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Literature summary extracted from
- Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine (1972), Biochim. Biophys. Acta, 284, 235-247.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.48 | 6-Bromo-2-naphthyl-alpha-glucoside | - |
Rattus rattus |  |
| 3.2.1.48 | maltose | - |
Rattus rattus | |
| 3.2.1.48 | p-Nitrophenyl-alpha-glucoside | competitive inhibitor, inhibits both sucrase and isomaltase | Rattus rattus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.48 | 0.12 | - |
6-bromo-2-naphthyl-alpha-D-glucoside | - |
Rattus rattus | |
| 3.2.1.48 | 1.5 | - |
p-nitrophenyl-alpha-D-glucoside | - |
Rattus rattus | |
| 3.2.1.48 | 3.1 | - |
p-nitrophenyl-alpha-D-glucoside | - |
Rattus rattus | |
| 3.2.1.48 | 7.2 | - |
maltose | - |
Rattus rattus | |
| 3.2.1.48 | 11.5 | - |
isomaltose | - |
Rattus rattus | |
| 3.2.1.48 | 13.5 | - |
maltose | the existence of 2 Km values supports the notion of substrate hydrolysis at 2 active sites on the sucrase-isomaltase complex | Rattus rattus | |
| 3.2.1.48 | 30.8 | - |
sucrose | - |
Rattus rattus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.48 | Na+ | - |
Rattus rattus | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.48 | isomaltose + H2O | Rattus rattus | - |
glucose | - |
? | |
| 3.2.1.48 | maltose + H2O | Rattus rattus | - |
2 glucose | - |
? | |
| 3.2.1.48 | sucrose + H2O | Rattus rattus | - |
D-glucose + D-fructose | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.48 | Rattus rattus | - |
sucrase-isomaltase | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.48 | - |
Rattus rattus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.48 | 6-bromo-2-naphthyl-alpha-D-glucoside + H2O | - |
Rattus rattus | 6-bromonaphthol + alpha-D-glucose | - |
? | |
| 3.2.1.48 | dextran + H2O | - |
Rattus rattus | D-glucose | - |
? | |
| 3.2.1.48 | isomaltose + H2O | - |
Rattus rattus | glucose | - |
? | |
| 3.2.1.48 | isomaltose + H2O | - |
Rattus rattus | 2 D-glucose | - |
? | |
| 3.2.1.48 | maltose + H2O | - |
Rattus rattus | 2 glucose | - |
? | |
| 3.2.1.48 | maltose + H2O | - |
Rattus rattus | 2 D-glucose | - |
? | |
| 3.2.1.48 | p-nitrophenyl-alpha-glucoside + H2O | - |
Rattus rattus | p-nitrophenol + D-glucose | - |
? | |
| 3.2.1.48 | sucrose + H2O | - |
Rattus rattus | D-glucose + D-fructose | - |
? | |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.48 | 50 | - |
pH 5.9, inactivation, soluble enzyme activity is stable to heat treatment, membrane associated enzyme was heat-labile under these conditions | Rattus rattus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.48 | 5.9 | - |
in the presence of 50 mM Na+ | Rattus rattus |
| 3.2.1.48 | 6.7 | - |
- |
Rattus rattus |
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