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Literature summary for 3.5.1.105 extracted from
- Chitin oligosaccharide deacetylase from Shewanella baltica ATCC BAA-1091 (2017), Biosci. Biotechnol. Biochem., 81, 547-550 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Sbal_1411, cloning in Escherichia coli strain DH5alpha and recombinant expression in Escherichia coli strain HMS174(DE3), the recombinant protein is secreted to the culture medium | Shewanella baltica |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.83 | - |
N,N'-diacetylchitobiose | pH 8.0, 37°C | Shewanella baltica |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| chitin + H2O | Shewanella baltica | - |
? | - |
? | |
| chitin + H2O | Shewanella baltica OS155 | - |
? | - |
? | |
| chitin + H2O | Shewanella baltica ATCC BAA-1091 | - |
? | - |
? | |
| additional information | Shewanella baltica | chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2 | ? | - |
? | |
| additional information | Shewanella baltica OS155 | chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2 | ? | - |
? | |
| additional information | Shewanella baltica ATCC BAA-1091 | chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2 | ? | - |
? | |
| N,N'-diacetylchitobiose + H2O | Shewanella baltica | - |
N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Shewanella baltica | A3D2G6 | - |
- |
| Shewanella baltica ATCC BAA-1091 | A3D2G6 | - |
- |
| Shewanella baltica OS155 | A3D2G6 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli strain HMS174(DE3) by ammonium sulfate fractionation, anion exchange and hydrophic interaction chromatography, ultrafiltration, and gel filtration | Shewanella baltica |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.029 | - |
purified recombinant enzyme, pH 8.0, 37°C, substrate N,N',N''-triacetylchitotriose | Shewanella baltica |
| 0.22 | - |
purified recombinant enzyme, pH 8.0, 37°C, substrate N,N',N'',N'''-tetraacetylchitotetraose | Shewanella baltica |
| 9.4 | - |
purified recombinant enzyme, pH 8.0, 37°C, substrate N,N'-diacetylchitobiose | Shewanella baltica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| chitin + H2O | - |
Shewanella baltica | ? | - |
? | |
| chitin + H2O | - |
Shewanella baltica OS155 | ? | - |
? | |
| chitin + H2O | - |
Shewanella baltica ATCC BAA-1091 | ? | - |
? | |
| additional information | chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2 | Shewanella baltica | ? | - |
? | |
| additional information | product determination by reaction with beta-N-acetylhexisosaminidase (NAGase), an exo-type glycosidase that liberates GlcNAc from non-reducing end of N-acetyl-beta-D-hexosaminides, detected by TLC. No activity of the recombinant enzyme with N-acetyl-D-glucosamine | Shewanella baltica | ? | - |
? | |
| additional information | chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2 | Shewanella baltica OS155 | ? | - |
? | |
| additional information | product determination by reaction with beta-N-acetylhexisosaminidase (NAGase), an exo-type glycosidase that liberates GlcNAc from non-reducing end of N-acetyl-beta-D-hexosaminides, detected by TLC. No activity of the recombinant enzyme with N-acetyl-D-glucosamine | Shewanella baltica OS155 | ? | - |
? | |
| additional information | chitin oligosaccharide deacetylase (COD) is an enzyme that catalyzes the hydrolysis of the acetamide bond of the second N-acetyl-D-glucosamine (GlcNAc) residue from the non-reducing end of chitin oligosaccharides and shows the highest activity against N,N'-diacetylchitobiose (GlcNAc)2 | Shewanella baltica ATCC BAA-1091 | ? | - |
? | |
| additional information | product determination by reaction with beta-N-acetylhexisosaminidase (NAGase), an exo-type glycosidase that liberates GlcNAc from non-reducing end of N-acetyl-beta-D-hexosaminides, detected by TLC. No activity of the recombinant enzyme with N-acetyl-D-glucosamine | Shewanella baltica ATCC BAA-1091 | ? | - |
? | |
| N,N',N'',N'''-tetraacetylchitotetraose + H2O | - |
Shewanella baltica | ? | - |
? | |
| N,N',N'',N'''-tetraacetylchitotetraose + H2O | - |
Shewanella baltica OS155 | ? | - |
? | |
| N,N',N'',N'''-tetraacetylchitotetraose + H2O | - |
Shewanella baltica ATCC BAA-1091 | ? | - |
? | |
| N,N',N''-triacetylchitotriose + H2O | - |
Shewanella baltica | ? | - |
? | |
| N,N',N''-triacetylchitotriose + H2O | - |
Shewanella baltica OS155 | ? | - |
? | |
| N,N',N''-triacetylchitotriose + H2O | - |
Shewanella baltica ATCC BAA-1091 | ? | - |
? | |
| N,N'-diacetylchitobiose + H2O | - |
Shewanella baltica | N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate | - |
? | |
| N,N'-diacetylchitobiose + H2O | preferred substrate | Shewanella baltica | N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| COD | - |
Shewanella baltica |
| Sb-COD | - |
Shewanella baltica |
| Sbal_1411 | - |
Shewanella baltica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
recombinant enzyme | Shewanella baltica |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 17 | - |
N,N'-diacetylchitobiose | pH 8.0, 37°C | Shewanella baltica | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
recombinant enzyme | Shewanella baltica |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | chitin oligosaccharide deacetylase (COD) typically comprise two carbohydrate-binding domains (CBDs) and one polysaccharide deacetylase domain. In contrast, Shewanella baltica ATCC BAA-1091 COD (Sb-COD) has only one CBD, yet exhibits chitin-binding properties and substrate specificities similar to those of other CODs | Shewanella baltica |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 20.5 | - |
N,N'-diacetylchitobiose | pH 8.0, 37°C | Shewanella baltica | |
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Release 2023.1 (January 2023)
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