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Literature summary extracted from

  • Aragunde, H.; Biarnes, X.; Planas, A.
    Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases (2018), Int. J. Mol. Sci., 19, E412 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.5.1.41 agriculture the enzyme is used as a biocontrol agent against a number of plant parasitic nematodes in food-security crops Pochonia chlamydosporia

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.41 recombinant expression of the enzyme in Hansenula polymorpha as a full length protein composed of the CE4 domain flanked by two CBM18 domains Podospora anserina

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.41 crystal structure PDB ID 2IW0 Colletotrichum lindemuthianum
3.5.1.41 crystal structure PDB ID 2Y8U Aspergillus nidulans
3.5.1.41 crystal structure PDB ID 3WX7 Vibrio parahaemolyticus
3.5.1.41 crystal structure PDB ID 4NY2 Vibrio cholerae
3.5.1.41 crystal structure PDB ID 5LFZ Arthrobacter sp. Hiyo8

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.41 Ni2+ required Arthrobacter sp. Hiyo8

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.41 extracellular the enzyme is secreted Colletotrichum lindemuthianum
-
-
3.5.1.41 extracellular the enzyme is secreted Aspergillus nidulans
-
-
3.5.1.41 extracellular the enzyme is secreted Arthrobacter sp. Hiyo8
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Vibrio parahaemolyticus
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Podospora anserina
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Colletotrichum lindemuthianum
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Vibrio cholerae
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Amylomyces rouxii
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Sinorhizobium meliloti
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Aspergillus nidulans
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Puccinia graminis f. sp. tritici
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Pestalotiopsis sp.
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Pochonia chlamydosporia
-
-
3.5.1.41 additional information in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis Arthrobacter sp. Hiyo8
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.41 Co2+ required Colletotrichum lindemuthianum
3.5.1.41 Co2+ required Aspergillus nidulans
3.5.1.41 Mg2+ required Sinorhizobium meliloti
3.5.1.41 Mn2+ required Sinorhizobium meliloti
3.5.1.41 Zn2+ required Vibrio parahaemolyticus
3.5.1.41 Zn2+ required Podospora anserina
3.5.1.41 Zn2+ required Colletotrichum lindemuthianum
3.5.1.41 Zn2+ required Vibrio cholerae
3.5.1.41 Zn2+ required Amylomyces rouxii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.41 additional information Amylomyces rouxii substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.41 Amylomyces rouxii P50325 i.e. Mucor rouxii
-
3.5.1.41 Arthrobacter sp. Hiyo8 A0A0K2RH66
-
-
3.5.1.41 Aspergillus nidulans B3VD85
-
-
3.5.1.41 Colletotrichum lindemuthianum Q6DWK3
-
-
3.5.1.41 Pestalotiopsis sp. A0A1L3THR9
-
-
3.5.1.41 Pochonia chlamydosporia A0A179EY19
-
-
3.5.1.41 Pochonia chlamydosporia 170 A0A179EY19
-
-
3.5.1.41 Podospora anserina
-
-
-
3.5.1.41 Puccinia graminis f. sp. tritici H6QRV0
-
-
3.5.1.41 Puccinia graminis f. sp. tritici CRL 75-36-700-3 H6QRV0
-
-
3.5.1.41 Puccinia graminis f. sp. tritici race SCCL H6QRV0
-
-
3.5.1.41 Sinorhizobium meliloti P02963 i.e. Sinorhizobium meliloti
-
3.5.1.41 Vibrio cholerae
-
-
-
3.5.1.41 Vibrio parahaemolyticus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.41 chitin + H2O
-
 Arthrobacter sp. Hiyo8 deacetylated chitin + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O
-
 Colletotrichum lindemuthianum ?
-
 r
3.5.1.41 chitooligosaccharides + H2O
-
 Podospora anserina deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O
-
 Amylomyces rouxii deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O
-
 Sinorhizobium meliloti deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O
-
 Pestalotiopsis sp. deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O
-
 Pochonia chlamydosporia deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O AnCDA is active towards chitooligosaccharides with a DP of 2 to 6 Aspergillus nidulans deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O the activity increases with the degree of acetylation. The minimal substrate is tetraacetylchitotetraose, the enzyme is not able to act on shorter substrates Puccinia graminis f. sp. tritici deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O the enzyme from Vibrio parahaemolyticus only deacetylate DP2 and DP3 substrates Vibrio parahaemolyticus deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O Vibrio cholera chitin deacetylase has a broader specificity, being active on DP2 to DP6 substrates. VcCDA is 10fold more active on DP2 than DP4 substrates, and it is highly specific for deacetylation of the penultimate residue from the non-reducing end, generating monodeacetylated products with the pattern Vibrio cholerae deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O
-
 Pochonia chlamydosporia 170 deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O the activity increases with the degree of acetylation. The minimal substrate is tetraacetylchitotetraose, the enzyme is not able to act on shorter substrates Puccinia graminis f. sp. tritici race SCCL deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitooligosaccharides + H2O the activity increases with the degree of acetylation. The minimal substrate is tetraacetylchitotetraose, the enzyme is not able to act on shorter substrates Puccinia graminis f. sp. tritici CRL 75-36-700-3 deacetylated chitooligosaccharides + acetate
-
 ?
3.5.1.41 chitosan + H2O
-
 Podospora anserina deacetylated chitosan + acetate
-
 ?
3.5.1.41 chitosan + H2O
-
 Arthrobacter sp. Hiyo8 deacetylated chitosan + acetate
-
 ?
3.5.1.41 colloidal chitin + H2O
-
 Puccinia graminis f. sp. tritici deacetylated colloidal chitin + acetate
-
 ?
3.5.1.41 colloidal chitin + H2O
-
 Pestalotiopsis sp. deacetylated colloidal chitin + acetate
-
 ?
3.5.1.41 colloidal chitin + H2O
-
 Puccinia graminis f. sp. tritici race SCCL deacetylated colloidal chitin + acetate
-
 ?
3.5.1.41 colloidal chitin + H2O
-
 Puccinia graminis f. sp. tritici CRL 75-36-700-3 deacetylated colloidal chitin + acetate
-
 ?
3.5.1.41 glycol chitin + H2O
-
 Podospora anserina deacetylated glycol chitin + acetate
-
 ?
3.5.1.41 glycol chitin + H2O
-
 Colletotrichum lindemuthianum deacetylated glycol chitin + acetate
-
 r
3.5.1.41 glycol chitin + H2O
-
 Amylomyces rouxii deacetylated glycol chitin + acetate
-
 ?
3.5.1.41 glycol chitin + H2O
-
 Aspergillus nidulans deacetylated glycol chitin + acetate
-
 ?
3.5.1.41 glycol chitin + H2O
-
 Puccinia graminis f. sp. tritici deacetylated glycol chitin + acetate
-
 ?
3.5.1.41 glycol chitin + H2O
-
 Pochonia chlamydosporia deacetylated glycol chitin + acetate
-
 ?
3.5.1.41 glycol chitin + H2O
-
 Pochonia chlamydosporia 170 deacetylated glycol chitin + acetate
-
 ?
3.5.1.41 glycol chitin + H2O
-
 Puccinia graminis f. sp. tritici race SCCL deacetylated glycol chitin + acetate
-
 ?
3.5.1.41 glycol chitin + H2O
-
 Puccinia graminis f. sp. tritici CRL 75-36-700-3 deacetylated glycol chitin + acetate
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview Vibrio parahaemolyticus ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview Vibrio cholerae ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview Amylomyces rouxii ?
-
 ?
3.5.1.41 additional information MrCDA is a specific enzyme for beta-1,4-GlcNAc polymers, such as glycol-chitin, colloidal chitin, chitosan, and chitin. IIt also deacetylates acetylxylan, but it is inactive on peptidoglycan or acetyl heparin polymers. It is active on chitooligosaccharides, and its activity increases with the degree of polymerization (DP), with triacetylchitotriose being the smallest substrate it acts on. The enzyme deacetylates its substrates following a multiple-attack mechanism, but the resulting pattern depends on the DP of the substrate: DP3, DP6, and DP7 substrates are not fully deacetylated, leaving the reducing GlcNAc unmodified, whereas DP4 and DP5 substrates are fully deacetylated. In all cases, deacetylation starts at the non-reducing end residue, and then proceeds to the neighboring monomer towards the reducing end Amylomyces rouxii ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. ArCE4 is active on alpha- and beta-chitin, chitosan (DA 64%), and acetylxylan. On COS substrates, activity increases with increasing DP, with higher activity against DP5 compared to DP6, and no activity on GlcNAc. The enzyme acts by a multiple-chain mechanism, as shown with DP5 substrate, where different mono- and di-deacetylated products are obtained. The first deacelylation happens at all three internal positions, whereas di-deacetylation mainly occurs at the GlcNAc unit next to the reducing end, and at either of the two other internal units (ADDAA and ADADA). Although other minor products are formed, it seems that the reducing end unit is not deacetylated Arthrobacter sp. Hiyo8 ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms. The enzyme from Puccinia graminis is not active on insoluble polymers such as alpha- or beta-chitin. The sequence of the products obtained by enzymatic deacetylation of tetramers to hexamers reveals that the enzyme specifically deacetylates all but the last two GlcNAc units on the non-reducing end via a multiple-chain mechanism Puccinia graminis f. sp. tritici ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. No activity on peptidoglycan. The enzyme is inactive towards GlcNAc, and catalyzes the mono-deacetylation of (GlcNAc)2. The deacetylation rate exhibits a counter-intuitive relationship with the length of the chitooligosaccharide substrates: odd-numbered chitooligosaccharides (DP5, DP3) have higher apparent rate constants than even-numbered oligomers (DP4, DP2). Monitoring of products formation with the DP6 substrate showed that the first deacetylation event occurs at random positions, except for the reducing end, which reacts much more slowly to yield the fully deacetylated product Aspergillus nidulans ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. NodB is active on chitooligosaccharides from DP2 to DP5 with no differences in kcat, but Km decreases with increasing DP. Specifically, kcat/KM is 5fold higher for DP5 than for DP2 substrates. DP4 or DP5 substrates are the natural substrates depending on the rhizobial strain. NodB only deacetylates the non-reducing end residue, but traces of a second deacetylation event are seen upon long incubations Sinorhizobium meliloti ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. PcCDA deacetylates chitooligosaccharides, requiring at least four GlcNAc units in order to be active, but it prefers longer substrates. For DP4 and DP5 substrates, it first deacetylates the penultimate residue from the non-reducing end, and continues to the next residue towards the reducing end, with a pattern of acetylation Pochonia chlamydosporia ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. PesCDA acts better on colloidal chitin as substrate, but it is also active on chitosans with a degree of acetylation (DA) of 10-60% (higher activity with a higher DA), as well as on chitooligosaccharides. It is not able to deacetylate crystalline chitin, neither alpha- or beta-allomorphs. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Pestalotiopsis sp. ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. The enzyme from Colletotrichum lindemuthianum is able to fully deacetylate chitooligosaccharides with a DP equal to or greater than 3, while it only deacetylates the non-reducing GlcNAc of N,N'-diacetylchitobiose. This enzyme is reversible, as it is also able to catalyze the acetylation of chitosan oligomers Colletotrichum lindemuthianum ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. The enzyme is active on soluble glycol-chitin, chitosan polymers with a high DA, and chitooligosaccharides, and shows low activity on insoluble alpha- and beta-chitin, which is reduced further by deletion of the CBM domains. On chitooligosaccharides, it is active against oligomers with a DP >2, leading to fully deacetylated products. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms. The mode of action of Podospora anserina CDA on DP3 and DP4 substrates reveals that it follows a multiple-chain mechanism. With the trimer, all possible isomers are found for both mono- and di-deacetylated intermediate products, although the first deacetylation event has a clear preference for the reducing end. This is not the case for the tetramer and pentamer substrates, where the residue next to the reducing end is preferentially deacetylated first, with the second deacetylation occurring mainly next to the existing GlcNH2 unit on either side. Overall, larger oligomers are deacetylated faster, with deacetylation of the reducing end occurring as a late event Podospora anserina ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. PcCDA deacetylates chitooligosaccharides, requiring at least four GlcNAc units in order to be active, but it prefers longer substrates. For DP4 and DP5 substrates, it first deacetylates the penultimate residue from the non-reducing end, and continues to the next residue towards the reducing end, with a pattern of acetylation Pochonia chlamydosporia 170 ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms. The enzyme from Puccinia graminis is not active on insoluble polymers such as alpha- or beta-chitin. The sequence of the products obtained by enzymatic deacetylation of tetramers to hexamers reveals that the enzyme specifically deacetylates all but the last two GlcNAc units on the non-reducing end via a multiple-chain mechanism Puccinia graminis f. sp. tritici race SCCL ?
-
 ?
3.5.1.41 additional information substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms. The enzyme from Puccinia graminis is not active on insoluble polymers such as alpha- or beta-chitin. The sequence of the products obtained by enzymatic deacetylation of tetramers to hexamers reveals that the enzyme specifically deacetylates all but the last two GlcNAc units on the non-reducing end via a multiple-chain mechanism Puccinia graminis f. sp. tritici CRL 75-36-700-3 ?
-
 ?
3.5.1.41 N,N'-diacetylchitobiose + H2O the enzyme deacetylates the non-reducing GlcNAc of N,N'-diacetylchitobiose Colletotrichum lindemuthianum deacetylated chitooligosaccharides + acetate
-
 r
3.5.1.41 N,N'-diacetylchitobiose + H2O
-
 Aspergillus nidulans ?
-
 r

Subunits

EC Number Subunits Comment Organism
3.5.1.41 More the enzyme protein is composed of the CE4 domain flanked by two CBM18 domains Podospora anserina

Synonyms

EC Number Synonyms Comment Organism
3.5.1.41 AnCDA
-
 Aspergillus nidulans
3.5.1.41 ArCE4
-
 Arthrobacter sp. Hiyo8
3.5.1.41 CDA
-
 Vibrio parahaemolyticus
3.5.1.41 CDA
-
 Podospora anserina
3.5.1.41 CDA
-
 Colletotrichum lindemuthianum
3.5.1.41 CDA
-
 Vibrio cholerae
3.5.1.41 CDA
-
 Amylomyces rouxii
3.5.1.41 CDA
-
 Sinorhizobium meliloti
3.5.1.41 CDA
-
 Aspergillus nidulans
3.5.1.41 CDA
-
 Puccinia graminis f. sp. tritici
3.5.1.41 CDA
-
 Pestalotiopsis sp.
3.5.1.41 CDA
-
 Pochonia chlamydosporia
3.5.1.41 CDA
-
 Arthrobacter sp. Hiyo8
3.5.1.41 chitin deacetylase 1
-
 Arthrobacter sp. Hiyo8
3.5.1.41 MrCDA
-
 Amylomyces rouxii
3.5.1.41 NodB
-
 Sinorhizobium meliloti
3.5.1.41 NodB deacetylase
-
 Sinorhizobium meliloti
3.5.1.41 PaCDA
-
 Podospora anserina
3.5.1.41 PcCDA
-
 Pochonia chlamydosporia
3.5.1.41 PesCDA
-
 Pestalotiopsis sp.
3.5.1.41 PgtCDA
-
 Puccinia graminis f. sp. tritici
3.5.1.41 VcCDA
-
 Vibrio cholerae
3.5.1.41 VpCDA
-
 Vibrio parahaemolyticus

General Information

EC Number General Information Comment Organism
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Vibrio parahaemolyticus
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Podospora anserina
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Colletotrichum lindemuthianum
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Vibrio cholerae
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Amylomyces rouxii
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Sinorhizobium meliloti
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Aspergillus nidulans
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Puccinia graminis f. sp. tritici
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Pestalotiopsis sp.
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Pochonia chlamydosporia
3.5.1.41 evolution the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms Arthrobacter sp. Hiyo8
3.5.1.41 additional information the chitin deacetylase from Colletotrichum lindemuthianum follows the multiple-chain mechanism, in which the enzyme forms an active enzyme-polymer complex, and catalyzes the hydrolysis of only one acetyl group before it dissociates and forms a new active complex Colletotrichum lindemuthianum
3.5.1.41 additional information the chitin deacetylase from Mucor rouxii follows the multiple-attack mechanism, in which binding of the enzyme to the polysaccharide chain is followed by a number of sequential deacetylations, after which the enzyme binds to another chain Amylomyces rouxii
3.5.1.41 additional information the chitin deacetylase from Rhizobium follows the single-chain mechanism, which refers to processive enzymes in which a number of catalytic events occur on a single substrate molecule, leading to sequential deacetylation Sinorhizobium meliloti
3.5.1.41 additional information the chitin deacetylase from Vibrio follows the single-chain mechanism, which refers to processive enzymes in which a number of catalytic events occur on a single substrate molecule, leading to sequential deacetylation Vibrio parahaemolyticus
3.5.1.41 additional information the chitin deacetylase from Vibrio follows the single-chain mechanism, which refers to processive enzymes in which a number of catalytic events occur on a single substrate molecule, leading to sequential deacetylation Vibrio cholerae
3.5.1.41 additional information the enzyme from Pestalotiopsis sp. follows a multiple-chain mechanism in which all residues are deacetylated, except the reducing end, and the last two GlcNAc residues from the non-reducing end, with a pattern of deacetylation Pestalotiopsis sp.
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases Vibrio parahaemolyticus
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases Podospora anserina
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases Colletotrichum lindemuthianum
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases Vibrio cholerae
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases Amylomyces rouxii
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases Puccinia graminis f. sp. tritici
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases Pestalotiopsis sp.
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases Pochonia chlamydosporia
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases Arthrobacter sp. Hiyo8
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases. Enzyme AnCDA is secreted into the extracellular medium to deacetylate the chitin oligomers produced by chitinases during cell autolysis Aspergillus nidulans
3.5.1.41 physiological function chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases. NodB deacetylases are involved in the biosynthesis of Nod factors, the morphogenic signal molecules produced by rhizobia, which initiate the development of root nodules in leguminous plants Sinorhizobium meliloti