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Literature summary for 3.1.1.74 extracted from

  • Brissos, V.; Eggert, T.; Cabral, J.M.; Jaeger, K.E.
    Improving activity and stability of cutinase towards the anionic detergent AOT by complete saturation mutagenesis (2008), Protein Eng. Des. Sel., 21, 387-393.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of recombinant cutinase and its variants is performed with strain Escherichia coli WK-6 (delta(lac-pro) galE strA F'[lacIq ZdeltaM15 proAB+]) Fusarium solani

Protein Variants

Protein Variants Comment Organism
A164E amino acid substitution, 74% of wild-type activity Fusarium solani
A185T amino acid substitution, 142% of wild-type activity Fusarium solani
G26P amino acid substitution, 68% of wild-type activity Fusarium solani
G41A amino acid substitution, 76% of wild-type activity Fusarium solani
K140D amino acid substitution, 39% of wild-type activity Fusarium solani
K151M amino acid substitution, 22% of wild-type activity Fusarium solani
K65P amino acid substitution, 99% of wild-type activity Fusarium solani
L153A amino acid substitution, 111% of wild-type activity Fusarium solani
L153Q amino acid substitution, 145% of wild-type activity Fusarium solani
additional information a complete saturation mutagenesis approach to search cutinase for amino acids contributing to increased stability in the presence of the anionic surfactant. Mutants showing substitutions in the large hydrophobic crevice (S54D, S57D, S61D, K65P, R196A), that is thought to be the region more involved in the unfolding by anionics, will be very important to obtain an enzyme less sensitive to AOT Fusarium solani
R156K amino acid substitution, 151% of wild-type activity Fusarium solani
R156N amino acid substitution, 89% of wild-type activity Fusarium solani
R158L amino acid substitution, 75% of wild-type activity Fusarium solani
R17S amino acid substitution, 69% of wild-type activity Fusarium solani
R196A amino acid substitution, 75% of wild-type activity Fusarium solani
R196E amino acid substitution, 21% of wild-type activity Fusarium solani
S54D amino acid substitution, 79% of wild-type activity Fusarium solani
S54E amino acid substitution, 83% of wild-type activity Fusarium solani
S57D amino acid substitution, 61% of wild-type activity Fusarium solani
S61D amino acid substitution, 83% of wild-type activity Fusarium solani
T179C amino acid substitution, 90% of wild-type activity Fusarium solani
T179E amino acid substitution, 10% of wild-type activity Fusarium solani
T179N amino acid substitution, 119% of wild-type activity Fusarium solani
T18D amino acid substitution, 65% of wild-type activity Fusarium solani
T45D amino acid substitution, 54% of wild-type activity Fusarium solani

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Fusarium solani
-
-

Organism

Organism UniProt Comment Textmining
Fusarium solani
-
pisi
-

Purification (Commentary)

Purification (Comment) Organism
-
Fusarium solani

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
Fusarium solani 4-nitrophenol + phosphate
-
?

Synonyms

Synonyms Comment Organism
cutinase
-
Fusarium solani