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Literature summary extracted from

  • Wang, Y.; Niu, X.; Guo, X.; Yu, H.; Liu, Z.; Zhang, Z.; Yuan, S.
    Heterologous expression, characterization and possible functions of the chitin deacetylases, Cda1 and Cda2, from mushroom Coprinopsis cinerea (2018), Glycobiology, 28, 318-332 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.41 recombinant expression of His-tagged isozyme Cda1 Coprinopsis cinerea
3.5.1.41 recombinant expression of His-tagged isozyme Cda2 Coprinopsis cinerea

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.41 Al3+
-
 Coprinopsis cinerea
3.5.1.41 Ba2+ slight inhibition of Cda1 Coprinopsis cinerea
3.5.1.41 Ca2+ inhibition of Cda2 Coprinopsis cinerea
3.5.1.41 Co2+ strong inhibition of Cda1 Coprinopsis cinerea
3.5.1.41 Cu2+ inhibition of Cda2; strong inhibition of Cda1 Coprinopsis cinerea
3.5.1.41 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
3.5.1.41 Fe2+ inhibition of Cda2 Coprinopsis cinerea
3.5.1.41 Mg2+ inhibition of Cda2 Coprinopsis cinerea
3.5.1.41 Mn2+ inhibition of Cda2 Coprinopsis cinerea
3.5.1.41 additional information no or poor inhibitory effects on Cda1 by 1 mM of Fe2+, Mg2+, Ni2+, and Mn2+ Coprinopsis cinerea
3.5.1.41 Zn2+ inhibition of Cda2; strong inhibition of Cda1 Coprinopsis cinerea

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.41 Al3+ slight activation of Cda2 Coprinopsis cinerea
3.5.1.41 Ba2+ slight activation of Cda2 Coprinopsis cinerea
3.5.1.41 Co2+ strong activation of Cda2 Coprinopsis cinerea
3.5.1.41 Ni2+ strong activation of Cda2 Coprinopsis cinerea

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.41 Coprinopsis cinerea
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.41 recombinant His-tagged isozyme Cda1 by nickel affinity chromatography Coprinopsis cinerea
3.5.1.41 recombinant His-tagged isozyme Cda2 by nickel affinity chromatography Coprinopsis cinerea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.41 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 ?
-
 ?
3.5.1.41 chitohexaose + H2O
-
 Coprinopsis cinerea ?
-
 ?
3.5.1.41 glycol chitin + H2O best substrate Coprinopsis cinerea ?
-
 ?
3.5.1.41 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 ?
-
 ?
3.5.1.41 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 ?
-
 ?
3.5.1.41 N,N',N''-triacetylchitotriose + H2O
-
 Coprinopsis cinerea ?
-
 ?
3.5.1.41 N,N'-diacetylchitobiose + H2O
-
 Coprinopsis cinerea ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.41 CDA1
-
 Coprinopsis cinerea
3.5.1.41 CDA2
-
 Coprinopsis cinerea

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.41 30 50 the deacetylation activity of Cda1 is essentially stable at 30-50°C Coprinopsis cinerea
3.5.1.41 30 60 the deacetylation activity of Cda2 is essentially stable at 30-50°C Coprinopsis cinerea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.41 7.5
-
-
 Coprinopsis cinerea
3.5.1.41 9
-
-
 Coprinopsis cinerea

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.5.1.41 6 9 the deacetylation activity of Cda1 is essentially stable at pH 6.0-9.0 Coprinopsis cinerea
3.5.1.41 7 9.5 the deacetylation activity of Cda1 is essentially stable at pH 7.0-9.5 Coprinopsis cinerea

General Information

EC Number General Information Comment Organism
3.5.1.41 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