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Literature summary extracted from
- Isolation and properties of two sialate-O-acetylesterases from horse liver with 4- and 9-O-acetyl specificities (2008), Glycoconj. J., 25, 625-632.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.1.1.53 | partially purified esterase (from second ion exchange chromatography) resistant to freezing-thawing cycles, presence of beta-mercaptoethanol during purification preserves enzyme activity | Equus sp. |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.53 | diisopropylfluorophosphate | 1 mM, 25°C, 15 min, total loss of activity | Equus sp. |  |
| 3.1.1.53 | additional information | bis-(4-nitrophenyl)phosphate, 1 mM Ca2+, 1 mM ethylene diaminotetraacetate (EDTA) without influence on activity | Equus sp. | |
| 3.1.1.53 | paraoxon | diethyl-4-nitrohenylphosphate (E600), 1 mM at 25°C within 15 min leads to total loss of activity | Equus sp. | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.53 | 0.3 | - |
4-O-acetyl-sialic acid | low pI esterase form, obtained with free sialic acid | Equus sp. | |
| 3.1.1.53 | 1.1 | - |
9-O-acetyl-sialic acid | low pI esterase form, obtained with free sialic acid | Equus sp. | |
| 3.1.1.53 | 1.3 | - |
9-O-acetyl-sialic acid | high pI esterase form, obtained with free sialic acid | Equus sp. | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.53 | Cu2+ | 1 mM, block of essential SH-groups | Equus sp. | |
| 3.1.1.53 | Hg2+ | 1 mM, block of essential SH-groups | Equus sp. | |
| 3.1.1.53 | Zn2+ | 1 mM, block of essential SH-groups | Equus sp. | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.53 | 54000 | - |
gel-filtration | Equus sp. |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.53 | Equus sp. | - |
- |
- |
Oxidation Stability
| EC Number | Oxidation Stability | Organism |
|---|---|---|
| 3.1.1.53 | 15 min incubation with 1 mM 4-hydroxymercuribenzoate at 25°C leads to total loss of activity | Equus sp. |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.1.53 | from fresh tissue by ultracentrifugation (dialysis of supernatant), followed by gel-filtration on Sephadex G-200 column, ion-exchange chromatography on Sephadex-DEAE-A-50 column, second ion-exchange chromatography on DEAE-Sephacel column, isoelectric focussing on ampholine of pH 3.5-9.5 and a saccharose gradient, and final dialysis, 866% purification compared to homogenate | Equus sp. |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.1.1.53 | liver | - |
Equus sp. | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.53 | 0.00012 | - |
homogenate | Equus sp. |
| 3.1.1.53 | 0.104 | - |
after preparative isoelectric focussing, pI 4.8 | Equus sp. |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 3.1.1.53 | -20°C, after preparative isoelectric focusing, few weeks, total loss of activity, -70°C, frozen liver, stable for 1-2 years | Equus sp. |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.53 | 4-O-acetyl sialic acid + H2O | - |
Equus sp. | sialic acid + acetate | - |
? | |
| 3.1.1.53 | 9-O-acetyl sialic acid + H2O | - |
Equus sp. | sialic acid + acetate | - |
? | |
| 3.1.1.53 | additional information | alpha-naphthylacetate, 9-O-acetyl sialyllactose, serum alpha1 acid glycoprotein, and erythrocyte membranes containing N-acetyl-4-O-acetylneuraminic acid or N-acetyl-9-O-acetylneuraminic acid are susceptible to SOAE catalysed hydrolysis | Equus sp. | ? | - |
? | |
| 3.1.1.53 | additional information | glycosidically linked sialic acids are also substrate, hydrolysis of 20% under standard conditions | Equus sp. | ? | - |
? | |
| 3.1.1.53 | additional information | liberation of sialic acid from gland mucin (mainly containing N-acetyl-4-O-acetylneuraminic acid) | Equus sp. | ? | - |
? | |
| 3.1.1.53 | additional information | N-acetyl-4-O-acetylneuraminic acid is slightly preferred over N-acetyl-9-O-acetylneuraminic acid as substrate for esterase with pI 5.7 | Equus sp. | ? | - |
? | |
| 3.1.1.53 | additional information | N-acetyl-7-O-acetylneuraminic acid is no substrate | Equus sp. | ? | - |
? | |
| 3.1.1.53 | N-acetyl-4-O-acetylneuraminic acid + H2O | pH 8, 30 min, 37°C, catalysed only by esterase with pI 5.7 | Equus sp. | N-acetylneuraminate + acetate | analyses by HPLC | ? | |
| 3.1.1.53 | N-acetyl-9-O-acetylneuraminic acid + H2O | pH 8, 30 min, 37°C, catalysed by esterase with pI 4.8 and esterase with pI 5.7 | Equus sp. | N-acetylneuraminate + acetate | analyses by HPLC | ? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.53 | sialate esterase | - |
Equus sp. |
| 3.1.1.53 | sialate-O-acetylesterase | - |
Equus sp. |
| 3.1.1.53 | SOAE | - |
Equus sp. |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.53 | 8.4 | 8.6 | - |
Equus sp. |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.53 | 7 | - |
60% lower activity compared to optimum | Equus sp. |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.1.1.53 | Equus sp. | isoelectric focusing, low pI form | - |
4.8 |
| 3.1.1.53 | Equus sp. | isoelectric focusing, high pI form | - |
5.7 |
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