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Literature summary for 3.5.1.41 extracted from
- Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4 (2017), Sci. Rep., 7, 1746 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ANIA_09380, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21 | Aspergillus nidulans |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant AnCDA, X-ray difraction structure determiantion analysis at 2.0 A resolution | Aspergillus nidulans |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics | Aspergillus nidulans | |
| 0.072 | - |
penta-N-acetyl-chitopentaose | pH 8.0, 50°C, recombinant enzyme | Aspergillus nidulans |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates, most effective bivalent metal ion | Aspergillus nidulans | |
| additional information | metal ion bound to the His-His-Asp triad | Aspergillus nidulans |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| chitin + H2O | Aspergillus nidulans | - |
? | - |
? | |
| chitin + H2O | Aspergillus nidulans ATCC 38163 | - |
? | - |
? | |
| chitin + H2O | Aspergillus nidulans CBS 112.46 | - |
? | - |
? | |
| chitin + H2O | Aspergillus nidulans FGSC A4 | - |
? | - |
? | |
| chitin + H2O | Aspergillus nidulans M139 | - |
? | - |
? | |
| chitin + H2O | Aspergillus nidulans NRRL 194 | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus nidulans | A0A1U8QU02 | i.e. Aspergillus nidulans strain FGSC A4 | - |
| Aspergillus nidulans ATCC 38163 | A0A1U8QU02 | i.e. Aspergillus nidulans strain FGSC A4 | - |
| Aspergillus nidulans CBS 112.46 | A0A1U8QU02 | i.e. Aspergillus nidulans strain FGSC A4 | - |
| Aspergillus nidulans FGSC A4 | A0A1U8QU02 | i.e. Aspergillus nidulans strain FGSC A4 | - |
| Aspergillus nidulans M139 | A0A1U8QU02 | i.e. Aspergillus nidulans strain FGSC A4 | - |
| Aspergillus nidulans NRRL 194 | A0A1U8QU02 | i.e. Aspergillus nidulans strain FGSC A4 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography to homogeneity | Aspergillus nidulans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetylated chitosan + H2O | - |
Aspergillus nidulans | ? | - |
? | |
| acetylated chitosan + H2O | - |
Aspergillus nidulans ATCC 38163 | ? | - |
? | |
| acetylated chitosan + H2O | - |
Aspergillus nidulans CBS 112.46 | ? | - |
? | |
| acetylated chitosan + H2O | - |
Aspergillus nidulans FGSC A4 | ? | - |
? | |
| acetylated chitosan + H2O | - |
Aspergillus nidulans M139 | ? | - |
? | |
| acetylated chitosan + H2O | - |
Aspergillus nidulans NRRL 194 | ? | - |
? | |
| acetylated glucoronoxylan + H2O | - |
Aspergillus nidulans | ? | - |
? | |
| acetylated glucoronoxylan + H2O | - |
Aspergillus nidulans ATCC 38163 | ? | - |
? | |
| acetylated glucoronoxylan + H2O | - |
Aspergillus nidulans CBS 112.46 | ? | - |
? | |
| acetylated glucoronoxylan + H2O | - |
Aspergillus nidulans FGSC A4 | ? | - |
? | |
| acetylated glucoronoxylan + H2O | - |
Aspergillus nidulans M139 | ? | - |
? | |
| acetylated glucoronoxylan + H2O | - |
Aspergillus nidulans NRRL 194 | ? | - |
? | |
| acetylated xylan + H2O | the dominating products are fully deacetylated xylooligosaccharides | Aspergillus nidulans | ? | - |
? | |
| acetylated xylan + H2O | the dominating products are fully deacetylated xylooligosaccharides | Aspergillus nidulans ATCC 38163 | ? | - |
? | |
| acetylated xylan + H2O | the dominating products are fully deacetylated xylooligosaccharides | Aspergillus nidulans CBS 112.46 | ? | - |
? | |
| acetylated xylan + H2O | the dominating products are fully deacetylated xylooligosaccharides | Aspergillus nidulans FGSC A4 | ? | - |
? | |
| acetylated xylan + H2O | the dominating products are fully deacetylated xylooligosaccharides | Aspergillus nidulans M139 | ? | - |
? | |
| acetylated xylan + H2O | the dominating products are fully deacetylated xylooligosaccharides | Aspergillus nidulans NRRL 194 | ? | - |
? | |
| chitin + H2O | - |
Aspergillus nidulans | ? | - |
? | |
| chitin + H2O | - |
Aspergillus nidulans ATCC 38163 | ? | - |
? | |
| chitin + H2O | - |
Aspergillus nidulans CBS 112.46 | ? | - |
? | |
| chitin + H2O | - |
Aspergillus nidulans FGSC A4 | ? | - |
? | |
| chitin + H2O | - |
Aspergillus nidulans M139 | ? | - |
? | |
| chitin + H2O | - |
Aspergillus nidulans NRRL 194 | ? | - |
? | |
| hexa-N-acetyl-chitohexaose + H2O | - |
Aspergillus nidulans | chitohexaose + 6 acetate | - |
? | |
| additional information | enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview | Aspergillus nidulans | ? | - |
? | |
| additional information | enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview | Aspergillus nidulans ATCC 38163 | ? | - |
? | |
| additional information | enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview | Aspergillus nidulans CBS 112.46 | ? | - |
? | |
| additional information | enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview | Aspergillus nidulans FGSC A4 | ? | - |
? | |
| additional information | enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview | Aspergillus nidulans M139 | ? | - |
? | |
| additional information | enzyme AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and cetylxylan, but not on peptidoglycan. AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar is much slower than deacetylation of the other sugars in chito-oligomers. AnCDA shows no activity on peptidoglycan, but the enzyme is active on oligomeric acetylxylan and acetylated glucuronoxylan, as well as on chitosan with an initial fraction of acetylated residues. AnCDA is active on insoluble chitin. Substrate specificity and MALDI-ToF-mass spectrometric product analysis, overview | Aspergillus nidulans NRRL 194 | ? | - |
? | |
| penta-N-acetyl-chitopentaose + H2O | - |
Aspergillus nidulans | chitopentaose + 5 acetate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | three-dimensional and secondary structure analysis | Aspergillus nidulans |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AN9380.2 | - |
Aspergillus nidulans |
| AnCDA | - |
Aspergillus nidulans |
| ANIA_09380 | - |
Aspergillus nidulans |
| NodB homology domain-containing protein | UniProt | Aspergillus nidulans |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
broad optimum, recombinant enzyme | Aspergillus nidulans |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | purified recombinant enzyme, pH 8.0, 60 min, stable | Aspergillus nidulans |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.4 | - |
penta-N-acetyl-chitopentaose | pH 8.0, 50°C, recombinant enzyme | Aspergillus nidulans | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
recombinant enzyme | Aspergillus nidulans |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 10 | purified recombinant enzyme, 37°C, 60 min, stable | Aspergillus nidulans |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4) | Aspergillus nidulans |
| additional information | His-His-Asp catalytic triad | Aspergillus nidulans |
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Release 2023.1 (January 2023)
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