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Literature summary extracted from

  • Li, J.; Zhang, S.; Yi, Z.; Pei, X.; Wu, Z.
    Removal of the free cysteine residue reduces irreversible thermal inactivation of feruloyl esterase: evidence from circular dichroism and fluorescence spectra (2015), Acta Biochim. Biophys. Sin. (Shanghai), 47, 612-619.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.73 expression in Pichia pastoris Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.73 D93G/S187F about 13fold increaase in catalytic turnover efficiency Aspergillus niger
3.1.1.73 D93G/S187F/C235I specific activity similar to wild-type, significant increase in thermal stability Aspergillus niger
3.1.1.73 D93G/S187F/C235N specific activity similar to wild-type, significant increase in thermal stability Aspergillus niger
3.1.1.73 D93G/S187F/C235R specific activity similar to wild-type, significant increase in thermal stability Aspergillus niger
3.1.1.73 D93G/S187F/C235S specific activity similar to wild-type, significant increase in thermal stability Aspergillus niger
3.1.1.73 D93G/S187F/C235V specific activity similar to wild-type, significant increase in thermal stability Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.73 Aspergillus niger O42807
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.1.1.73 the thermal unfolding of the parental enzyme is irreversible on all the tested conditions, while that of the Cys235 mutants is reversible, and their ability to refold is highly dependent on the denaturing temperature. Mutants denatured at 75°C are able to efficiently reverse the unfolding to regain native structure during the cooling process Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
3.1.1.73 FAEA
-
 Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.73 additional information
-
 the unfolding of the parental enzyme is irreversible on all the tested conditions, while that of the Cys235 mutants is reversible, and their ability to refold is highly dependent on the denaturing temperature. Mutants denatured at 75°C are able to efficiently reverse the unfolding to regain native structure during the cooling process Aspergillus niger
3.1.1.73 60
-
 wild-type half-life 8.3 min, half-lifes of mutants D93G/S187/C235I, D93G/S187F/C235N, D93G/S187F/C235S, D93G/S187F/C235V, D93G/S187F/C235R 9.8 to 14 min Aspergillus niger
3.1.1.73 70
-
 wild-type half-life 1.6 min, half-lifes of mutants D93G/S187/C235I, D93G/S187F/C235N, D93G/S187F/C235S, D93G/S187F/C235V, D93G/S187F/C235R 21 to 63 min Aspergillus niger