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Literature summary for 3.1.1.74 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Aspergillus niger | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 22800 | - |
x * 22800, about, sequence calculation, x * 25000-35000, glycosylated recombinant enzyme, SDS-PAGE | Aspergillus niger |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | ? |  |
| 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 | ? | |
| poly(caprolactone) + H2O | Aspergillus niger | - |
? | - |
? | |
| poly(caprolactone) + H2O | Aspergillus niger CBS 513.88 | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | - |
gene anig5 | - |
| Aspergillus niger CBS 513.88 | - |
gene anig5 | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the enzyme has six putative glycosylation sites | Aspergillus niger |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| 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)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl butyrate + H2O | - |
Aspergillus niger | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Aspergillus niger CBS 513.88 | 4-nitrophenol + butyrate | - |
? | |
| 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 | ? | |
| 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 | ? | |
| poly(caprolactone) + H2O | - |
Aspergillus niger | ? | - |
? | |
| poly(caprolactone) + H2O | - |
Aspergillus niger CBS 513.88 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 22800, about, sequence calculation, x * 25000-35000, glycosylated recombinant enzyme, SDS-PAGE | Aspergillus niger |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acidic cutinase | - |
Aspergillus niger |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
assay at | Aspergillus niger |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
purified recombinant enzyme, pH 3.0-6.0, 24 h, completely stable at | Aspergillus niger |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6.5 | broad optimum | Aspergillus niger |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 7.5 | activity range, no activity at pH 8.0 and pH 2.0 | Aspergillus niger |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 6 | purified recombinant enzyme, 40°C, 24 h, completely stable at | Aspergillus niger |
| 7 | - |
purified recombinant enzyme, 40°C, 24 h, loss of 70% activity | Aspergillus niger |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | enzyme homology modeling | Aspergillus niger |
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