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Literature summary for 3.5.1.41 extracted from

  • Hossbach, J.; Busswinkel, F.; Kranz, A.; Wattjes, J.; Cord-Landwehr, S.; Moerschbacher, B.M.
    A chitin deacetylase of Podospora anserina has two functional chitin binding domains and a unique mode of action (2018), Carbohydr. Polym., 183, 1-10 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic tree, recombinant expression of Strep-tagged enzyme in Hansenula polymorpha strain RB11 Podospora anserina

Protein Variants

Protein Variants Comment Organism
additional information generation of enzyme deletion mutants lacking one or both chitin-binding domains, CBDs Podospora anserina

Inhibitors

Inhibitors Comment Organism Structure
Co2+ 80.9% inhibition at 10 mM, 19.4% at 1 mM Podospora anserina
EDTA moderate inhibition at 10 mM Podospora anserina
Fe2+ 70.5% inhibition at 10 mM Podospora anserina
Mn2+ 9% activating at 1 mM, 22.6% inhibition at 10 mM Podospora anserina
additional information no inhibition by 100 mM acetate Podospora anserina
Zn2+ 98.3% inhibition at 10 mM, 68.3% at 1 mM Podospora anserina

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ 9% activating at 1 mM, 22.6% inhibition at 10 mM Podospora anserina

Organism

Organism UniProt Comment Textmining
Podospora anserina B2AAQ0 i.e. Pleurage anserina
-
Podospora anserina ATCC MYA-4624 B2AAQ0 i.e. Pleurage anserina
-
Podospora anserina DSM 980 B2AAQ0 i.e. Pleurage anserina
-
Podospora anserina FGSC 10383 B2AAQ0 i.e. Pleurage anserina
-
Podospora anserina S B2AAQ0 i.e. Pleurage anserina
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Strep-tagged enzyme from Hansenula polymorpha strain RB11 by StrepTactin affinity chromatography Podospora anserina

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylated chitin oligomer + H2O
-
Podospora anserina ?
-
?
acetylated chitin oligomer + H2O
-
Podospora anserina ATCC MYA-4624 ?
-
?
acetylated chitin oligomer + H2O
-
Podospora anserina DSM 980 ?
-
?
acetylated chitin oligomer + H2O
-
Podospora anserina FGSC 10383 ?
-
?
acetylated chitin oligomer + H2O
-
Podospora anserina S ?
-
?
acetylated chitosan oligomer + H2O increasing activity with increasing degree of acetylation Podospora anserina ?
-
?
alpha-chitin + H2O
-
Podospora anserina ?
-
?
alpha-chitin + H2O
-
Podospora anserina ATCC MYA-4624 ?
-
?
alpha-chitin + H2O
-
Podospora anserina DSM 980 ?
-
?
alpha-chitin + H2O
-
Podospora anserina FGSC 10383 ?
-
?
alpha-chitin + H2O
-
Podospora anserina S ?
-
?
beta-chitin + H2O
-
Podospora anserina ?
-
?
beta-chitin + H2O
-
Podospora anserina ATCC MYA-4624 ?
-
?
beta-chitin + H2O
-
Podospora anserina DSM 980 ?
-
?
beta-chitin + H2O
-
Podospora anserina FGSC 10383 ?
-
?
beta-chitin + H2O
-
Podospora anserina S ?
-
?
chitin pentamer + H2O
-
Podospora anserina ?
-
?
colloidal chitin + H2O high activity Podospora anserina ?
-
?
colloidal chitin + H2O high activity Podospora anserina ATCC MYA-4624 ?
-
?
colloidal chitin + H2O high activity Podospora anserina DSM 980 ?
-
?
colloidal chitin + H2O high activity Podospora anserina FGSC 10383 ?
-
?
colloidal chitin + H2O high activity Podospora anserina S ?
-
?
additional information analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing Podospora anserina ?
-
?
additional information analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing Podospora anserina ATCC MYA-4624 ?
-
?
additional information analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing Podospora anserina DSM 980 ?
-
?
additional information analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing Podospora anserina FGSC 10383 ?
-
?
additional information analysis of the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing Podospora anserina S ?
-
?

Subunits

Subunits Comment Organism
? x * 40000, about, sequence calculation, x * 35500, recombinant enzyme, SDS-PAGE Podospora anserina

Synonyms

Synonyms Comment Organism
CDA
-
Podospora anserina
PaCDA
-
Podospora anserina
PODANS_1_4780
-
Podospora anserina

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
broad optimum at 40-60°C Podospora anserina

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 90 activity range, profile overview Podospora anserina

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
purified recombinant enzyme, half-life is 11.8 min Podospora anserina

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10.5
-
-
Podospora anserina

pH Range

pH Minimum pH Maximum Comment Organism
4 12 activity range, almost linear increase of activity over the pH range 4.0-10.5 Podospora anserina

General Information

General Information Comment Organism
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 Podospora anserina
additional information mode of action on chitin, overview Podospora anserina
physiological function proposed function of the enzyme in conversion of the insoluble substrate colloidal chitin Podospora anserina