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Literature summary for 3.5.1.41 extracted from
- SSF production, purification and characterization of chitin deacetylase from Aspergillus flavus (2018), Biocatal. Biotransform., 36, 296-306 .
No PubMed abstract available
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Triton X-100 | slight activation at 1% | Aspergillus flavus |  |
| Tween 20 | slight activation at 1% | Aspergillus flavus | |
| Tween 40 | slight activation at 1% | Aspergillus flavus | |
| Tween 60 | slight activation at 1% | Aspergillus flavus | |
| Tween 80 | about 30% activation at 1% | Aspergillus flavus | |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | strong inhibition | Aspergillus flavus | |
| Ag+ | - |
Aspergillus flavus | |
| Co2+ | - |
Aspergillus flavus | |
| Cu2+ | - |
Aspergillus flavus | |
| DTT | strong inhibition | Aspergillus flavus | |
| EDTA | - |
Aspergillus flavus | |
| Fe2+ | - |
Aspergillus flavus | |
| Fe3+ | - |
Aspergillus flavus | |
| Hg2+ | - |
Aspergillus flavus | |
| Mg2+ | - |
Aspergillus flavus | |
| additional information | no product inhibition by acetate up to 70 mM concentration | Aspergillus flavus | |
| SDS | strong inhibition | Aspergillus flavus | |
| Urea | moderate inhibition | Aspergillus flavus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km and kcat values of the enzyme are determined to be 9.45 mg/ml using colloidal chitin as substrate, Michaelis-Menten kinetics | Aspergillus flavus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Aspergillus flavus | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | slight activation at 10 mM | Aspergillus flavus | |
| Mn2+ | slight activation | Aspergillus flavus | |
| additional information | no or poor effects by 10-20 mm Na+, Sn2+, and Ni2+ | Aspergillus flavus | |
| Na+ | slight activation at 10 mM | Aspergillus flavus | |
| Zn2+ | slight activation | Aspergillus flavus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus flavus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme 3.94fold by ammonium sulfate precipitation, ion exchange chromatography, and gel filtration | Aspergillus flavus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | the CDA production in SSF increases 1.79fold in comparison to the unoptimized basal level medium. Optimization of significant parameters affecting CDA production in SSF by response surface methodology (RSM) | Aspergillus flavus | - |
| mycelium | solid-substrate fermentation, wheat bran is used as the substrate | Aspergillus flavus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 55.91 | - |
purified native enzyme, substrate colloidal chitin, pH 6.5, 50°C | Aspergillus flavus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| colloidal chitin + H2O | - |
Aspergillus flavus | ? | - |
? | |
| glycol chitin + H2O | - |
Aspergillus flavus | ? | - |
? | |
| N,N',N'',N'''-tetraacetylchitotetraose + H2O | - |
Aspergillus flavus | ? | - |
? | |
| N,N',N''-triacetylchitotriose + H2O | - |
Aspergillus flavus | ? | - |
? | |
| N,N'-diacetylchitobiose + H2O | - |
Aspergillus flavus | ? | - |
? | |
| N-acetylglucosamine + H2O | - |
Aspergillus flavus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 28000, SDS-PAGE | Aspergillus flavus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CDA | - |
Aspergillus flavus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Aspergillus flavus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
purified native enzyme, 3 h, stable | Aspergillus flavus |
| 50 | - |
purified native enzyme, 3 h, 40% activity remaining, half-life is 135 min. At temperatures above 50°C, the enzyme stability is significantly reduced | Aspergillus flavus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km and kcat values of the enzyme are determined to be 26.72/s using colloidal chitin as substrate | Aspergillus flavus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Aspergillus flavus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 2.5 | 10.5 | activity range, profile overview | Aspergillus flavus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 2.5 | 10.5 | stability range, profile overview. Most stable at pH 7.0-9.0 | Aspergillus flavus |
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