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Literature summary extracted from

  • Nyyssoelae, A.; Pihlajaniemi, V.; Jaervinen, R.; Mikander, S.; Kontkanen, H.; Kruus, K.; Kallio, H.; Buchert, J.
    Screening of microbes for novel acidic cutinases and cloning and expression of an acidic cutinase from Aspergillus niger CBS 513.88 (2013), Enzyme Microb. Technol., 52, 272-278.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.74 codon optimized cutinase gene anig5, subcloning of C-terminally His-tagged enzyme in Escherichia coli strain XL1-Blue and recombinant expression in Pichia pastoris after selection from 38 strains for production, screening and pH-Profiling of the cutinase activities of the culture supernatants, overview Aspergillus niger

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.74 extracellular
-
 Aspergillus niger
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.74 22800
-
 x * 22800, about, sequence calculation, x * 25000-35000, glycosylated recombinant enzyme, SDS-PAGE Aspergillus niger

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 hydrolysis of tritiated apple cutin, and GC-MS analysis of the hydrolysis products, overview 16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid major apple cutin monomers released by the action of cutinases, but no formation of 18-hydroxyoctadeca-9-enoic acid and 18-hydroxyoctadeca-9,12-dienoic acid ?
3.1.1.74 cutin + H2O Aspergillus niger CBS 513.88 hydrolysis of tritiated apple cutin, and GC-MS analysis of the hydrolysis products, overview 16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid major apple cutin monomers released by the action of cutinases, but no formation of 18-hydroxyoctadeca-9-enoic acid and 18-hydroxyoctadeca-9,12-dienoic acid ?
3.1.1.74 poly(caprolactone) + H2O Aspergillus niger
-
 ?
-
 ?
3.1.1.74 poly(caprolactone) + H2O Aspergillus niger CBS 513.88
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.74 Aspergillus niger
-
 gene anig5
-
3.1.1.74 Aspergillus niger CBS 513.88
-
 gene anig5
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.74 glycoprotein the enzyme has six putative glycosylation sites Aspergillus niger

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.74 additional information cultures are grown on agar plates at pH 4.0 with the cutinase model substrate polycaprolactone as a carbon source Aspergillus niger
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Aspergillus niger 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Aspergillus niger CBS 513.88 4-nitrophenol + butyrate
-
 ?
3.1.1.74 cutin + H2O hydrolysis of tritiated apple cutin, and GC-MS analysis of the hydrolysis products, overview Aspergillus niger 16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid major apple cutin monomers released by the action of cutinases, but no formation of 18-hydroxyoctadeca-9-enoic acid and 18-hydroxyoctadeca-9,12-dienoic acid ?
3.1.1.74 cutin + H2O hydrolysis of tritiated apple cutin, and GC-MS analysis of the hydrolysis products, overview Aspergillus niger CBS 513.88 16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid major apple cutin monomers released by the action of cutinases, but no formation of 18-hydroxyoctadeca-9-enoic acid and 18-hydroxyoctadeca-9,12-dienoic acid ?
3.1.1.74 poly(caprolactone) + H2O
-
 Aspergillus niger ?
-
 ?
3.1.1.74 poly(caprolactone) + H2O
-
 Aspergillus niger CBS 513.88 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.74 ? x * 22800, about, sequence calculation, x * 25000-35000, glycosylated recombinant enzyme, SDS-PAGE Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
3.1.1.74 acidic cutinase
-
 Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.74 40
-
 assay at Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.74 40
-
 purified recombinant enzyme, pH 3.0-6.0, 24 h, completely stable at Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.74 5 6.5 broad optimum Aspergillus niger

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.74 3.5 7.5 activity range, no activity at pH 8.0 and pH 2.0 Aspergillus niger

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.74 3 6 purified recombinant enzyme, 40°C, 24 h, completely stable at Aspergillus niger
3.1.1.74 7
-
 purified recombinant enzyme, 40°C, 24 h, loss of 70% activity Aspergillus niger

General Information

EC Number General Information Comment Organism
3.1.1.74 additional information enzyme homology modeling Aspergillus niger