to 9°C Streptomyces coelicolor
S73C/A115C introduction of an additional disulfide bridge, mutant displays a 9°C increase in melting temperature Streptomyces coelicolor

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor Q9RJY2
-
-
Streptomyces coelicolor ATCC BAA-471 Q9RJY2
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information when the three disulfide bridges of the protein are broken, irreversible unfolding occurs and no residual activity can be detected after a heat treatment at 80°C Streptomyces coelicolor

Synonyms

Synonyms Comment Organism
LPMO10C
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Streptomyces coelicolor
SCO1188
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Streptomyces coelicolor

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
51
-
melting temperature, wild-type Streptomyces coelicolor
60
-
melting temperature, mutant S73C/A115C Streptomyces coelicolor
63
-
melting temperature, mutant A143C/P183C/S73C/A115C Streptomyces coelicolor
80
-
2 h, 34% residual activity. When the three disulfide bridges of the protein are broken, irreversible unfolding occurs and no residual activity can be detected after a similar heat treatment Streptomyces coelicolor