Application | Comment | Organism |
---|---|---|
synthesis | threonine aldolase is a very promising enzyme that can be used to prepare biologically active compounds or building blocks for pharmaceutical industry. Rational design is applied to thermophilic threonine aldolase from Thermotoga maritima to improve thermal stability by the incorporation of salt and disulfide bridges between subunits in the functional tetramer | Thermotoga maritima |
Cloned (Comment) | Organism |
---|---|
the gene of L-threonine aldolase from Thermotoga maritima is cloned into c-LEctas expression vector pLE1A17 under control of the T7 promoter. Expression in Escherichia coli BL21(DE3) | Thermotoga maritima |
Protein Variants | Comment | Organism |
---|---|---|
A21C | L-threonine cleavage activity is similar to the activity of the wild-type enzyme | Thermotoga maritima |
F85Y | L-threonine cleavage activity is about 65% of the activity of the wild-type enzyme | Thermotoga maritima |
I124D | L-threonine cleavage activity is about 65% of the activity of the wild-type enzyme | Thermotoga maritima |
additional information | rational design is applied to the enzyme to improve thermal stability by the incorporation of salt and disulfide bridges between subunits in the functional tetramer | Thermotoga maritima |
P56C | L-threonine cleavage activity is about 95% of the activity of the wild-type enzyme, the mutant enzyme displays significantly enhanced stability compared to the wild type enzyme | Thermotoga maritima |
Q22K | L-threonine cleavage activity is about 75% of the activity of the wild-type enzyme | Thermotoga maritima |
S198D | L-threonine cleavage activity is about 110% of the activity of the wild-type enzyme | Thermotoga maritima |
T59D | L-threonine cleavage activity is about 10% of the activity of the wild-type enzyme | Thermotoga maritima |
V235C | L-threonine cleavage activity is about 110% of the activity of the wild-type enzyme | Thermotoga maritima |
V29D | L-threonine cleavage activity is about 90% of the activity of the wild-type enzyme | Thermotoga maritima |
W86E | the mutant enzyme displays enhanced activity, with stability similar to the wild type enzyme | Thermotoga maritima |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
37000 | - |
SDS-PAGE | Thermotoga maritima |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | Q9X266 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycine + acetaldehyde | - |
Thermotoga maritima | L-threonine | - |
r | |
L-threonine | - |
Thermotoga maritima | glycine + acetaldehyde | - |
r |
Subunits | Comment | Organism |
---|---|---|
tetramer | 4 * 37000, SDS-PAGE | Thermotoga maritima |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
75 | - |
- |
Thermotoga maritima |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
75 | - |
15 h, 50% loss of activity | Thermotoga maritima |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | dependent on | Thermotoga maritima |