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Literature summary for 3.5.1.41 extracted from

  • Cord-Landwehr, S.; Melcher, R.L.; Kolkenbrock, S.; Moerschbacher, B.M.
    A chitin deacetylase from the endophytic fungus Pestalotiopsis sp. efficiently inactivates the elicitor activity of chitin oligomers in rice cells (2016), Sci. Rep., 6, 38018 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.41

Inhibitors

Inhibitors Comment Organism Structure
ammonium acetate 20% inhibition at 100 mM Pestalotiopsis sp.
EDTA
-
 Pestalotiopsis sp.
Fe2+ causes almost complete inactivation Pestalotiopsis sp.
Mn2+ 50% inhibition Pestalotiopsis sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Pestalotiopsis sp.
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
 Pestalotiopsis sp.
Mg2+
-
 Pestalotiopsis sp.
Zn2+
-
 Pestalotiopsis sp.

Organism

Organism UniProt Comment Textmining
Pestalotiopsis sp. A0A1L3THR9
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information propagation in suspension-cultured rice cells Pestalotiopsis sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylated chitosan polymer + H2O increasing activity with increasing chain length Pestalotiopsis sp. ?
-
 ?
alpha-chitin + H2O
-
 Pestalotiopsis sp. ?
-
 ?
beta-chitin + H2O
-
 Pestalotiopsis sp. ?
-
 ?
chitin hexamer + H2O
-
 Pestalotiopsis sp. ?
-
 ?
chitosan hexamer + H2O
-
 Pestalotiopsis sp. ?
-
 ?
colloidal chitin + H2O high activity Pestalotiopsis sp. ?
-
 ?
additional information PesCDA modifies chitin oligomers, the products are partially deacetylated chitosan oligomers with a specific acetylation pattern: GlcNAc-GlcNAc-(GlcN)n-GlcNAc (n > 1). Substrate specificity with activity against chitosan polymers that have degrees of acetylation of 10-60% as well as against colloidal chitin, alpha-chitin and beta-chitin, overview Pestalotiopsis sp. ?
-
 ?

Subunits

Subunits Comment Organism
More domain architecture of the chitin deacetylase PesCDA from Pestalotiopsis sp.. The enzyme contains an N-terminal putative signal peptide (SP), a polysaccharide deacetylase domain (PDD), and a C-terminal carbohydrate binding module representing motif family 18 (CBM18) Pestalotiopsis sp.

Synonyms

Synonyms Comment Organism
CDA
-
 Pestalotiopsis sp.
PesCDA
-
 Pestalotiopsis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Pestalotiopsis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Pestalotiopsis sp.

General Information

General Information Comment Organism
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 Pestalotiopsis sp.
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 Pestalotiopsis sp.