Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
CDA belongs to the carbohydrate esterase family 4 (CE4) according to the classification of the CAZY database
evolution
-
chitin deacetylases belong to family 4 of carbohydrate esterases. All CE4 enzymes share the NodB homologous domain, with a distorted (beta/alpha)8 barrel structure17 that contains the catalytic active site
evolution
A0A1U8QU02
chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
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
evolution
evolutionary relationships, phylogenetic analysis
evolution
sequence comparisons to CDAs from Tribolium castaneum, Bombyx mori, Drosophila melanogaster, Anopheles gambiae, Oxya chinensis, and Choristoneura funiferana
evolution
the CDA from Podospora anserina (PaCDA) is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. The catalytic domain of PaCDA is also functionally similar to Colletotrichum lindemuthianum CDA, though differing in detail
evolution
-
the CdaYJ is homologous to some known chitin deacetylases and contains conserved chitin deacetylase active sites. CdaYJ protein exhibits a long N-terminal and a relative short C-terminal. Phylogenetic analysis reveals that CdaYJ shows highest homology to CDAs from Alphaproteobacteria. Construction of metagenomic library of the Arctic deep-sea sediments, phylogenetic analysis of CdaYJ
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
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
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
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
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
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
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
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
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
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
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
evolution
-
chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
-
evolution
-
chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
-
evolution
-
chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
-
evolution
-
the CDA from Podospora anserina (PaCDA) is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. The catalytic domain of PaCDA is also functionally similar to Colletotrichum lindemuthianum CDA, though differing in detail
-
evolution
-
the CDA from Podospora anserina (PaCDA) is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. The catalytic domain of PaCDA is also functionally similar to Colletotrichum lindemuthianum CDA, though differing in detail
-
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
-
evolution
-
chitin deacetylases belong to family 4 of carbohydrate esterases. All CE4 enzymes share the NodB homologous domain, with a distorted (beta/alpha)8 barrel structure17 that contains the catalytic active site
-
evolution
-
CDA belongs to the carbohydrate esterase family 4 (CE4) according to the classification of the CAZY database
-
evolution
-
chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
-
evolution
Puccinia graminis f. sp. tritici race SCCL
-
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
-
evolution
-
the CDA from Podospora anserina (PaCDA) is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. The catalytic domain of PaCDA is also functionally similar to Colletotrichum lindemuthianum CDA, though differing in detail
-
evolution
-
chitin deacetylases belong to the family 4 of carbohydrate esterases (CE4)
-
evolution
-
the CDA from Podospora anserina (PaCDA) is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. The catalytic domain of PaCDA is also functionally similar to Colletotrichum lindemuthianum CDA, though differing in detail
-
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
-
malfunction
enzyme silencing results in abnormal molting phenotypes
malfunction
analysis of LmCDA5a knockout mutant phenotype, overview. Silencing of LmCDA5a does not affect the chitin content and organization
malfunction
analysis of LmCDA5a knockout mutant phenotype, overview. Silencing of LmCDA5b does not affect the chitin content and organization
malfunction
LmCDA2-deficient cuticle is less compact suggesting that LmCDA2 is needed for chitin packaging. Animals with reduced LmCDA2 activity die at molting, underlining that correct chitin organization is essential for survival
malfunction
silencing of LmCDA4 does not affect the chitin content and organization
metabolism
CDA is a key enzyme involved in the chitin metabolism
metabolism
model for plant cell recognition of fungi containing chitin in their cell walls and hypothetical fungal strategy to overcome recognition by the plant immune system. Chitin in the fungal cell wall, consisting of N-acetyl-D-glucosamine units, is degraded by plant chitinases
physiological function
-
chitin deacetylase is required for proper spore formation
physiological function
-
the enzyme is associated with cell wall synthesis
physiological function
the strong expression of CfCDA2 in the epidermis of molting individuals points to an important role of this gene in the molting process of Choristoneura fumiferana
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
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
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
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
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
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
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
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
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
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
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
physiological function
chitin deacetylase converts chitin into chitosan, the N-deacetylated form of chitin, which influences the mechanical and permeability properties of structures such as the cuticle and peritrophic matrices
physiological function
in fungi, the key enzymes that convert chitin to chitosan are chitin deacetylases (CDA). Chitin deacetylase from the endophytic fungus Pestalotiopsis sp. efficiently inactivates the elicitor activity of chitin oligomers in rice cells. A bioactivity assay where suspension-cultured rice cells are incubated with the PesCDA products (processed chitin hexamers), chitosan oligomer products no longer elicit the plant immune system, unlike the substrate hexamers. The endophytic enzyme can prevent the endophyte from being recognized by the plant immune system
physiological function
LmCDA2-mediated chitin deacetylation at the beginning of chitin production is a decisive reaction that triggers helicoidal arrangement of subsequently assembled chitin-protein microfibrils. In the body cuticle of nymphs of the migratory locust Locusta migratoria, helicoidal chitin organization is changed to an organization with unidirectional microfibril orientation. The enzyme is involved in cuticle organization. LmCDA2 is needed for tracheal cuticle formation and feeding, and LmCDA2 is required for locust molting and development
physiological function
proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin
physiological function
the CDA enzyme plays a significant role only during the growth phase of the fungus
physiological function
the enzyme is involved in the molting process of Locusta migratoria
physiological function
the enzyme is invovled in the molting process of Locusta migratoria
physiological function
-
the enzyme might have a role in pathogenicity
physiological function
-
proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin
-
physiological function
-
proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin
-
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
-
physiological function
-
the enzyme might have a role in pathogenicity
-
physiological function
Puccinia graminis f. sp. tritici race SCCL
-
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
-
physiological function
-
proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin
-
physiological function
-
proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin
-
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
-
physiological function
-
the CDA enzyme plays a significant role only during the growth phase of the fungus
-
additional information
the enzyme sequence has a 16 amino acid residue signal peptide, a putative polysaccharide deacetylase-like domain (residues 46-182), and 15 cysteine residues present in three clusters, residues 24-83, 183-243, and 332-365, structure comparison, overview
additional information
-
the enzyme sequence has a 16 amino acid residue signal peptide, a putative polysaccharide deacetylase-like domain (residues 46-182), and 15 cysteine residues present in three clusters, residues 24-83, 183-243, and 332-365, structure comparison, overview
additional information
-
the enzyme structure shows presence of 56.26% alpha-helical and 15.63% beta-helical structures, structure comparison, overview
additional information
the isoforms differ only in the alternatively spliced region, representing 43 and 37 amino acid residues in isoforms A and B, respectively
additional information
the isoforms differ only in the alternatively spliced region, representing 43 and 37 amino acid residues in isoforms A and B, respectively
additional information
-
the isoforms differ only in the alternatively spliced region, representing 43 and 37 amino acid residues in isoforms A and B, respectively
additional information
Absidia orchidis vel coerulea
-
chitin deacetylase is the only known enzyme that can deacetylate the N-acetyl-D-glucosamine units in chitin and chitosan to D-glucosamine
additional information
A0A1U8QU02
His-His-Asp catalytic triad
additional information
-
identification and characterization of a chitin deacetylase from a metagenomic library of deep-sea sediments of the arctic ocean, genotyping
additional information
mode of action on chitin, overview
additional information
-
mode of action on chitin, overview
additional information
molecular structure-function relationships, three-dimensional modeling. Bioinformatic analysis of the chitin deacetylase PgtCDA gene
additional information
-
molecular structure-function relationships, three-dimensional modeling. Bioinformatic analysis of the chitin deacetylase PgtCDA gene
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
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
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
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
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
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
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
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
additional information
-
the extracellular CE4 deacetylase has two CBM18 chitin binding modules, molecular modelling of the PcCDA catalytic domain and ligand docking using 2IW0 and 2Y8U as templates, overview. Structure-function relationships with regard to specificity and pattern of deacetylation. The catalytic domain (CE4 domain, residues 107 to 303) is flanked by two (N- and C-terminal) CBM18 modules (residues 30 to 74 and 360 to 441, respectively). These family 18 carbohydrate binding modules are typically involved in chitin binding. PcCDA full-length protein includes 25 cysteine residues, of which only two are located in the CE4 catalytic domain
additional information
Absidia orchidis vel coerulea NCAIM F00642
-
chitin deacetylase is the only known enzyme that can deacetylate the N-acetyl-D-glucosamine units in chitin and chitosan to D-glucosamine
-
additional information
-
His-His-Asp catalytic triad
-
additional information
-
His-His-Asp catalytic triad
-
additional information
-
His-His-Asp catalytic triad
-
additional information
-
mode of action on chitin, overview
-
additional information
-
mode of action on chitin, overview
-
additional information
-
the extracellular CE4 deacetylase has two CBM18 chitin binding modules, molecular modelling of the PcCDA catalytic domain and ligand docking using 2IW0 and 2Y8U as templates, overview. Structure-function relationships with regard to specificity and pattern of deacetylation. The catalytic domain (CE4 domain, residues 107 to 303) is flanked by two (N- and C-terminal) CBM18 modules (residues 30 to 74 and 360 to 441, respectively). These family 18 carbohydrate binding modules are typically involved in chitin binding. PcCDA full-length protein includes 25 cysteine residues, of which only two are located in the CE4 catalytic domain
-
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
-
additional information
-
His-His-Asp catalytic triad
-
additional information
-
mode of action on chitin, overview
-
additional information
-
His-His-Asp catalytic triad
-
additional information
-
mode of action on chitin, overview
-
additional information
-
the enzyme structure shows presence of 56.26% alpha-helical and 15.63% beta-helical structures, structure comparison, overview
-