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Literature summary for 3.1.1.73 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)

Cloned (Comment) Organism
expression in Pichia pastoris Aspergillus niger

Protein Variants

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

Organism

Organism UniProt Comment Textmining
Aspergillus niger O42807
-
-

Renatured (Commentary)

Renatured (Comment) Organism
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

Synonyms Comment Organism
FAEA
-
Aspergillus niger

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
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
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