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Literature summary extracted from

  • Chen, S.; Tong, X.; Woodard, R.W.; Du, G.; Wu, J.; Chen, J.
    Identification and characterization of bacterial cutinase (2008), J. Biol. Chem., 283, 25854-25862.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 cloned and overexpressed in Escherichia coli cells Thermobifida fusca

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.3 S170A mutation of the putative catalytic serine to alanine completely eliminates activity Thermobifida fusca
3.1.1.3 S188A mutation of the putative catalytic serine to alanine completely eliminates activity Thermobifida fusca

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.3 29000
-
 SDS-PAGE analysis of proteins in the culture supernatant clearly indicates that a polypeptide of 29 kDa is the major protein induced by cutin, suggesting that it might be a candidate for cutinase protein Thermobifida fusca

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Thermobifida fusca Q47RJ6 Tfu_0883
-
3.1.1.3 Thermobifida fusca Q47RJ7 Tfu_0882
-
3.1.1.74 Fusarium solani
-
 pisi
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 ammonium sulfate precipitation, hydrophobic interaction (phenyl Sepharose), and anion exchange (DEAE-Sepharose) chromatography Thermobifida fusca

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 p-nitrophenyl butyrate + H2O
-
 Thermobifida fusca p-nitrophenol + butyrate
-
 ?
3.1.1.3 triolein + H2O
-
 Thermobifida fusca 1,2-diolein + oleate
-
 ?
3.1.1.74 cutin + H2O
-
 Fusarium solani cutin monomers main products: hexadecaoic acid, octadecaoic acid, and 10,16-dihydroxyhexadecaoic acid ?
3.1.1.74 p-nitrophenyl butyrate + H2O
-
 Fusarium solani p-nitrophenol + butyrate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 cutinase
-
 Thermobifida fusca
3.1.1.3 pNPB hydrolase
-
 Thermobifida fusca
3.1.1.74 cutinase
-
 Fusarium solani
3.1.1.74 fungal cutinase
-
 Fusarium solani

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 60
-
-
 Thermobifida fusca
3.1.1.74 30
-
 displays an optimal temperature at 30°C for triolein and 40°C for 4-nitrophenyl butyrate Fusarium solani
3.1.1.74 40
-
 displays an optimal temperature at 30°C for triolein and 40°C for 4-nitrophenyl butyrate Fusarium solani

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.3 20 70 temperature dependence of enzyme activity is determined between 20 and 70°C Thermobifida fusca
3.1.1.74 20 70 temperature dependence of enzyme activity is determined between 20 and 70°C Fusarium solani

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 40 60 thermostability is evaluated at both 40 and 60°C. Activity increases initially during incubation at both temperatures. It exhibits superior thermostability, with residual activities of over 80% after 160 h at 40°C or over 50% after 40 h at 60°C Thermobifida fusca
3.1.1.74 40 60 thermostability of Fusarium solani pisi cutinase is evaluated at both 40 and 60°C. It exhibits a similar initial increase at 40°C, but a simple exponential decay at 60°C. 50% of activity retained after 85 h at 40°C or after 5 min at 60°C Fusarium solani

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 8
-
-
 Thermobifida fusca
3.1.1.74 8
-
-
 Fusarium solani

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.3 6 9 pH dependence of enzyme activity is determined between pH 6.0 and 9.0 Thermobifida fusca
3.1.1.74 6 9 pH dependence of enzyme activity is determined between pH 6.0 and 9.0 Fusarium solani