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Literature summary extracted from

  • Chen, S.; Su, L.; Chen, J.; Wu, J.
    Cutinase: characteristics, preparation, and application (2013), Biotechnol. Adv., 31, 1754-1767.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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)

EC Number Cloned (Comment) Organism
3.1.1.74 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)

EC Number Crystallization (Comment) Organism
3.1.1.74 PDB ID 2CZQ, X-ray diffraction structure determination at 1.05 A resolution Cryptococcus sp. (in: Fungi)
3.1.1.74 PDB ID: 3VIS, X-ray diffraction structure determination at 1.76 A resolution Thermobifida alba
3.1.1.74 PDB IDs 1CUS and 2CUT, X-ray diffraction structure determination Fusarium solani
3.1.1.74 PDB IDs 3GBS, 3PQD, X-ray diffraction structure determination at 1.75 A resolution Aspergillus oryzae
3.1.1.74 PDB IDs: two inhibited structures 3DEA and 3DD5 and one uninhibited structure 3DCN Colletotrichum gloeosporioides

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.74 A164R site-directed mutagenesis, the mutant shows 59% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 A185L site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 A195S site-directed mutagenesis, the mutant shows 62% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 A199C site-directed mutagenesis, the mutant shows no activity in olive oil Fusarium solani
3.1.1.74 A29S site-directed mutagenesis, the mutant shows 36% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 A79G site-directed mutagenesis, the mutant shows 50% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 A85F site-directed mutagenesis, the mutant shows 36% increased activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 A85F the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme Fusarium solani
3.1.1.74 A85W site-directed mutagenesis, the mutant shows 9% increased activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 A85W the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme Fusarium solani
3.1.1.74 D111N site-directed mutagenesis, the mutant shows 61% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 D134S site-directed mutagenesis, the mutant shows 63% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 D33S site-directed mutagenesis, the mutant shows 26% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 D83S site-directed mutagenesis, the mutant shows 38% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 E201K site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 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)
3.1.1.74 G192Q site-directed mutagenesis, the mutant shows 56% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 G26A site-directed mutagenesis, the mutant shows 67% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 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
3.1.1.74 I183F site-directed mutagenesis, the mutant shows 75% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 I204K site-directed mutagenesis, the mutant shows 34% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 I24S site-directed mutagenesis, the mutant shows 96% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 K151R site-directed mutagenesis, the mutant shows 71% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 K168L site-directed mutagenesis, the mutant shows 17% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 L114Y site-directed mutagenesis, the mutant shows 80% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 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)
3.1.1.74 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
3.1.1.74 L182W site-directed mutagenesis, the mutant shows 81% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 L189F site-directed mutagenesis, the mutant shows 9% increased activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 L189F the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme Fusarium solani
3.1.1.74 L81A the mutant shows activity enhancement of 4fold toward high-molecular weight PET fibers compared to the wild-type enzyme Fusarium solani
3.1.1.74 L99K site-directed mutagenesis, the mutant shows 22% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 M98C site-directed mutagenesis, the mutant shows 65% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 N161D site-directed mutagenesis, the mutant shows 37% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 N172K site-directed mutagenesis, the mutant shows 55% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 N84A site-directed mutagenesis, the mutant shows 73.5% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 N84A the mutant shows activity enhancement of 1.7fold toward high-molecular weight PET fibers compared to the wild-type enzyme Fusarium solani
3.1.1.74 N84D site-directed mutagenesis, the mutant shows almost no activity in olive oil Fusarium solani
3.1.1.74 N84L site-directed mutagenesis, the mutant shows 97% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 N84W site-directed mutagenesis, the mutant shows almost no activity in olive oil Fusarium solani
3.1.1.74 R156E site-directed mutagenesis, the mutant shows 21% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R156K site-directed mutagenesis, the mutant shows 15% increased activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R156L site-directed mutagenesis, the mutant shows 29% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R17E site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R17N site-directed mutagenesis, the mutant shows 69% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R196E site-directed mutagenesis, the mutant shows 55% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R196K site-directed mutagenesis, the mutant shows 62% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R196L site-directed mutagenesis, the mutant shows 56% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R19SS the mutant shows strongly increased PET hydrolysis activity compared to the wild-type enzyme Thermobifida cellulosilytica
3.1.1.74 R208A site-directed mutagenesis, the mutant shows 36% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R29SS the mutant shows strongly increased PET hydrolysis activity compared to the wild-type enzyme Thermobifida cellulosilytica
3.1.1.74 R78L site-directed mutagenesis, the mutant shows 51% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R78N site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R88A site-directed mutagenesis, the mutant shows 61% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 R96N site-directed mutagenesis, the mutant shows 43% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 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
3.1.1.74 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
3.1.1.74 S120A site-directed mutagenesis, the mutant shows no activity in olive oil Fusarium solani
3.1.1.74 S42A site-directed mutagenesis, the mutant shows almost no activity in olive oil Fusarium solani
3.1.1.74 S54E site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 S54K site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 S54W site-directed mutagenesis, the mutant shows 11% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 S92R site-directed mutagenesis, the mutant shows 50% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 T144C site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 T167L site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 T173K site-directed mutagenesis, the mutant shows 19% increased activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 T173K the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme Fusarium solani
3.1.1.74 T179Y site-directed mutagenesis, the mutant shows 31% increased activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 T179Y the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme Fusarium solani
3.1.1.74 T18V site-directed mutagenesis, the mutant shows 10% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 T19V site-directed mutagenesis, the mutant shows 65% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 T45A site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 T45K site-directed mutagenesis, the mutant shows 26% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 T50V site-directed mutagenesis, the mutant shows 75% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 T80D site-directed mutagenesis, the mutant shows 68% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 V184A the mutant shows activity enhancement of 2fold toward high-molecular weight PET fibers compared to the wild-type enzyme Fusarium solani
3.1.1.74 W69Y site-directed mutagenesis, the mutant shows 88% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani
3.1.1.74 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
3.1.1.74 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
3.1.1.74 Y38F site-directed mutagenesis, the mutant shows 38% reduced activity in olive oil compared to the wild-type enzyme Fusarium solani

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.74 0.127
-
 4-nitrophenyl acetate pH and temperature not specified in the publication Thermobifida cellulosilytica
3.1.1.74 0.167
-
 4-nitrophenyl acetate pH and temperature not specified in the publication Thermobifida fusca
3.1.1.74 0.2
-
 4-nitrophenyl acetate pH and temperature not specified in the publication Thermobifida cellulosilytica
3.1.1.74 0.213
-
 4-nitrophenyl acetate pH and temperature not specified in the publication Thermobifida alba
3.1.1.74 55.3
-
 4-nitrophenyl valerate pH and temperature not specified in the publication Aspergillus oryzae
3.1.1.74 59.2
-
 4-nitrophenyl butyrate pH and temperature not specified in the publication Aspergillus oryzae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.74 extracellular
-
 Aspergillus niger
-
-
3.1.1.74 extracellular
-
 Pseudomonas aeruginosa
-
-
3.1.1.74 extracellular
-
 Pseudomonas putida
-
-
3.1.1.74 extracellular
-
 Pseudomonas mendocina
-
-
3.1.1.74 extracellular
-
 Humicola insolens
-
-
3.1.1.74 extracellular
-
 Penicillium citrinum
-
-
3.1.1.74 extracellular
-
 Colletotrichum gloeosporioides
-
-
3.1.1.74 extracellular
-
 Bipolaris maydis
-
-
3.1.1.74 extracellular
-
 Penicillium sp.
-
-
3.1.1.74 extracellular
-
 Thermobifida fusca
-
-
3.1.1.74 extracellular
-
 Fusarium oxysporum
-
-
3.1.1.74 extracellular
-
 Thermoactinomyces vulgaris
-
-
3.1.1.74 extracellular
-
 Rhizoctonia solani
-
-
3.1.1.74 extracellular
-
 Fusarium sambucinum
-
-
3.1.1.74 extracellular
-
 Venturia inaequalis
-
-
3.1.1.74 extracellular
-
 Streptomyces scabiei
-
-
3.1.1.74 extracellular
-
 Thermothielavioides terrestris
-
-
3.1.1.74 extracellular
-
 Helminthosporium sativum
-
-
3.1.1.74 extracellular
-
 Fusarium solani
-
-
3.1.1.74 extracellular
-
 Alternaria brassicicola
-
-
3.1.1.74 extracellular
-
 Coprinopsis cinerea
-
-
3.1.1.74 extracellular
-
 Alternaria consortialis
-
-
3.1.1.74 extracellular
-
 Aspergillus nidulans
-
-
3.1.1.74 extracellular
-
 Monilinia fructicola
-
-
3.1.1.74 extracellular
-
 Pyrenopeziza brassicae
-
-
3.1.1.74 extracellular
-
 Botrytis cinerea
-
-
3.1.1.74 extracellular
-
 Pyricularia grisea
-
-
3.1.1.74 extracellular
-
 Aspergillus oryzae
-
-
3.1.1.74 extracellular
-
 Moesziomyces antarcticus
-
-
3.1.1.74 extracellular
-
 Streptomyces acidiscabies
-
-
3.1.1.74 extracellular
-
 Streptomyces badius
-
-
3.1.1.74 extracellular
-
 Thermobifida alba
-
-
3.1.1.74 extracellular
-
 Thermobifida cellulosilytica
-
-
3.1.1.74 extracellular
-
 Cryptococcus sp. (in: Fungi)
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.74 cutin + H2O Aspergillus niger
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Pseudomonas aeruginosa
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Pseudomonas putida
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Pseudomonas mendocina
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Humicola insolens
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Penicillium citrinum
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Colletotrichum gloeosporioides
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Bipolaris maydis
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Penicillium sp.
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Fusarium oxysporum
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Thermoactinomyces vulgaris
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Rhizoctonia solani
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Fusarium sambucinum
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Venturia inaequalis
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Streptomyces scabiei
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Thermothielavioides terrestris
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Helminthosporium sativum
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Alternaria brassicicola
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Coprinopsis cinerea
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Alternaria consortialis
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Aspergillus nidulans
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Monilinia fructicola
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Pyrenopeziza brassicae
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Botrytis cinerea
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Pyricularia grisea
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Moesziomyces antarcticus
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Streptomyces acidiscabies
-
 cutin monomers
-
 ?
3.1.1.74 cutin + H2O Streptomyces badius
-
 cutin monomers
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 additional information Aspergillus niger cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Pseudomonas aeruginosa cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Pseudomonas putida cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Humicola insolens cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Penicillium citrinum cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Colletotrichum gloeosporioides cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Bipolaris maydis cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Penicillium sp. cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Thermobifida fusca cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Fusarium oxysporum cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Thermoactinomyces vulgaris cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Rhizoctonia solani cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Fusarium sambucinum cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Venturia inaequalis cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Streptomyces scabiei cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Thermothielavioides terrestris cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Helminthosporium sativum cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Alternaria brassicicola cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Coprinopsis cinerea cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Alternaria consortialis cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Aspergillus nidulans cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Monilinia fructicola cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Pyrenopeziza brassicae cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Botrytis cinerea cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Pyricularia grisea cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Aspergillus oryzae cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Moesziomyces antarcticus cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Streptomyces badius cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Thermobifida alba cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Thermobifida cellulosilytica cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Cryptococcus sp. (in: Fungi) cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 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 ?
-
 ?
3.1.1.74 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 ?
-
 ?
3.1.1.74 additional information Fusarium solani cutinases are capable of catalyzing esterification and transesterification. The enzyme prefers triacylglyceride substrates with short acyl groups ?
-
 ?
3.1.1.74 additional information Cryptococcus sp. (in: Fungi) S-2 cutinases are capable of catalyzing esterification and transesterification ?
-
 ?
3.1.1.74 additional information Thermobifida fusca DSM 44342 cutinases are capable of catalyzing esterification and transesterification ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.74 Alternaria brassicicola
-
 gene cut1, the organism harbors four cutinases
-
3.1.1.74 Alternaria consortialis
-
-
-
3.1.1.74 Aspergillus nidulans Q5AVY9 Cut2; isozyme Cut2, the organism harbors four cutinases
-
3.1.1.74 Aspergillus niger
-
 gene An09g00790, the organism harbors five cutinases
-
3.1.1.74 Aspergillus oryzae P52956 Cut1; gene cut1, the organism harbors two cutinases
-
3.1.1.74 Bipolaris maydis
-
-
-
3.1.1.74 Botrytis cinerea Q00298 Cut1; gene cutA, the organism harbors one cutinase
-
3.1.1.74 Colletotrichum gloeosporioides
-
 the organism harbors one cutinase
-
3.1.1.74 Colletotrichum gloeosporioides P11373
-
-
3.1.1.74 Coprinopsis cinerea B9U443
-
-
3.1.1.74 Cryptococcus sp. (in: Fungi) Q874E9 cutinase-like enzyme
-
3.1.1.74 Cryptococcus sp. (in: Fungi) S-2 Q874E9 cutinase-like enzyme
-
3.1.1.74 Fusarium oxysporum
-
 the organism harbors one cutinase
-
3.1.1.74 Fusarium sambucinum
-
 var. culmorum
-
3.1.1.74 Fusarium sambucinum
-
 var. sambucinum
-
3.1.1.74 Fusarium solani P00590 Cut1; gene cut1, the organism harbors two cutinases
-
3.1.1.74 Helminthosporium sativum
-
-
-
3.1.1.74 Humicola insolens
-
-
-
3.1.1.74 Moesziomyces antarcticus M9M134 gene PANT_9c00247; gene PANT_9c00247
-
3.1.1.74 Monilinia fructicola Q2VF46 gene cut1, the organism harbors four cutinases
-
3.1.1.74 Penicillium citrinum
-
-
-
3.1.1.74 Penicillium sp.
-
 the organism harbors one cutinase
-
3.1.1.74 Pseudomonas aeruginosa
-
-
-
3.1.1.74 Pseudomonas mendocina
-
-
-
3.1.1.74 Pseudomonas putida
-
-
-
3.1.1.74 Pyrenopeziza brassicae Q9Y7G8 Cut1; gene cut1, the organism harbors one cutinase
-
3.1.1.74 Pyricularia grisea P30272 Cut1; gene cut1, the organism harbors five cutinases
-
3.1.1.74 Rhizoctonia solani
-
-
-
3.1.1.74 Streptomyces acidiscabies
-
-
-
3.1.1.74 Streptomyces badius
-
-
-
3.1.1.74 Streptomyces scabiei
-
-
-
3.1.1.74 Thermoactinomyces vulgaris
-
-
-
3.1.1.74 Thermobifida alba E9LVH7 Cut1; gene cut1, the organism harbors two cutinases
-
3.1.1.74 Thermobifida cellulosilytica E9LVH8 Cut1; gene cut1, the organsim harbors two cutinases
-
3.1.1.74 Thermobifida cellulosilytica E9LVH9 Cut2; gene cut2, the organism harbors two cutinases
-
3.1.1.74 Thermobifida fusca
-
 Cut1
-
3.1.1.74 Thermobifida fusca DSM 44342
-
 Cut1
-
3.1.1.74 Thermothielavioides terrestris
-
-
-
3.1.1.74 Venturia inaequalis
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.74 conidium ungerminated Botrytis cinerea
-
3.1.1.74 additional information optimization of culture conditions for heterologous expression of the enzyme, overview Fusarium solani
-
3.1.1.74 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.74 4-nitrophenyl acetate + H2O
-
 Thermobifida fusca 4-nitrophenol + acetate
-
 ?
3.1.1.74 4-nitrophenyl acetate + H2O
-
 Fusarium solani 4-nitrophenol + acetate
-
 ?
3.1.1.74 4-nitrophenyl acetate + H2O
-
 Aspergillus oryzae 4-nitrophenol + acetate
-
 ?
3.1.1.74 4-nitrophenyl acetate + H2O
-
 Streptomyces acidiscabies 4-nitrophenol + acetate
-
 ?
3.1.1.74 4-nitrophenyl acetate + H2O
-
 Thermobifida alba 4-nitrophenol + acetate
-
 ?
3.1.1.74 4-nitrophenyl acetate + H2O
-
 Thermobifida cellulosilytica 4-nitrophenol + acetate
-
 ?
3.1.1.74 4-nitrophenyl acetate + H2O
-
 Thermobifida fusca DSM 44342 4-nitrophenol + acetate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Thermobifida fusca 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Thermoactinomyces vulgaris 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Fusarium solani 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Aspergillus nidulans 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Monilinia fructicola 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Aspergillus oryzae 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Streptomyces acidiscabies 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Streptomyces badius 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Thermobifida fusca DSM 44342 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl hexanoate + H2O
-
 Fusarium solani 4-nitrophenol + hexanoate
-
 ?
3.1.1.74 4-nitrophenyl hexanoate + H2O
-
 Aspergillus oryzae 4-nitrophenol + hexanoate
-
 ?
3.1.1.74 4-nitrophenyl palmitate + H2O
-
 Cryptococcus sp. (in: Fungi) 4-nitrophenol + palmitate
-
 ?
3.1.1.74 4-nitrophenyl palmitate + H2O
-
 Cryptococcus sp. (in: Fungi) S-2 4-nitrophenol + palmitate
-
 ?
3.1.1.74 4-nitrophenyl valerate + H2O
-
 Fusarium solani 4-nitrophenol + valerate
-
 ?
3.1.1.74 4-nitrophenyl valerate + H2O
-
 Aspergillus oryzae 4-nitrophenol + valerate
-
 ?
3.1.1.74 cutin + H2O
-
 Aspergillus niger cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Pseudomonas aeruginosa cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Pseudomonas putida cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Pseudomonas mendocina cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Humicola insolens cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Penicillium citrinum cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Colletotrichum gloeosporioides cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Bipolaris maydis cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Penicillium sp. cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Thermobifida fusca cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Fusarium oxysporum cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Thermoactinomyces vulgaris cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Rhizoctonia solani cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Fusarium sambucinum cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Venturia inaequalis cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Streptomyces scabiei cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Thermothielavioides terrestris cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Helminthosporium sativum cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Fusarium solani cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Alternaria brassicicola cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Coprinopsis cinerea cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Alternaria consortialis cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Aspergillus nidulans cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Monilinia fructicola cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Pyrenopeziza brassicae cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Botrytis cinerea cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Pyricularia grisea cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Aspergillus oryzae cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Moesziomyces antarcticus cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Streptomyces acidiscabies cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Streptomyces badius cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Thermobifida alba cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Thermobifida cellulosilytica cutin monomers
-
 ?
3.1.1.74 cutin + H2O
-
 Cryptococcus sp. (in: Fungi) cutin monomers
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 cutin + H2O
-
 Cryptococcus sp. (in: Fungi) S-2 cutin monomers
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 cutin + H2O
-
 Thermobifida fusca DSM 44342 cutin monomers
-
 ?
3.1.1.74 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
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Aspergillus niger ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Pseudomonas aeruginosa ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Pseudomonas putida ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Humicola insolens ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Penicillium citrinum ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Colletotrichum gloeosporioides ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Bipolaris maydis ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Penicillium sp. ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Thermobifida fusca ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Fusarium oxysporum ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Thermoactinomyces vulgaris ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Rhizoctonia solani ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Fusarium sambucinum ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Venturia inaequalis ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Streptomyces scabiei ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Thermothielavioides terrestris ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Helminthosporium sativum ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Alternaria brassicicola ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Coprinopsis cinerea ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Alternaria consortialis ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Aspergillus nidulans ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Monilinia fructicola ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Pyrenopeziza brassicae ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Botrytis cinerea ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Pyricularia grisea ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Aspergillus oryzae ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Moesziomyces antarcticus ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Streptomyces badius ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Thermobifida alba ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Thermobifida cellulosilytica ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Cryptococcus sp. (in: Fungi) ?
-
 ?
3.1.1.74 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 ?
-
 ?
3.1.1.74 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 ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification. The enzyme prefers triacylglyceride substrates with short acyl groups Fusarium solani ?
-
 ?
3.1.1.74 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 ?
-
 ?
3.1.1.74 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 ?
-
 ?
3.1.1.74 additional information the optimum ratio of butyrate, acetate, and lactate is 4:1:3 Streptomyces acidiscabies ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Cryptococcus sp. (in: Fungi) S-2 ?
-
 ?
3.1.1.74 additional information cutinases are capable of catalyzing esterification and transesterification Thermobifida fusca DSM 44342 ?
-
 ?
3.1.1.74 tributyrin + H2O
-
 Fusarium solani butyric acid + 1,2-dibutyrylglycerol
-
 ?
3.1.1.74 trioctanoin + H2O
-
 Fusarium solani ?
-
 ?
3.1.1.74 triolein + H2O
-
 Fusarium solani ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.74 CLE
-
 Cryptococcus sp. (in: Fungi)
3.1.1.74 Cut1
-
 Thermobifida fusca
3.1.1.74 Cut1
-
 Botrytis cinerea
3.1.1.74 Cut1
-
 Pyricularia grisea
3.1.1.74 Cut1
-
 Thermobifida cellulosilytica
3.1.1.74 cutinase 1
-
 Fusarium sambucinum
3.1.1.74 cutinase 1
-
 Fusarium solani
3.1.1.74 cutinase 1
-
 Aspergillus oryzae
3.1.1.74 cutinase 1
-
 Thermobifida alba
3.1.1.74 cutinase 1
-
 Thermobifida cellulosilytica
3.1.1.74 cutinase 2
-
 Aspergillus nidulans
3.1.1.74 cutinase 2
-
 Thermobifida cellulosilytica
3.1.1.74 cutinase-like enzyme
-
 Cryptococcus sp. (in: Fungi)

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.74 2.4
-
 4-nitrophenyl acetate pH and temperature not specified in the publication Thermobifida cellulosilytica
3.1.1.74 2.72
-
 4-nitrophenyl acetate pH and temperature not specified in the publication Thermobifida alba
3.1.1.74 39.5
-
 4-nitrophenyl acetate pH and temperature not specified in the publication Thermobifida fusca
3.1.1.74 211.9
-
 4-nitrophenyl acetate pH and temperature not specified in the publication Thermobifida cellulosilytica

Expression

EC Number Organism Comment Expression
3.1.1.74 Thermobifida fusca increased enzyme production in strain WSH03-11 by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. tomato peel up
3.1.1.74 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
3.1.1.74 Streptomyces acidiscabies increased enzyme production in wild-type strain by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. apple cutin up
3.1.1.74 Streptomyces badius increased enzyme production in wild-type strain by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. apple cutin up
3.1.1.74 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

EC Number General Information Comment Organism
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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.
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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)
3.1.1.74 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
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Aspergillus niger
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Humicola insolens
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Penicillium citrinum
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Colletotrichum gloeosporioides
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Bipolaris maydis
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Penicillium sp.
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Fusarium oxysporum
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Rhizoctonia solani
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Fusarium sambucinum
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Venturia inaequalis
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Thermothielavioides terrestris
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Helminthosporium sativum
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Fusarium solani
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Alternaria brassicicola
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Coprinopsis cinerea
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Alternaria consortialis
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Aspergillus nidulans
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Monilinia fructicola
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Pyrenopeziza brassicae
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Botrytis cinerea
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Pyricularia grisea
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Aspergillus oryzae
3.1.1.74 malfunction specific inhibition of the enzyme blocks infectivity in several pathogen/host systems Moesziomyces antarcticus
3.1.1.74 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
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Aspergillus niger
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Pseudomonas aeruginosa
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Pseudomonas putida
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Pseudomonas mendocina
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Humicola insolens
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Penicillium citrinum
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Colletotrichum gloeosporioides
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Bipolaris maydis
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Penicillium sp.
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Thermobifida fusca
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Fusarium oxysporum
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Thermoactinomyces vulgaris
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Rhizoctonia solani
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Fusarium sambucinum
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Venturia inaequalis
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Streptomyces scabiei
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Thermothielavioides terrestris
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Helminthosporium sativum
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Alternaria brassicicola
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Coprinopsis cinerea
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Alternaria consortialis
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Aspergillus nidulans
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Pyrenopeziza brassicae
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Botrytis cinerea
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Pyricularia grisea
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Moesziomyces antarcticus
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Streptomyces acidiscabies
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Streptomyces badius
3.1.1.74 additional information the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent Thermobifida cellulosilytica
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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)
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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.
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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
3.1.1.74 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.1.74 42.4
-
 4-nitrophenyl acetate pH and temperature not specified in the publication Fusarium solani