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Literature summary for 3.1.1.74 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 3.1.1.74

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
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
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

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.
cutin + H2O apple cutin Trichoderma reesei cutin monomers
-
 ?
cutin + H2O apple cutin Trichoderma reesei QM6a cutin monomers
-
 ?

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
4
-
 the enzyme exhibits two local pH optima, one at pH 4.0 and the other one at pH 7.3 Trichoderma reesei
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

pH Minimum pH Maximum Comment Organism
3 8 active over a broad pH range 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