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Literature summary for 3.1.1.74 extracted from
- Cutinase: characteristics, preparation, and application (2013), Biotechnol. Adv., 31, 1754-1767.
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | cutinase combined with alkaline pectinase or xylanase, can improve the degradation of cotton seed coat during the cotton fabric bioscouring process | Pseudomonas mendocina |
| additional information | cutinase combined with alkaline pectinase or xylanase, can improve the degradation of cotton seed coat during the cotton fabric bioscouring process. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability | Fusarium solani |
| additional information | cutinase combined with alkaline pectinase or xylanase, can improve the degradation of cotton seed coat during the cotton fabric bioscouring process. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability | Streptomyces acidiscabies |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| heterologous enzyme expression, mostly with secretion to the medium, in different hosts, e.g. Escherichia coli strain W6, Bacillus subtilis, Saccharomyces cerevisiae strain SU50, Pichia pastoris, Aspergillus awamori, and Fusarium venenatum, from different plasmids and using different promoters, and using different signal peptides, e.g. alkaline phosphatase (PhoA) signal peptide, LipA signal peptide, alpha-factor signal peptide, and Fusarium solani cutinase signal peptide, overview. Optimization of method and culture conditions | Fusarium solani |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| PDB ID 2CZQ, X-ray diffraction structure determination at 1.05 A resolution | Cryptococcus sp. (in: Fungi) |
| PDB ID: 3VIS, X-ray diffraction structure determination at 1.76 A resolution | Thermobifida alba |
| PDB IDs 1CUS and 2CUT, X-ray diffraction structure determination | Fusarium solani |
| PDB IDs 3GBS, 3PQD, X-ray diffraction structure determination at 1.75 A resolution | Aspergillus oryzae |
| PDB IDs: two inhibited structures 3DEA and 3DD5 and one uninhibited structure 3DCN | Colletotrichum gloeosporioides |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A164R | site-directed mutagenesis, the mutant shows 59% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| A185L | site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| A195S | site-directed mutagenesis, the mutant shows 62% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| A199C | site-directed mutagenesis, the mutant shows no activity in olive oil | Fusarium solani |
| A29S | site-directed mutagenesis, the mutant shows 36% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| A79G | site-directed mutagenesis, the mutant shows 50% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| A85F | site-directed mutagenesis, the mutant shows 36% increased activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| A85F | the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme | Fusarium solani |
| A85W | site-directed mutagenesis, the mutant shows 9% increased activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| A85W | the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme | Fusarium solani |
| D111N | site-directed mutagenesis, the mutant shows 61% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| D134S | site-directed mutagenesis, the mutant shows 63% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| D33S | site-directed mutagenesis, the mutant shows 26% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| D83S | site-directed mutagenesis, the mutant shows 38% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| E201K | site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| F52W | site-directed mutagenesis, the mutant shows increased activity with 4-nitrophenyl palmitate by 4.86fold and altered substrate specificity toward substrates with longer chain lengths | Cryptococcus sp. (in: Fungi) |
| G192Q | site-directed mutagenesis, the mutant shows 56% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| G26A | site-directed mutagenesis, the mutant shows 67% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| H137L | site-directed mutageneis, the mutant exhibits a slightly increased Km value with the soluble substrate 4-nitrophenyl butyrate compared to the wild-type enzyme | Monilinia fructicola |
| I183F | site-directed mutagenesis, the mutant shows 75% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| I204K | site-directed mutagenesis, the mutant shows 34% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| I24S | site-directed mutagenesis, the mutant shows 96% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| K151R | site-directed mutagenesis, the mutant shows 71% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| K168L | site-directed mutagenesis, the mutant shows 17% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| L114Y | site-directed mutagenesis, the mutant shows 80% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| L181F | site-directed mutagenesis, the mutant shows increased activity with 4-nitrophenyl palmitate by 4.86fold and altered substrate specificity toward substrates with longer chain lengths | Cryptococcus sp. (in: Fungi) |
| L182A | site-directed mutagenesis, the mutant shows activity enhancement of 5fold toward high-molecular weight PET fibers compared to the wild-type enzyme | Fusarium solani |
| L182W | site-directed mutagenesis, the mutant shows 81% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| L189F | site-directed mutagenesis, the mutant shows 9% increased activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| L189F | the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme | Fusarium solani |
| L81A | the mutant shows activity enhancement of 4fold toward high-molecular weight PET fibers compared to the wild-type enzyme | Fusarium solani |
| L99K | site-directed mutagenesis, the mutant shows 22% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| M98C | site-directed mutagenesis, the mutant shows 65% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| additional information | generation of a fusion protein, fusing cellobiohydrolase Is from Thermobifida fusca cellulase Cel6A (CBMCel6A) and Cellulomonas fimi cellulase CenA (CBMCenA), separately, to Thermobifida fusca cutinase. Both fusion proteins display catalytic properties and pH stabilities similar to those of Thermobifida fusca cutinase. Addition of pectinase enhances the cotton fiber binding activities of cutinase-CBMCel6A and cutinase-CBMCenA by 40%, and 45%, respectively. A dramatic increase of up to 3fold is observed in the amount of fatty acids released from cotton fiber by the combination of cutinase-CBM fusion proteins with pectinase | Thermobifida fusca |
| additional information | the cutinase id fused with binding modules from Hypocrea jecorina cellobiohydrolase I (CBM) and Alcaligenes faecalis polyhydroxyalkanoate depolymerase (PBM), respectively. The adsorption of the fusion enzymes to PET is increased, and PET hydrolysis activity of one of the fusions (Thc_Cut1 + CBM) is enhanced 3.8fold | Thermobifida cellulosilytica |
| additional information | the cutinase is fused with binding modules from Hypocrea jecorina cellobiohydrolase I (CBM) and Alcaligenes faecalis polyhydroxyalkanoate depolymerase (PBM), respectively. The adsorption of the fusion enzymes to PET is increased, and PET hydrolysis activity of one of the fusions (Thc_Cut1 + CBM) is enhanced 3.8fold | Thermobifida cellulosilytica |
| N161D | site-directed mutagenesis, the mutant shows 37% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| N172K | site-directed mutagenesis, the mutant shows 55% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| N84A | site-directed mutagenesis, the mutant shows 73.5% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| N84A | the mutant shows activity enhancement of 1.7fold toward high-molecular weight PET fibers compared to the wild-type enzyme | Fusarium solani |
| N84D | site-directed mutagenesis, the mutant shows almost no activity in olive oil | Fusarium solani |
| N84L | site-directed mutagenesis, the mutant shows 97% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| N84W | site-directed mutagenesis, the mutant shows almost no activity in olive oil | Fusarium solani |
| R156E | site-directed mutagenesis, the mutant shows 21% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R156K | site-directed mutagenesis, the mutant shows 15% increased activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R156L | site-directed mutagenesis, the mutant shows 29% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R17E | site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R17N | site-directed mutagenesis, the mutant shows 69% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R196E | site-directed mutagenesis, the mutant shows 55% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R196K | site-directed mutagenesis, the mutant shows 62% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R196L | site-directed mutagenesis, the mutant shows 56% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R19SS | the mutant shows strongly increased PET hydrolysis activity compared to the wild-type enzyme | Thermobifida cellulosilytica |
| R208A | site-directed mutagenesis, the mutant shows 36% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R29SS | the mutant shows strongly increased PET hydrolysis activity compared to the wild-type enzyme | Thermobifida cellulosilytica |
| R78L | site-directed mutagenesis, the mutant shows 51% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R78N | site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R88A | site-directed mutagenesis, the mutant shows 61% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| R96N | site-directed mutagenesis, the mutant shows 43% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| S103A | site-directed mutageneis, the mutant exhibits a slightly increased Km value and a 2.3fold higher kcat with the soluble substrate 4-nitrophenyl butyrate compared to the wild-type enzyme | Monilinia fructicola |
| S103T | site-directed mutageneis, the mutant exhibits a slightly increased Km valuet with the soluble substrate 4-nitrophenyl butyrate compared to the wild-type enzyme | Monilinia fructicola |
| S120A | site-directed mutagenesis, the mutant shows no activity in olive oil | Fusarium solani |
| S42A | site-directed mutagenesis, the mutant shows almost no activity in olive oil | Fusarium solani |
| S54E | site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| S54K | site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| S54W | site-directed mutagenesis, the mutant shows 11% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| S92R | site-directed mutagenesis, the mutant shows 50% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| T144C | site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| T167L | site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| T173K | site-directed mutagenesis, the mutant shows 19% increased activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| T173K | the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme | Fusarium solani |
| T179Y | site-directed mutagenesis, the mutant shows 31% increased activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| T179Y | the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme | Fusarium solani |
| T18V | site-directed mutagenesis, the mutant shows 10% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| T19V | site-directed mutagenesis, the mutant shows 65% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| T45A | site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| T45K | site-directed mutagenesis, the mutant shows 26% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| T50V | site-directed mutagenesis, the mutant shows 75% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| T80D | site-directed mutagenesis, the mutant shows 68% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| V184A | the mutant shows activity enhancement of 2fold toward high-molecular weight PET fibers compared to the wild-type enzyme | Fusarium solani |
| W69Y | site-directed mutagenesis, the mutant shows 88% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
| W86L | site-directed mutagenesis, the mutant exhibits an improvement in binding and catalytic efficiency of 1.4fold toward PET fiber compared with the wild-type enzyme | Thermobifida fusca |
| W86Y | site-directed mutagenesis, the mutant exhibits an improvement in binding and catalytic efficiency of 1.5fold toward PET fiber compared with the wild-type enzyme | Thermobifida fusca |
| Y38F | site-directed mutagenesis, the mutant shows 38% reduced activity in olive oil compared to the wild-type enzyme | Fusarium solani |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.127 | - |
4-nitrophenyl acetate | pH and temperature not specified in the publication | Thermobifida cellulosilytica |  |
| 0.167 | - |
4-nitrophenyl acetate | pH and temperature not specified in the publication | Thermobifida fusca | |
| 0.2 | - |
4-nitrophenyl acetate | pH and temperature not specified in the publication | Thermobifida cellulosilytica | |
| 0.213 | - |
4-nitrophenyl acetate | pH and temperature not specified in the publication | Thermobifida alba | |
| 55.3 | - |
4-nitrophenyl valerate | pH and temperature not specified in the publication | Aspergillus oryzae | |
| 59.2 | - |
4-nitrophenyl butyrate | pH and temperature not specified in the publication | Aspergillus oryzae | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Aspergillus niger | - |
- |
| extracellular | - |
Pseudomonas aeruginosa | - |
- |
| extracellular | - |
Pseudomonas putida | - |
- |
| extracellular | - |
Pseudomonas mendocina | - |
- |
| extracellular | - |
Humicola insolens | - |
- |
| extracellular | - |
Penicillium citrinum | - |
- |
| extracellular | - |
Colletotrichum gloeosporioides | - |
- |
| extracellular | - |
Bipolaris maydis | - |
- |
| extracellular | - |
Penicillium sp. | - |
- |
| extracellular | - |
Thermobifida fusca | - |
- |
| extracellular | - |
Fusarium oxysporum | - |
- |
| extracellular | - |
Thermoactinomyces vulgaris | - |
- |
| extracellular | - |
Rhizoctonia solani | - |
- |
| extracellular | - |
Fusarium sambucinum | - |
- |
| extracellular | - |
Venturia inaequalis | - |
- |
| extracellular | - |
Streptomyces scabiei | - |
- |
| extracellular | - |
Thermothielavioides terrestris | - |
- |
| extracellular | - |
Helminthosporium sativum | - |
- |
| extracellular | - |
Fusarium solani | - |
- |
| extracellular | - |
Alternaria brassicicola | - |
- |
| extracellular | - |
Coprinopsis cinerea | - |
- |
| extracellular | - |
Alternaria consortialis | - |
- |
| extracellular | - |
Aspergillus nidulans | - |
- |
| extracellular | - |
Monilinia fructicola | - |
- |
| extracellular | - |
Pyrenopeziza brassicae | - |
- |
| extracellular | - |
Botrytis cinerea | - |
- |
| extracellular | - |
Pyricularia grisea | - |
- |
| extracellular | - |
Aspergillus oryzae | - |
- |
| extracellular | - |
Moesziomyces antarcticus | - |
- |
| extracellular | - |
Streptomyces acidiscabies | - |
- |
| extracellular | - |
Streptomyces badius | - |
- |
| extracellular | - |
Thermobifida alba | - |
- |
| extracellular | - |
Thermobifida cellulosilytica | - |
- |
| extracellular | - |
Cryptococcus sp. (in: Fungi) | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cutin + H2O | Aspergillus niger | - |
cutin monomers | - |
? | |
| cutin + H2O | Pseudomonas aeruginosa | - |
cutin monomers | - |
? | |
| cutin + H2O | Pseudomonas putida | - |
cutin monomers | - |
? | |
| cutin + H2O | Pseudomonas mendocina | - |
cutin monomers | - |
? | |
| cutin + H2O | Humicola insolens | - |
cutin monomers | - |
? | |
| cutin + H2O | Penicillium citrinum | - |
cutin monomers | - |
? | |
| cutin + H2O | Colletotrichum gloeosporioides | - |
cutin monomers | - |
? | |
| cutin + H2O | Bipolaris maydis | - |
cutin monomers | - |
? | |
| cutin + H2O | Penicillium sp. | - |
cutin monomers | - |
? | |
| cutin + H2O | Fusarium oxysporum | - |
cutin monomers | - |
? | |
| cutin + H2O | Thermoactinomyces vulgaris | - |
cutin monomers | - |
? | |
| cutin + H2O | Rhizoctonia solani | - |
cutin monomers | - |
? | |
| cutin + H2O | Fusarium sambucinum | - |
cutin monomers | - |
? | |
| cutin + H2O | Venturia inaequalis | - |
cutin monomers | - |
? | |
| cutin + H2O | Streptomyces scabiei | - |
cutin monomers | - |
? | |
| cutin + H2O | Thermothielavioides terrestris | - |
cutin monomers | - |
? | |
| cutin + H2O | Helminthosporium sativum | - |
cutin monomers | - |
? | |
| cutin + H2O | Alternaria brassicicola | - |
cutin monomers | - |
? | |
| cutin + H2O | Coprinopsis cinerea | - |
cutin monomers | - |
? | |
| cutin + H2O | Alternaria consortialis | - |
cutin monomers | - |
? | |
| cutin + H2O | Aspergillus nidulans | - |
cutin monomers | - |
? | |
| cutin + H2O | Monilinia fructicola | - |
cutin monomers | - |
? | |
| cutin + H2O | Pyrenopeziza brassicae | - |
cutin monomers | - |
? | |
| cutin + H2O | Botrytis cinerea | - |
cutin monomers | - |
? | |
| cutin + H2O | Pyricularia grisea | - |
cutin monomers | - |
? | |
| cutin + H2O | Moesziomyces antarcticus | - |
cutin monomers | - |
? | |
| cutin + H2O | Streptomyces acidiscabies | - |
cutin monomers | - |
? | |
| cutin + H2O | Streptomyces badius | - |
cutin monomers | - |
? | |
| cutin + H2O | Thermobifida fusca | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | cutin monomers | - |
? | |
| cutin + H2O | Fusarium solani | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | cutin monomers | - |
? | |
| cutin + H2O | Aspergillus oryzae | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | cutin monomers | - |
? | |
| cutin + H2O | Thermobifida alba | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | cutin monomers | - |
? | |
| cutin + H2O | Thermobifida cellulosilytica | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | cutin monomers | - |
? | |
| cutin + H2O | Cryptococcus sp. (in: Fungi) | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | cutin monomers | - |
? | |
| cutin + H2O | Cryptococcus sp. (in: Fungi) S-2 | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | cutin monomers | - |
? | |
| cutin + H2O | Thermobifida fusca DSM 44342 | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | cutin monomers | - |
? | |
| additional information | Aspergillus niger | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Pseudomonas aeruginosa | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Pseudomonas putida | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Humicola insolens | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Penicillium citrinum | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Colletotrichum gloeosporioides | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Bipolaris maydis | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Penicillium sp. | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Thermobifida fusca | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Fusarium oxysporum | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Thermoactinomyces vulgaris | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Rhizoctonia solani | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Fusarium sambucinum | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Venturia inaequalis | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Streptomyces scabiei | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Thermothielavioides terrestris | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Helminthosporium sativum | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Alternaria brassicicola | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Coprinopsis cinerea | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Alternaria consortialis | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Aspergillus nidulans | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Monilinia fructicola | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Pyrenopeziza brassicae | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Botrytis cinerea | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Pyricularia grisea | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Aspergillus oryzae | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Moesziomyces antarcticus | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Streptomyces badius | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Thermobifida alba | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Thermobifida cellulosilytica | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Cryptococcus sp. (in: Fungi) | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Pseudomonas mendocina | cutinases are capable of catalyzing esterification and transesterification. The cuticle layer of a cotton fiber has a complicated composition that includes cutin, wax, pectin and protein, and both the wax and cutin can be hydrolysed by the cutinase | ? | - |
? | |
| additional information | Streptomyces acidiscabies | cutinases are capable of catalyzing esterification and transesterification. The cuticle layer of a cotton fiber has a complicated composition that includes cutin, wax, pectin and protein, and both the wax and cutin can be hydrolysed by the cutinase. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability | ? | - |
? | |
| additional information | Fusarium solani | cutinases are capable of catalyzing esterification and transesterification. The enzyme prefers triacylglyceride substrates with short acyl groups | ? | - |
? | |
| additional information | Cryptococcus sp. (in: Fungi) S-2 | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
| additional information | Thermobifida fusca DSM 44342 | cutinases are capable of catalyzing esterification and transesterification | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Alternaria brassicicola | - |
gene cut1, the organism harbors four cutinases | - |
| Alternaria consortialis | - |
- |
- |
| Aspergillus nidulans | Q5AVY9 | Cut2; isozyme Cut2, the organism harbors four cutinases | - |
| Aspergillus niger | - |
gene An09g00790, the organism harbors five cutinases | - |
| Aspergillus oryzae | P52956 | Cut1; gene cut1, the organism harbors two cutinases | - |
| Bipolaris maydis | - |
- |
- |
| Botrytis cinerea | Q00298 | Cut1; gene cutA, the organism harbors one cutinase | - |
| Colletotrichum gloeosporioides | - |
the organism harbors one cutinase | - |
| Colletotrichum gloeosporioides | P11373 | - |
- |
| Coprinopsis cinerea | B9U443 | - |
- |
| Cryptococcus sp. (in: Fungi) | Q874E9 | cutinase-like enzyme | - |
| Cryptococcus sp. (in: Fungi) S-2 | Q874E9 | cutinase-like enzyme | - |
| Fusarium oxysporum | - |
the organism harbors one cutinase | - |
| Fusarium sambucinum | - |
var. culmorum | - |
| Fusarium sambucinum | - |
var. sambucinum | - |
| Fusarium solani | P00590 | Cut1; gene cut1, the organism harbors two cutinases | - |
| Helminthosporium sativum | - |
- |
- |
| Humicola insolens | - |
- |
- |
| Moesziomyces antarcticus | M9M134 | gene PANT_9c00247; gene PANT_9c00247 | - |
| Monilinia fructicola | Q2VF46 | gene cut1, the organism harbors four cutinases | - |
| Penicillium citrinum | - |
- |
- |
| Penicillium sp. | - |
the organism harbors one cutinase | - |
| Pseudomonas aeruginosa | - |
- |
- |
| Pseudomonas mendocina | - |
- |
- |
| Pseudomonas putida | - |
- |
- |
| Pyrenopeziza brassicae | Q9Y7G8 | Cut1; gene cut1, the organism harbors one cutinase | - |
| Pyricularia grisea | P30272 | Cut1; gene cut1, the organism harbors five cutinases | - |
| Rhizoctonia solani | - |
- |
- |
| Streptomyces acidiscabies | - |
- |
- |
| Streptomyces badius | - |
- |
- |
| Streptomyces scabiei | - |
- |
- |
| Thermoactinomyces vulgaris | - |
- |
- |
| Thermobifida alba | E9LVH7 | Cut1; gene cut1, the organism harbors two cutinases | - |
| Thermobifida cellulosilytica | E9LVH8 | Cut1; gene cut1, the organsim harbors two cutinases | - |
| Thermobifida cellulosilytica | E9LVH9 | Cut2; gene cut2, the organism harbors two cutinases | - |
| Thermobifida fusca | - |
Cut1 | - |
| Thermobifida fusca DSM 44342 | - |
Cut1 | - |
| Thermothielavioides terrestris | - |
- |
- |
| Venturia inaequalis | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| conidium | ungerminated | Botrytis cinerea | - |
| additional information | optimization of culture conditions for heterologous expression of the enzyme, overview | Fusarium solani | - |
| additional information | production of Fusarium oxysporum cutinase by solid-state fermentation using Brazilian agricultural by-products, with maximum yield 21.7 U/mL after 120 h of fermentation at 28.3°C | Fusarium oxysporum | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl acetate + H2O | - |
Thermobifida fusca | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Fusarium solani | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Aspergillus oryzae | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Streptomyces acidiscabies | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Thermobifida alba | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Thermobifida cellulosilytica | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Thermobifida fusca DSM 44342 | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Thermobifida fusca | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Thermoactinomyces vulgaris | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Fusarium solani | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Aspergillus nidulans | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Monilinia fructicola | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Aspergillus oryzae | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Streptomyces acidiscabies | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Streptomyces badius | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Thermobifida fusca DSM 44342 | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl hexanoate + H2O | - |
Fusarium solani | 4-nitrophenol + hexanoate | - |
? | |
| 4-nitrophenyl hexanoate + H2O | - |
Aspergillus oryzae | 4-nitrophenol + hexanoate | - |
? | |
| 4-nitrophenyl palmitate + H2O | - |
Cryptococcus sp. (in: Fungi) | 4-nitrophenol + palmitate | - |
? | |
| 4-nitrophenyl palmitate + H2O | - |
Cryptococcus sp. (in: Fungi) S-2 | 4-nitrophenol + palmitate | - |
? | |
| 4-nitrophenyl valerate + H2O | - |
Fusarium solani | 4-nitrophenol + valerate | - |
? | |
| 4-nitrophenyl valerate + H2O | - |
Aspergillus oryzae | 4-nitrophenol + valerate | - |
? | |
| cutin + H2O | - |
Aspergillus niger | cutin monomers | - |
? | |
| cutin + H2O | - |
Pseudomonas aeruginosa | cutin monomers | - |
? | |
| cutin + H2O | - |
Pseudomonas putida | cutin monomers | - |
? | |
| cutin + H2O | - |
Pseudomonas mendocina | cutin monomers | - |
? | |
| cutin + H2O | - |
Humicola insolens | cutin monomers | - |
? | |
| cutin + H2O | - |
Penicillium citrinum | cutin monomers | - |
? | |
| cutin + H2O | - |
Colletotrichum gloeosporioides | cutin monomers | - |
? | |
| cutin + H2O | - |
Bipolaris maydis | cutin monomers | - |
? | |
| cutin + H2O | - |
Penicillium sp. | cutin monomers | - |
? | |
| cutin + H2O | - |
Thermobifida fusca | cutin monomers | - |
? | |
| cutin + H2O | - |
Fusarium oxysporum | cutin monomers | - |
? | |
| cutin + H2O | - |
Thermoactinomyces vulgaris | cutin monomers | - |
? | |
| cutin + H2O | - |
Rhizoctonia solani | cutin monomers | - |
? | |
| cutin + H2O | - |
Fusarium sambucinum | cutin monomers | - |
? | |
| cutin + H2O | - |
Venturia inaequalis | cutin monomers | - |
? | |
| cutin + H2O | - |
Streptomyces scabiei | cutin monomers | - |
? | |
| cutin + H2O | - |
Thermothielavioides terrestris | cutin monomers | - |
? | |
| cutin + H2O | - |
Helminthosporium sativum | cutin monomers | - |
? | |
| cutin + H2O | - |
Fusarium solani | cutin monomers | - |
? | |
| cutin + H2O | - |
Alternaria brassicicola | cutin monomers | - |
? | |
| cutin + H2O | - |
Coprinopsis cinerea | cutin monomers | - |
? | |
| cutin + H2O | - |
Alternaria consortialis | cutin monomers | - |
? | |
| cutin + H2O | - |
Aspergillus nidulans | cutin monomers | - |
? | |
| cutin + H2O | - |
Monilinia fructicola | cutin monomers | - |
? | |
| cutin + H2O | - |
Pyrenopeziza brassicae | cutin monomers | - |
? | |
| cutin + H2O | - |
Botrytis cinerea | cutin monomers | - |
? | |
| cutin + H2O | - |
Pyricularia grisea | cutin monomers | - |
? | |
| cutin + H2O | - |
Aspergillus oryzae | cutin monomers | - |
? | |
| cutin + H2O | - |
Moesziomyces antarcticus | cutin monomers | - |
? | |
| cutin + H2O | - |
Streptomyces acidiscabies | cutin monomers | - |
? | |
| cutin + H2O | - |
Streptomyces badius | cutin monomers | - |
? | |
| cutin + H2O | - |
Thermobifida alba | cutin monomers | - |
? | |
| cutin + H2O | - |
Thermobifida cellulosilytica | cutin monomers | - |
? | |
| cutin + H2O | - |
Cryptococcus sp. (in: Fungi) | cutin monomers | - |
? | |
| cutin + H2O | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | Thermobifida fusca | cutin monomers | - |
? | |
| cutin + H2O | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | Fusarium solani | cutin monomers | - |
? | |
| cutin + H2O | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | Aspergillus oryzae | cutin monomers | - |
? | |
| cutin + H2O | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | Thermobifida alba | cutin monomers | - |
? | |
| cutin + H2O | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | Thermobifida cellulosilytica | cutin monomers | - |
? | |
| cutin + H2O | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | Cryptococcus sp. (in: Fungi) | cutin monomers | - |
? | |
| cutin + H2O | - |
Cryptococcus sp. (in: Fungi) S-2 | cutin monomers | - |
? | |
| cutin + H2O | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | Cryptococcus sp. (in: Fungi) S-2 | cutin monomers | - |
? | |
| cutin + H2O | - |
Thermobifida fusca DSM 44342 | cutin monomers | - |
? | |
| cutin + H2O | cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed | Thermobifida fusca DSM 44342 | cutin monomers | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Aspergillus niger | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Pseudomonas aeruginosa | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Pseudomonas putida | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Humicola insolens | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Penicillium citrinum | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Colletotrichum gloeosporioides | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Bipolaris maydis | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Penicillium sp. | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Thermobifida fusca | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Fusarium oxysporum | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Thermoactinomyces vulgaris | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Rhizoctonia solani | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Fusarium sambucinum | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Venturia inaequalis | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Streptomyces scabiei | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Thermothielavioides terrestris | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Helminthosporium sativum | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Alternaria brassicicola | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Coprinopsis cinerea | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Alternaria consortialis | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Aspergillus nidulans | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Monilinia fructicola | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Pyrenopeziza brassicae | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Botrytis cinerea | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Pyricularia grisea | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Aspergillus oryzae | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Moesziomyces antarcticus | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Streptomyces badius | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Thermobifida alba | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Thermobifida cellulosilytica | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Cryptococcus sp. (in: Fungi) | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification. The cuticle layer of a cotton fiber has a complicated composition that includes cutin, wax, pectin and protein, and both the wax and cutin can be hydrolysed by the cutinase | Pseudomonas mendocina | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification. The cuticle layer of a cotton fiber has a complicated composition that includes cutin, wax, pectin and protein, and both the wax and cutin can be hydrolysed by the cutinase. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability | Streptomyces acidiscabies | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification. The enzyme prefers triacylglyceride substrates with short acyl groups | Fusarium solani | ? | - |
? | |
| additional information | the cuticle layer of a cotton fiber has a complicated composition that includes cutin, wax, pectin and protein, and both the wax and cutin can be hydrolysed by the cutinase. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability | Fusarium solani | ? | - |
? | |
| additional information | the enzyme hydrolyzes synthetic polyesters, including Ecoflex, poly(caprolactone), poly(butylene succinate-coadipate), poly(butylene succinate), poly(L-lactic acid) and poly(D-lactic acid), but not poly(3-hydroxybutyric acid) | Thermobifida alba | ? | - |
? | |
| additional information | the optimum ratio of butyrate, acetate, and lactate is 4:1:3 | Streptomyces acidiscabies | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Cryptococcus sp. (in: Fungi) S-2 | ? | - |
? | |
| additional information | cutinases are capable of catalyzing esterification and transesterification | Thermobifida fusca DSM 44342 | ? | - |
? | |
| tributyrin + H2O | - |
Fusarium solani | butyric acid + 1,2-dibutyrylglycerol | - |
? | |
| trioctanoin + H2O | - |
Fusarium solani | ? | - |
? | |
| triolein + H2O | - |
Fusarium solani | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CLE | - |
Cryptococcus sp. (in: Fungi) |
| Cut1 | - |
Thermobifida fusca |
| Cut1 | - |
Botrytis cinerea |
| Cut1 | - |
Pyricularia grisea |
| Cut1 | - |
Thermobifida cellulosilytica |
| cutinase 1 | - |
Fusarium sambucinum |
| cutinase 1 | - |
Fusarium solani |
| cutinase 1 | - |
Aspergillus oryzae |
| cutinase 1 | - |
Thermobifida alba |
| cutinase 1 | - |
Thermobifida cellulosilytica |
| cutinase 2 | - |
Aspergillus nidulans |
| cutinase 2 | - |
Thermobifida cellulosilytica |
| cutinase-like enzyme | - |
Cryptococcus sp. (in: Fungi) |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.4 | - |
4-nitrophenyl acetate | pH and temperature not specified in the publication | Thermobifida cellulosilytica | |
| 2.72 | - |
4-nitrophenyl acetate | pH and temperature not specified in the publication | Thermobifida alba | |
| 39.5 | - |
4-nitrophenyl acetate | pH and temperature not specified in the publication | Thermobifida fusca | |
| 211.9 | - |
4-nitrophenyl acetate | pH and temperature not specified in the publication | Thermobifida cellulosilytica | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Thermobifida fusca | increased enzyme production in strain WSH03-11 by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. tomato peel | up |
| Aspergillus nidulans | increased enzyme production in wild-type strain by induction induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. olive oil | up |
| Streptomyces acidiscabies | increased enzyme production in wild-type strain by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. apple cutin | up |
| Streptomyces badius | increased enzyme production in wild-type strain by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. apple cutin | up |
| Thermoactinomyces vulgaris | increased enzyme production in wild-type strain by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. tomato peel | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Aspergillus niger |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Pseudomonas aeruginosa |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Pseudomonas putida |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Pseudomonas mendocina |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Humicola insolens |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Penicillium citrinum |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Colletotrichum gloeosporioides |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Bipolaris maydis |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Penicillium sp. |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Thermobifida fusca |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Fusarium oxysporum |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Thermoactinomyces vulgaris |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Rhizoctonia solani |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Fusarium sambucinum |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Venturia inaequalis |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Streptomyces scabiei |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Thermothielavioides terrestris |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Helminthosporium sativum |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Fusarium solani |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Alternaria brassicicola |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Coprinopsis cinerea |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Alternaria consortialis |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Aspergillus nidulans |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Monilinia fructicola |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Pyrenopeziza brassicae |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Botrytis cinerea |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Pyricularia grisea |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Aspergillus oryzae |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Moesziomyces antarcticus |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Streptomyces acidiscabies |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Streptomyces badius |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Thermobifida cellulosilytica |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters | Cryptococcus sp. (in: Fungi) |
| evolution | cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters. The cutinase from Thermobifida alba also adopts an alpha/beta fold, but it is larger than the ones from other family members. It contains nine sheets at the heart of the protein, two of which are antiparallel, rather than the five parallel sheets present in the fungal enzymes | Thermobifida alba |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Aspergillus niger |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Humicola insolens |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Penicillium citrinum |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Colletotrichum gloeosporioides |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Bipolaris maydis |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Penicillium sp. |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Fusarium oxysporum |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Rhizoctonia solani |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Fusarium sambucinum |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Venturia inaequalis |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Thermothielavioides terrestris |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Helminthosporium sativum |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Fusarium solani |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Alternaria brassicicola |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Coprinopsis cinerea |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Alternaria consortialis |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Aspergillus nidulans |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Monilinia fructicola |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Pyrenopeziza brassicae |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Botrytis cinerea |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Pyricularia grisea |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Aspergillus oryzae |
| malfunction | specific inhibition of the enzyme blocks infectivity in several pathogen/host systems | Moesziomyces antarcticus |
| additional information | structure-activity relationship analysis, active site structure, the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S120, H188, D175, and key residues in the oxyanion hole, S42 and Q121, are important for stabilizing the transitions states in the acylation/deacylation steps of the enzyme mechanism | Fusarium solani |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Aspergillus niger |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Pseudomonas aeruginosa |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Pseudomonas putida |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Pseudomonas mendocina |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Humicola insolens |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Penicillium citrinum |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Colletotrichum gloeosporioides |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Bipolaris maydis |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Penicillium sp. |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Thermobifida fusca |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Fusarium oxysporum |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Thermoactinomyces vulgaris |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Rhizoctonia solani |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Fusarium sambucinum |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Venturia inaequalis |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Streptomyces scabiei |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Thermothielavioides terrestris |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Helminthosporium sativum |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Alternaria brassicicola |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Coprinopsis cinerea |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Alternaria consortialis |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Aspergillus nidulans |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Pyrenopeziza brassicae |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Botrytis cinerea |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Pyricularia grisea |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Moesziomyces antarcticus |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Streptomyces acidiscabies |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Streptomyces badius |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent | Thermobifida cellulosilytica |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S126, H194, and D181, and key residues in the oxyanion hole, S48 and Q127 | Aspergillus oryzae |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S169, H247, and D215, and key residues in the oxyanion hole, M179 and Y99, active site structure, overview | Thermobifida alba |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S85, H180, and D165, and key residues in the oxyanion hole, T17 and Q86 | Cryptococcus sp. (in: Fungi) |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Residues S103 and H173 from Monilinia fructicola cutinase play important roles in catalysis | Monilinia fructicola |
| additional information | the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. The conformation of the Glomerella cingulata catalytic triad appears to cycle between an inactive form and an active form during catalysis. In the uninhibited structure, the histidine residue that forms the center of the catalytic triad is positioned outside of the active site, and does not interact with the remainder of the triad, catalytic serine and catalytic aspartate. In addition, there is a small helix in the vicinity of the active site that places the catalytic serine in a deep hole in a deep pocketwithin the active site | Colletotrichum gloeosporioides |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Aspergillus niger |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Humicola insolens |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Penicillium citrinum |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Colletotrichum gloeosporioides |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Bipolaris maydis |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Penicillium sp. |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Fusarium oxysporum |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Rhizoctonia solani |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Fusarium sambucinum |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Venturia inaequalis |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Thermothielavioides terrestris |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Helminthosporium sativum |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Fusarium solani |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Alternaria brassicicola |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Coprinopsis cinerea |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Alternaria consortialis |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Aspergillus nidulans |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Monilinia fructicola |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Pyrenopeziza brassicae |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Botrytis cinerea |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Pyricularia grisea |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Aspergillus oryzae |
| physiological function | role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase | Moesziomyces antarcticus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 42.4 | - |
4-nitrophenyl acetate | pH and temperature not specified in the publication | Fusarium solani | |
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