Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged isozyme Cda1 | Coprinopsis cinerea |
recombinant expression of His-tagged isozyme Cda2 | Coprinopsis cinerea |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Al3+ | - |
Coprinopsis cinerea | |
Ba2+ | slight inhibition of Cda1 | Coprinopsis cinerea | |
Ca2+ | inhibition of Cda2 | Coprinopsis cinerea | |
Co2+ | strong inhibition of Cda1 | Coprinopsis cinerea | |
Cu2+ | inhibition of Cda2; strong inhibition of Cda1 | Coprinopsis cinerea | |
EDTA | slight inhibition of Cda1 at 1-2 mM; the deacetylation activity of Cda2 is inhibited by 62 and 82% by 1 and 2 mM EDTA, respectively | Coprinopsis cinerea | |
Fe2+ | inhibition of Cda2 | Coprinopsis cinerea | |
Mg2+ | inhibition of Cda2 | Coprinopsis cinerea | |
Mn2+ | inhibition of Cda2 | Coprinopsis cinerea | |
additional information | no or poor inhibitory effects on Cda1 by 1 mM of Fe2+, Mg2+, Ni2+, and Mn2+ | Coprinopsis cinerea | |
Zn2+ | inhibition of Cda2; strong inhibition of Cda1 | Coprinopsis cinerea |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Al3+ | slight activation of Cda2 | Coprinopsis cinerea | |
Ba2+ | slight activation of Cda2 | Coprinopsis cinerea | |
Co2+ | strong activation of Cda2 | Coprinopsis cinerea | |
Ni2+ | strong activation of Cda2 | Coprinopsis cinerea |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Coprinopsis cinerea | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged isozyme Cda1 by nickel affinity chromatography | Coprinopsis cinerea |
recombinant His-tagged isozyme Cda2 by nickel affinity chromatography | Coprinopsis cinerea |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetylated chitosan + H2O | activity with chitosan with an acetylation degree (DDA) of 40%, no activity with chitosan with DDA of 75 or 85% | Coprinopsis cinerea | ? | - |
? | |
chitohexaose + H2O | - |
Coprinopsis cinerea | ? | - |
? | |
glycol chitin + H2O | best substrate | Coprinopsis cinerea | ? | - |
? | |
additional information | Cda1 preferably deacetylates the nonreducing end residue of (GlcNAc)2, the internal or nonreducing end residue of (GlcNAc)3 and the nonreducing residue of (GlcNAc)6 after deacetylating the internal residues. Cda1 prefers chitohexaose with higher degrees of acetylation for deacetylation. Pathway of chitin deacetylation. Comparison of isozymes Cda1 and Cda2, overview. No activity of Cda1 with colloidal chitin, chitin powder, and N-acetylglucosamine | Coprinopsis cinerea | ? | - |
? | |
additional information | Cda2 preferably deacetylates the reducing end residue of (GlcNAc)2, the internal or reducing end residue of (GlcNAc)3 and the reducing residue of (GlcNAc)6 after deacetylating the internal residues. Cda2 shows a weaker preference for chitohexaose with varying degrees of acetylation. Pathway of chitin deacetylation. #Comparison of isozymes Cda1 and Cda2, overview. No activity of Cda2 with colloidal chitin, chitin powder, and N-acetylglucosamine | Coprinopsis cinerea | ? | - |
? | |
N,N',N''-triacetylchitotriose + H2O | - |
Coprinopsis cinerea | ? | - |
? | |
N,N'-diacetylchitobiose + H2O | - |
Coprinopsis cinerea | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CDA1 | - |
Coprinopsis cinerea |
CDA2 | - |
Coprinopsis cinerea |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 50 | the deacetylation activity of Cda1 is essentially stable at 30-50°C | Coprinopsis cinerea |
30 | 60 | the deacetylation activity of Cda2 is essentially stable at 30-50°C | Coprinopsis cinerea |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Coprinopsis cinerea |
9 | - |
- |
Coprinopsis cinerea |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
6 | 9 | the deacetylation activity of Cda1 is essentially stable at pH 6.0-9.0 | Coprinopsis cinerea |
7 | 9.5 | the deacetylation activity of Cda1 is essentially stable at pH 7.0-9.5 | Coprinopsis cinerea |
General Information | Comment | Organism |
---|---|---|
evolution | comparison of isozymes Cda1 and Cda2, sequence and structure comparison. The predicted Cda1 structure shows more hydrophobic aromatic amino acids on the surface near subsite +1 in the active site than on the surface near subsite -1, whereas the predicted Cda2 structure has more hydrophobic aromatic amino acids on the surface near subsite -1 than on the surface near subsite +1, which may be the molecular basis of the distinctive catalytic features between Cda1 and Cda2. Notably, Cda1 has a high transcription level in the nonelongating basal stipe region, whereas Cda2 has a high transcription level in the elongating apical stipe region, and the transcription level of the former is approximately five times that of the latter. Correspondingly, the molar ratio of GlcN/GlcNAc increased from 0.15 in the cell wall of the apical stipe region to 0.22 in the cell wall of the basal stipe region. Different modes of action of Cda1 and Cda2 may be related to their functions in the different stipe regions. Mode of action of Cda1 and Cda2 with chitin oligomers, overview | Coprinopsis cinerea |