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Literature summary for 3.1.1.3 extracted from

  • Roussel, A.; Amara, S.; Nyyssölä, A.; Mateos-Diaz, E.; Blangy, S.; Kontkanen, H.; Westerholm-Parvinen, A.; Carrière, F.; Cambillau, C.
    A cutinase from Trichoderma reesei with a lid-covered active site and kinetic properties of true lipases (2014), J. Mol. Biol., 426, 3757-3772 .
    View publication on PubMed
Search for more literature for 3.1.1.3

Cloned(Commentary)

Cloned (Comment) Organism
-
 Trichoderma reesei

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor diffusion method, the structure of a cutinase in native and inhibitor-bound conformations is reported Trichoderma reesei

Inhibitors

Inhibitors Comment Organism Structure
C11Y4 phosphonate in the absence of surfactant, the rate of cutinase inhibition is very low. The addition of beta-octylglucoside is required to trigger the inhibition of cutinase, which is completely inactivated after 60 min Trichoderma reesei
E600 in the absence of surfactant, no inhibition is observed with E600. The addition of beta-octylglucoside is required to trigger the inhibition of cutinase, which is completely inactivated after 12 min Trichoderma reesei

Metals/Ions

Metals/Ions Comment Organism Structure
CaCl2 no absolute requirement for CaCl2 for lipase activity (65% of maximum activity in the absence of calcium), but maximum activity is measured in the presence of 4 mM CaCl2 Trichoderma reesei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23748
-
 matrix-assisted laser desorption-ionization/time-of-flight mass spectrometry Trichoderma reesei

Organism

Organism UniProt Comment Textmining
Trichoderma reesei G0RH85
-
-
Trichoderma reesei QM6a G0RH85
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification cleavage of a propeptide Trichoderma reesei

Purification (Commentary)

Purification (Comment) Organism
-
 Trichoderma reesei

Renatured (Commentary)

Renatured (Comment) Organism
after unfolding cutinase at 80°C, cooling at 20°C restores the initial conformation Trichoderma reesei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
olive oil + H2O
-
 Trichoderma reesei ?
-
 ?
olive oil + H2O
-
 Trichoderma reesei QM6a ?
-
 ?
tributyrin + 3 H2O
-
 Trichoderma reesei glycerol + 3 butyrate
-
 ?
tributyrin + 3 H2O
-
 Trichoderma reesei QM6a glycerol + 3 butyrate
-
 ?
vinyl butyrate + H2O
-
 Trichoderma reesei ?
-
 ?
vinyl butyrate + H2O
-
 Trichoderma reesei QM6a ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 pH 5.0, 20 h, less than 20% loss of activity Trichoderma reesei
60
-
 pH 5.0, 1 h, less than 20% loss of activity Trichoderma reesei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 using tributyrin as substrate at 37 °C, the enzyme shows optimum activity at pH 6 in the presence of 1 mM sodium taurodeoxycholate and 4 mM CaCl2 Trichoderma reesei

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 7 over 80% of the initial activity is retained between pH 4.0 and pH 7.4 after 20 h at 50°C Trichoderma reesei