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Literature summary for 3.2.1.18 extracted from
- Bifunctional properties and characterization of a novel sialidase with esterase activity from Bifidobacterium bifidum (2018), Biosci. Biotechnol. Biochem., 82, 2030-2039 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(lambdaDE3) cells | Bifidobacterium bifidum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | 30% residual activity at 5 mM | Bifidobacterium bifidum |  |
| additional information | EDTA has no significant effect on the enzyme activity | Bifidobacterium bifidum |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.28 | - |
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid | at pH 5.0 and 37°C | Bifidobacterium bifidum | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Bifidobacterium bifidum | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | Ca2+, Zn2+, Co2+, Mn2+ and Mg2+ have no significant effect on the enzyme activity | Bifidobacterium bifidum |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 463000 | - |
gel filtration | Bifidobacterium bifidum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bifidobacterium bifidum | - |
- |
- |
| Bifidobacterium bifidum JCM1254 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni-NTA column chromatography and Superdex 200 gel filtration | Bifidobacterium bifidum |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.00495 | - |
with 4-nitrophenyl acetate as substrate, at pH 5.0 and 37°C | Bifidobacterium bifidum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O | - |
Bifidobacterium bifidum | 4-methylumbelliferone + alpha-D-N-acetylneuraminic acid | - |
? | |
| 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O | - |
Bifidobacterium bifidum JCM1254 | 4-methylumbelliferone + alpha-D-N-acetylneuraminic acid | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Bifidobacterium bifidum | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Bifidobacterium bifidum JCM1254 | 4-nitrophenol + acetate | - |
? | |
| additional information | isoform SiaBb1 preferentially hydrolyzes alpah2,3-linked sialic acid over alpha2,6-linked sialic acid from sialoglycan. Isoform SiaBb1 also has an SGNH hydrolase domain with sialate-O-acetylesterase activity | Bifidobacterium bifidum | ? | - |
? | |
| additional information | no activity with 4-nitrophenyl butyrate, 4-nitrophenyl valerate, 4-nitrophenyl decanoate, 4-nitrophenyl palmitate, and 4-nitrophenyl phosphate | Bifidobacterium bifidum | ? | - |
? | |
| additional information | isoform SiaBb1 preferentially hydrolyzes alpah2,3-linked sialic acid over alpha2,6-linked sialic acid from sialoglycan. Isoform SiaBb1 also has an SGNH hydrolase domain with sialate-O-acetylesterase activity | Bifidobacterium bifidum JCM1254 | ? | - |
? | |
| additional information | no activity with 4-nitrophenyl butyrate, 4-nitrophenyl valerate, 4-nitrophenyl decanoate, 4-nitrophenyl palmitate, and 4-nitrophenyl phosphate | Bifidobacterium bifidum JCM1254 | ? | - |
? | |
| mucin of bovine submaxillary gland + H2O | - |
Bifidobacterium bifidum | sialic acid + ? | - |
? | |
| mucin of bovine submaxillary gland + H2O | - |
Bifidobacterium bifidum JCM1254 | sialic acid + ? | - |
? | |
| pyridylamino-3'-sialyllactose + H2O | - |
Bifidobacterium bifidum | ? | - |
? | |
| pyridylamino-6'-sialyllactose + H2O | - |
Bifidobacterium bifidum | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 190000, SDS-PAGE | Bifidobacterium bifidum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SiaBb1 | - |
Bifidobacterium bifidum |
| sialyl hydrolase | - |
Bifidobacterium bifidum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 45 | - |
Bifidobacterium bifidum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
the enzyme is stable at temperatures less than 40°C | Bifidobacterium bifidum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 33 | - |
4-methylumbelliferyl alpha-D-N-acetylneuraminic acid | at pH 5.0 and 37°C | Bifidobacterium bifidum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | - |
- |
Bifidobacterium bifidum |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 9 | the enzyme is stable over the pH range of 6.0-9.0 | Bifidobacterium bifidum |
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Release 2023.1 (January 2023)
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