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Literature summary for 3.5.1.41 extracted from

  • Aranda-Martinez, A.; Grifoll-Romero, L.; Aragunde, H.; Sancho-Vaello, E.; Biarnes, X.; Lopez-Llorca, L.V.; Planas, A.
    Expression and specificity of a chitin deacetylase from the nematophagous fungus Pochonia chlamydosporia potentially involved in pathogenicity (2018), Sci. Rep., 8, 2170 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.41

Cloned(Commentary)

Cloned (Comment) Organism
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

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Pochonia chlamydosporia
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc coordination analysis Pochonia chlamydosporia

Organism

Organism UniProt Comment Textmining
Pochonia chlamydosporia
-
-
-
Pochonia chlamydosporia 123
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme exhibits one potential N-linked glycosylation site and six potential O-glycosylation sites Pochonia chlamydosporia

Purification (Commentary)

Purification (Comment) Organism
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

Renatured (Commentary)

Renatured (Comment) Organism
recombinant Strep-tagged CDA catalytic domain from Escherichia coli strain BL21(DE3) inclusion bodies by solubilization in 7 M urea Pochonia chlamydosporia

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
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 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 48700, about, sequence calculation, x * 26800, recombinant Strep-tagged catalytic domain, SDS-PAGE Pochonia chlamydosporia

Synonyms

Synonyms Comment Organism
CDA
-
 Pochonia chlamydosporia
CE4 deacetylase
-
 Pochonia chlamydosporia
PcCDA
-
 Pochonia chlamydosporia
pc_2566
-
 Pochonia chlamydosporia

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Pochonia chlamydosporia

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Pochonia chlamydosporia

pI Value

Organism Comment pI Value Maximum pI Value
Pochonia chlamydosporia sequence calculation
-
 7.7

General Information

General Information Comment Organism
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
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
physiological function the enzyme might have a role in pathogenicity Pochonia chlamydosporia