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Literature summary extracted from
- Bacillus licheniformis trehalose-6-phosphate hydrolase structures suggest keys to substrate specificity (2016), Acta Crystallogr. Sect. D, 72, 59-70 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.93 | expression in Escherichia coli M15 cells | Bacillus licheniformis |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.2.1.93 | crystal structures of Bacillus licheniformis TreA and its R201Q mutant complexed with 4-nitrophenyl-alpha-D-glucopyranoside are presented at 2.0 and 2.05 A resolution, respectively | Bacillus licheniformis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.93 | D203E | no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside | Bacillus licheniformis |
| 3.2.1.93 | D329E | no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside | Bacillus licheniformis |
| 3.2.1.93 | E254D | no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside | Bacillus licheniformis |
| 3.2.1.93 | H281A | kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 5.3fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 5.25fold as compared to wild-type value | Bacillus licheniformis |
| 3.2.1.93 | H282A | kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 2.65fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 2.6fold as compared to wild-type value | Bacillus licheniformis |
| 3.2.1.93 | K284A | kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 1.5fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 1.5fold as compared to wild-type value | Bacillus licheniformis |
| 3.2.1.93 | K292A | kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 265fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 189fold as compared to wild-type value | Bacillus licheniformis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.93 | 2.5 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, wild-type enzyme | Bacillus licheniformis |  |
| 3.2.1.93 | 3.2 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme K284A | Bacillus licheniformis | |
| 3.2.1.93 | 4.9 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme H282A | Bacillus licheniformis | |
| 3.2.1.93 | 5.3 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme H281A | Bacillus licheniformis | |
| 3.2.1.93 | 5.8 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, wild-type enzyme | Bacillus licheniformis | |
| 3.2.1.93 | 5.9 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme K292A | Bacillus licheniformis | |
| 3.2.1.93 | 7.4 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme K284A | Bacillus licheniformis | |
| 3.2.1.93 | 11.4 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme H282A | Bacillus licheniformis | |
| 3.2.1.93 | 12.2 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme H281A | Bacillus licheniformis | |
| 3.2.1.93 | 13.6 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme K292A | Bacillus licheniformis | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.93 | Bacillus licheniformis | Q65MI2 | - |
- |
| 3.2.1.93 | Bacillus licheniformis DSM13 | Q65MI2 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.93 | - |
Bacillus licheniformis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.93 | 4-nitrophenyl alpha-D-glucopyranoside + H2O | - |
Bacillus licheniformis | 4-nitrophenol + alpha-D-glucose | - |
? | |
| 3.2.1.93 | 4-nitrophenyl alpha-D-glucopyranoside + H2O | - |
Bacillus licheniformis DSM13 | 4-nitrophenol + alpha-D-glucose | - |
? | |
| 3.2.1.93 | alpha,alpha-trehalose 6-phosphate + H2O | - |
Bacillus licheniformis | D-glucose + D-glucose 6-phosphate | - |
? | |
| 3.2.1.93 | alpha,alpha-trehalose 6-phosphate + H2O | - |
Bacillus licheniformis DSM13 | D-glucose + D-glucose 6-phosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.93 | TreA | - |
Bacillus licheniformis |
| 3.2.1.93 | trehalose-6-phosphate hydrolase | - |
Bacillus licheniformis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.93 | 30 | - |
assay at | Bacillus licheniformis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.93 | 0.3 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme K292A | Bacillus licheniformis | |
| 3.2.1.93 | 0.4 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme K292A | Bacillus licheniformis | |
| 3.2.1.93 | 12.4 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme H281A | Bacillus licheniformis | |
| 3.2.1.93 | 19.1 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme H281A | Bacillus licheniformis | |
| 3.2.1.93 | 22.6 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme H282A | Bacillus licheniformis | |
| 3.2.1.93 | 25.6 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme K284A | Bacillus licheniformis | |
| 3.2.1.93 | 30.3 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, wild-type enzyme | Bacillus licheniformis | |
| 3.2.1.93 | 34.8 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme H282A | Bacillus licheniformis | |
| 3.2.1.93 | 39.5 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme K284A | Bacillus licheniformis | |
| 3.2.1.93 | 46.7 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, wild-type enzyme | Bacillus licheniformis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.93 | 8 | - |
assay at | Bacillus licheniformis |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.93 | 0.02 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme K292A | Bacillus licheniformis | |
| 3.2.1.93 | 0.1 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme K292A | Bacillus licheniformis | |
| 3.2.1.93 | 1 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme H281A | Bacillus licheniformis | |
| 3.2.1.93 | 2 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme H282A | Bacillus licheniformis | |
| 3.2.1.93 | 3.5 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, mutant enzyme K284A | Bacillus licheniformis | |
| 3.2.1.93 | 3.6 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme H281A | Bacillus licheniformis | |
| 3.2.1.93 | 5.3 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 8.0, 30°C, wild-type enzyme | Bacillus licheniformis | |
| 3.2.1.93 | 7.2 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme H282A | Bacillus licheniformis | |
| 3.2.1.93 | 12.2 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, mutant enzyme K284A | Bacillus licheniformis | |
| 3.2.1.93 | 18.9 | - |
alpha,alpha-trehalose 6-phosphate | pH 8.0, 30°C, wild-type enzyme | Bacillus licheniformis | |
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