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Literature summary extracted from

  • Zhu, X.Y.; Zhao, Y.; Zhang, H.D.; Wang, W.X.; Cong, H.H.; Yin, H.
    Characterization of the specific mode of action of a chitin deacetylase and separation of the partially acetylated chitosan oligosaccharides (2019), Mar. Drugs, 17, 74 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.41 gene CDA2, sequence comparisons, recombinant expression of His-tagged enzyme in Pichia pastoris strain X-33, the enzyme is secreted Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.41 Ca2+ activates Saccharomyces cerevisiae
3.5.1.41 Co2+ activates Saccharomyces cerevisiae
3.5.1.41 Zn2+ activates, zinc-binding triad consists of residues Asp103, His149, and His153 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.41 acetylated chitosan oligosaccharide + H2O Saccharomyces cerevisiae
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 ?
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 ?
3.5.1.41 acetylated chitosan oligosaccharide + H2O Saccharomyces cerevisiae ATCC 204508
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 ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.41 Saccharomyces cerevisiae Q06703
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3.5.1.41 Saccharomyces cerevisiae ATCC 204508 Q06703
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Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.1.41 glycoprotein N-glycosylation post-translational modifications in ScCDA2 positions Asn181, Asn199, and Asn203 Saccharomyces cerevisiae

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.41 recombinant extracellular His-tagged enzyme from Pichia pastoris strain X-33 culture medium by ultrafiltration, nickel affinity chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.41 acetylated chitosan oligosaccharide + H2O
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 Saccharomyces cerevisiae ?
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 ?
3.5.1.41 acetylated chitosan oligosaccharide + H2O analysis of deacetylation pattern of ScCDA2, MALDI-TOF-MS analysis, overview. ScCDA2 shows highest activity on colloidal chitin, followed by alpha-chitin, and then beta-chitin Saccharomyces cerevisiae ?
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 ?
3.5.1.41 acetylated chitosan oligosaccharide + H2O
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 Saccharomyces cerevisiae ATCC 204508 ?
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 ?
3.5.1.41 acetylated chitosan oligosaccharide + H2O analysis of deacetylation pattern of ScCDA2, MALDI-TOF-MS analysis, overview. ScCDA2 shows highest activity on colloidal chitin, followed by alpha-chitin, and then beta-chitin Saccharomyces cerevisiae ATCC 204508 ?
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 ?
3.5.1.41 chitin + H2O chitin oligomers are deacetylated with recombinant ScCDA2 to form partially acetylated chitosan oligosaccharides Saccharomyces cerevisiae ?
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3.5.1.41 chitin + H2O chitin oligomers are deacetylated with recombinant ScCDA2 to form partially acetylated chitosan oligosaccharides Saccharomyces cerevisiae ATCC 204508 ?
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 ?
3.5.1.41 additional information ScCDA2 can hydrolyze N-acetamido groups rather than the reducing ends of chitin oligosaccharides, producing fully defined chitosan oligosaccharides by a multiple attack mode of action. Furthermore, ScCDA2 is able to remove about 8% and 20% of the acetyl groups from crystalline chitin and colloidal chitin. Partially acetylated chitosan oligosaccharides (COS) consist of N-acetylglucosamine (GlcNAc) and glucosamine (GlcN) residues. Enzyme ScCDA2 produces COS with specific acetylation patterns of DAAA, ADAA, AADA, DDAA, DADA, ADDA and DDDA, respectively. ScCDA2 does not deacetylate the GlcNAc unit that is closest to the reducing end of the oligomer furthermore ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides. ScCDA2 also exhibits about 8% and 20% deacetylation activity on crystalline chitin and colloid chitin, respectively. ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides Saccharomyces cerevisiae ?
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 ?
3.5.1.41 additional information ScCDA2 can hydrolyze N-acetamido groups rather than the reducing ends of chitin oligosaccharides, producing fully defined chitosan oligosaccharides by a multiple attack mode of action. Furthermore, ScCDA2 is able to remove about 8% and 20% of the acetyl groups from crystalline chitin and colloidal chitin. Partially acetylated chitosan oligosaccharides (COS) consist of N-acetylglucosamine (GlcNAc) and glucosamine (GlcN) residues. Enzyme ScCDA2 produces COS with specific acetylation patterns of DAAA, ADAA, AADA, DDAA, DADA, ADDA and DDDA, respectively. ScCDA2 does not deacetylate the GlcNAc unit that is closest to the reducing end of the oligomer furthermore ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides. ScCDA2 also exhibits about 8% and 20% deacetylation activity on crystalline chitin and colloid chitin, respectively. ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides Saccharomyces cerevisiae ATCC 204508 ?
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 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.41 More the secondary structure consists of a conserved (alpha/beta)8 folded barrel structure and six loops. Structure comparisons, overview Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
3.5.1.41 N-acetylglucosamine deacetylase
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 Saccharomyces cerevisiae
3.5.1.41 ScCDA2
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 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.41 37
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 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.41 8
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 assay at Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
3.5.1.41 evolution CDA belongs to the carbohydrate esterase family 4 (CE4) according to the classification of the CAZY database Saccharomyces cerevisiae
3.5.1.41 additional information ScCDA2 has a multiple-attack deacetylation mechanism on chitin oligosaccharides, acetylation patterns, overview. Active site residues are Asp102 and His250. Homology modeling and substrate binding specificity of ScCDA2 using crystal structures (PDB ID: 5LFZ, 2CC0 and 2C1G) as templates. The docking results show that chitin lies in the substrate-binding pocket which is surrounded by six loops, His250, Asp102, Asp103, His149 and His153. Asp103, His149 and His153 form a coordinate bond with Zn2+, and the metal ion serves as a Lewis acid to assist the water affinity attack on the carbon atom on the amide bond. The adjacent His250 and Asp102 play a catalytic role through protonation, and the common action of these amino acids leads to the cleaving of the acetyl group Saccharomyces cerevisiae