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Literature summary for 3.5.1.41 extracted from

  • Kang, L.; Liang, Y.; Ma, L.
    Novel characteristics of chitin deacetylase from Colletotrichum lindemuthianum: production of fully acetylated chitooligomers, and hydrolysis of deacetylated chitooligomers (2014), Process Biochem., 49, 1936-1940.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Pichia pastoris Colletotrichum lindemuthianum

Organism

Organism UniProt Comment Textmining
Colletotrichum lindemuthianum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
monoacetylated chitopentaose + H2O
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Colletotrichum lindemuthianum chitopentaose + acetate
-
?
monoacetylated chitotetraose + H2O
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Colletotrichum lindemuthianum chitotetraose + acetate
-
?
monoacetylated chitotriose + H2O
-
Colletotrichum lindemuthianum chitotriose + acetate
-
?
additional information the recombinant enzyme deacetylates the complex oligosaccharide substrates with various acetyls produced by endo-chitosanase from Aspergillus fumigatus hydrolyzing chitosan. Substrate and product identification by mass spectrometric analysis, overview. (GlcNAc)4 is fully deacetylated into (GlcN)4, and the enzyme deacetylates (GlcNAc)4 and (GlcNAc)5 much faster than (GlcNAc)3 and (GlcNAc)2. Chitotriose is also fully deacetylated through a random deacetylation process, while chitobiose (GlcNAc)2, is only deacetylated at the non-reducing GlcNAc residue. The enzyme exclusively produces Glc-NGlcNAc, and cannot deacetylate GlcNAc Colletotrichum lindemuthianum ?
-
?

Synonyms

Synonyms Comment Organism
ClCDA
-
Colletotrichum lindemuthianum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
assay at Colletotrichum lindemuthianum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Colletotrichum lindemuthianum