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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3
-
 Trichoderma reesei
3.1.1.74
-
 Trichoderma reesei

Crystallization (Commentary)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.3 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
3.1.1.3 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
3.1.1.74 butyl 4-nitrophenyl undecylphosphonate 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
3.1.1.74 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

EC Number Metals/Ions Comment Organism Structure
3.1.1.3 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.3 23748
-
 matrix-assisted laser desorption-ionization/time-of-flight mass spectrometry Trichoderma reesei
3.1.1.74 23748
-
 matrix-assisted laser desorption-ionization/time-of-flight mass spectrometry Trichoderma reesei

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Trichoderma reesei G0RH85
-
-
3.1.1.3 Trichoderma reesei QM6a G0RH85
-
-
3.1.1.74 Trichoderma reesei G0RH85
-
-
3.1.1.74 Trichoderma reesei QM6a G0RH85
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.3 proteolytic modification cleavage of a propeptide Trichoderma reesei
3.1.1.74 proteolytic modification cleavage of a propeptide Trichoderma reesei

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3
-
 Trichoderma reesei
3.1.1.74
-
 Trichoderma reesei

Renatured (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 olive oil + H2O
-
 Trichoderma reesei ?
-
 ?
3.1.1.3 olive oil + H2O
-
 Trichoderma reesei QM6a ?
-
 ?
3.1.1.3 tributyrin + 3 H2O
-
 Trichoderma reesei glycerol + 3 butyrate
-
 ?
3.1.1.3 tributyrin + 3 H2O
-
 Trichoderma reesei QM6a glycerol + 3 butyrate
-
 ?
3.1.1.3 vinyl butyrate + H2O
-
 Trichoderma reesei ?
-
 ?
3.1.1.3 vinyl butyrate + H2O
-
 Trichoderma reesei QM6a ?
-
 ?
3.1.1.74 cutin + H2O apple cutin Trichoderma reesei cutin monomers
-
 ?
3.1.1.74 cutin + H2O apple cutin Trichoderma reesei QM6a cutin monomers
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 50
-
 pH 5.0, 20 h, less than 20% loss of activity Trichoderma reesei
3.1.1.3 60
-
 pH 5.0, 1 h, less than 20% loss of activity Trichoderma reesei
3.1.1.74 50
-
 pH 5.0, 20 h, less than 20% loss of activity Trichoderma reesei
3.1.1.74 60
-
 pH 5.0, 1 h, less than 20% loss of activity Trichoderma reesei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 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
3.1.1.74 4
-
 the enzyme exhibits two local pH optima, one at pH 4.0 and the other one at pH 7.3 Trichoderma reesei
3.1.1.74 7.3
-
 the enzyme exhibits two local pH optima, one at pH 4.0 and the other one at pH 7.3 Trichoderma reesei

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.74 3 8 active over a broad pH range Trichoderma reesei

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.3 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
3.1.1.74 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