EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.41 | gene pc_2566, sequence comparisons and phylogenetic tree, functional recombinant expression of C-terminally StrepII-tagged CDA catalytic domain in Escherichia coli strain BL21(DE3) in inclusion bodies | Pochonia chlamydosporia |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.5.1.41 | extracellular | - |
Pochonia chlamydosporia | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.41 | Zn2+ | zinc coordination analysis | Pochonia chlamydosporia |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.41 | Pochonia chlamydosporia | - |
- |
- |
3.5.1.41 | Pochonia chlamydosporia 123 | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.5.1.41 | glycoprotein | the enzyme exhibits one potential N-linked glycosylation site and six potential O-glycosylation sites | Pochonia chlamydosporia |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.1.41 | functional recombinant solubilized and refolded C-terminally Strep-tagged CDA catalytic domain expressed in Escherichia coli strain BL21(DE3) by affinity chromatography, dialysis, and ultrafiltration | Pochonia chlamydosporia |
EC Number | Renatured (Comment) | Organism |
---|---|---|
3.5.1.41 | recombinant Strep-tagged CDA catalytic domain from Escherichia coli strain BL21(DE3) inclusion bodies by solubilization in 7 M urea | Pochonia chlamydosporia |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.41 | acetylated chitosan oligosaccharide + H2O | the recombinant isolated catalytic domain displays deacetylase activity on chitooligosaccharides with a degree of polymerization (DP) larger than 3, generating mono- and di-deacetylated products with a pattern different from those of closely related fungal CDAs. On a DP5 substrate, PcCDA gave a single mono-deacetylated product in the penultimate position from the non-reducing end (ADAAA) which is then transformed into a di-deacetylated product (ADDAA). Structure-function relationships with regard to specificity and pattern of deacetylation | Pochonia chlamydosporia | ? | - |
? | |
3.5.1.41 | acetylated chitosan oligosaccharide + H2O | the recombinant isolated catalytic domain displays deacetylase activity on chitooligosaccharides with a degree of polymerization (DP) larger than 3, generating mono- and di-deacetylated products with a pattern different from those of closely related fungal CDAs. On a DP5 substrate, PcCDA gave a single mono-deacetylated product in the penultimate position from the non-reducing end (ADAAA) which is then transformed into a di-deacetylated product (ADDAA). Structure-function relationships with regard to specificity and pattern of deacetylation | Pochonia chlamydosporia 123 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.1.41 | ? | x * 48700, about, sequence calculation, x * 26800, recombinant Strep-tagged catalytic domain, SDS-PAGE | Pochonia chlamydosporia |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.41 | CDA | - |
Pochonia chlamydosporia |
3.5.1.41 | CE4 deacetylase | - |
Pochonia chlamydosporia |
3.5.1.41 | PcCDA | - |
Pochonia chlamydosporia |
3.5.1.41 | pc_2566 | - |
Pochonia chlamydosporia |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.41 | 37 | - |
assay at | Pochonia chlamydosporia |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.41 | 8 | - |
assay at | Pochonia chlamydosporia |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
3.5.1.41 | Pochonia chlamydosporia | sequence calculation | - |
7.7 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.1.41 | 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 | Pochonia chlamydosporia |
3.5.1.41 | 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 | Pochonia chlamydosporia |
3.5.1.41 | physiological function | the enzyme might have a role in pathogenicity | Pochonia chlamydosporia |