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Literature summary extracted from
- The catalytic and other residues essential for the activity of the midgut trehalase from Spodoptera frugiperda (2010), Insect Biochem. Mol. Biol., 40, 733-741.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.28 | - |
Spodoptera frugiperda |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.28 | D322A | at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis | Spodoptera frugiperda |
| 3.2.1.28 | E520A | at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis. In presence of azide, activity increases three fold | Spodoptera frugiperda |
| 3.2.1.28 | R169A | at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis | Spodoptera frugiperda |
| 3.2.1.28 | R222A | at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis | Spodoptera frugiperda |
| 3.2.1.28 | R222A/R287A | at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis | Spodoptera frugiperda |
| 3.2.1.28 | R287A | at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis | Spodoptera frugiperda |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.28 | 0.06 | - |
alpha,alpha-trehalose | mutant R222A/R287A, pH 7.0, 30°C | Spodoptera frugiperda |  |
| 3.2.1.28 | 0.22 | - |
alpha,alpha-trehalose | mutant E520A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.22 | - |
alpha,alpha-trehalose | mutant R287A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.3 | - |
alpha,alpha-trehalose | wild-type, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.45 | - |
alpha,alpha-trehalose | mutant R169A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 1 | - |
alpha,alpha-trehalose | mutant D322A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 3.33 | - |
alpha,alpha-trehalose | mutant R222A, pH 7.0, 30°C | Spodoptera frugiperda | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.28 | Spodoptera frugiperda | Q0ZIF5 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.28 | recombinant enzyme | Spodoptera frugiperda |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.28 | alpha,alpha-trehalose + H2O | - |
Spodoptera frugiperda | 2 D-glucose | - |
? | |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.28 | 0.00045 | - |
alpha,alpha-trehalose | mutant R222A/R287A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.0005 | - |
alpha,alpha-trehalose | mutant E520A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.0009 | - |
alpha,alpha-trehalose | mutant R287A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.12 | - |
alpha,alpha-trehalose | mutant R169A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.18 | - |
alpha,alpha-trehalose | mutant D322A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.3 | - |
alpha,alpha-trehalose | mutant R222A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 730 | - |
alpha,alpha-trehalose | wild-type, pH 7.0, 30°C | Spodoptera frugiperda | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.28 | 0.008 | - |
alpha,alpha-trehalose | mutant R222A/R287A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.009 | - |
alpha,alpha-trehalose | mutant R222A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.027 | - |
alpha,alpha-trehalose | mutant E520A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.045 | - |
alpha,alpha-trehalose | mutant R287A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.18 | - |
alpha,alpha-trehalose | mutant D322A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 0.27 | - |
alpha,alpha-trehalose | mutant R169A, pH 7.0, 30°C | Spodoptera frugiperda | |
| 3.2.1.28 | 2400 | - |
alpha,alpha-trehalose | wild-type, pH 7.0, 30°C | Spodoptera frugiperda | |
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