EC Number | Application | Comment | Organism |
---|---|---|---|
3.5.1.105 | synthesis | enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases. Production of chitosan oligomers by partial chemical or physical depolymerisation of the respective polymers has severe disadvantages. Not only does the production of the oligomers typically involve harsh thermo-chemical treatments or strong physical forces, which may be environmentally unfriendly and/or partially destructive to the oligosaccharides produced, but also the production is highly difficult to control leading to broad heterogeneous mixtures, and the outcome is strongly dependent on the chemical and physical characteristics of the starting material. Partial enzymatic hydrolysis of chitosan polymers using chitosan hydrolysing enzymes such as chitinases or chitosanases with well-defined cleavage specificities has been proposed as an alternative to chemical or physical depolymerisation. But, this attempt is also strongly dependent on the starting material and it, too, leads to the production of heterogeneous mixtures of chitosan oligomers. Still, due to the cleavage specificities of the enzymes, the resulting mixture will be better defined than the chitosan oligomer mixtures obtained by chemical or physical depolymerisation | Vibrio cholerae |
3.5.1.105 | synthesis | enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases. Production of chitosan oligomers by partial chemical or physical depolymerisation of the respective polymers has severe disadvantages. Not only does the production of the oligomers typically involve harsh thermo-chemical treatments or strong physical forces, which may be environmentally unfriendly and/or partially destructive to the oligosaccharides produced, but also the production is highly difficult to control leading to broad heterogeneous mixtures, and the outcome is strongly dependent on the chemical and physical characteristics of the starting material. Partial enzymatic hydrolysis of chitosan polymers using chitosan hydrolysing enzymes such as chitinases or chitosanases with well-defined cleavage specificities has been proposed as an alternative to chemical or physical depolymerisation. But, this attempt is also strongly dependent on the starting material and it, too, leads to the production of heterogeneous mixtures of chitosan oligomers. Still, due to the cleavage specificities of the enzymes, the resulting mixture will be better defined than the chitosan oligomer mixtures obtained by chemical or physical depolymerisation | Rhizobium sp. |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.105 | gene cod, recombinant expression of StrepII-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3) | Vibrio cholerae |
3.5.1.105 | gene nodB, recombinant expression of StrepII-tagged enzyme in Escherichia coli strain BL21(DE3) | Rhizobium sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.105 | Rhizobium sp. | A0A0N7AXL7 | - |
- |
3.5.1.105 | Rhizobium sp. GRH2 | A0A0N7AXL7 | - |
- |
3.5.1.105 | Vibrio cholerae | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.1.105 | recombinant StrepII-tagged enzyme from Escherichia coli strain BL21(DE3) by streptactin affinity chromatography | Rhizobium sp. |
3.5.1.105 | recombinant StrepII-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) by streptactin affinity chromatography | Vibrio cholerae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.105 | additional information | enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases, method evaluation and optiization, overview. Production of specific chitosan oligomers which are deacetylated at the first two units starting from the non-reducing end by the combined use of two different chitin deacetylases, namely NodB from Rhizobium sp. GRH2 that deacetylates the first unit and chitin oligosaccharide deacetylase (COD) from Vibrio cholerae that deacetylates the second unit starting from the non-reducing end. Both chitin deacetylases accept the product of each other resulting in production of chitosan oligomers with a novel and defined PA. COD deacetylates the second unit from the non-reducing end. COD is active on short chitin oligosaccharides | Vibrio cholerae | ? | - |
? | |
3.5.1.105 | additional information | enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases, method evaluation and optimization, overview. Production of specific chitosan oligomers which are deacetylated at the first two units starting from the non-reducing end by the combined use of two different chitin deacetylases, namely NodB from Rhizobium sp. GRH2 that deacetylates the first unit and COD from Vibrio cholerae that deacetylates the second unit starting from the non-reducing end. Both chitin deacetylases accept the product of each other resulting in production of chitosan oligomers with a novel and defined PA. NodB deacetylates exclusively the GlcNAc unit at the non-reducing end. The chitin deacetylase activity of NodB is tested against GlcNAc1-6. NodB is not active towards GlcNAc1, but converts GlcNAc2-6 completely into mono-deacetylated chitosan oligomers | Rhizobium sp. | ? | - |
? | |
3.5.1.105 | additional information | enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases, method evaluation and optimization, overview. Production of specific chitosan oligomers which are deacetylated at the first two units starting from the non-reducing end by the combined use of two different chitin deacetylases, namely NodB from Rhizobium sp. GRH2 that deacetylates the first unit and COD from Vibrio cholerae that deacetylates the second unit starting from the non-reducing end. Both chitin deacetylases accept the product of each other resulting in production of chitosan oligomers with a novel and defined PA. NodB deacetylates exclusively the GlcNAc unit at the non-reducing end. The chitin deacetylase activity of NodB is tested against GlcNAc1-6. NodB is not active towards GlcNAc1, but converts GlcNAc2-6 completely into mono-deacetylated chitosan oligomers | Rhizobium sp. GRH2 | ? | - |
? | |
3.5.1.105 | N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O | - |
Vibrio cholerae | GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate | - |
? | |
3.5.1.105 | N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O | - |
Rhizobium sp. | GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate | - |
? | |
3.5.1.105 | N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O | - |
Rhizobium sp. GRH2 | GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.105 | chitin oligosaccharide deacetylase | - |
Vibrio cholerae |
3.5.1.105 | COD | - |
Vibrio cholerae |
3.5.1.105 | NodB | - |
Rhizobium sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.105 | 37 | - |
recombinant enzyme | Rhizobium sp. |
3.5.1.105 | 45 | - |
recombinant enzyme | Vibrio cholerae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.105 | 8 | - |
recombinant enzyme | Vibrio cholerae |
3.5.1.105 | 9 | - |
recombinant enzyme | Rhizobium sp. |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.1.105 | additional information | pattern of acetylation of GlcNAc5 after hydrolysis with NodB from Rhizobium sp. strain GRH2 by enzymatic sequencing in combination with UHPLC-ELSD-ESI-MS analysis, overview | Rhizobium sp. |