Application | Comment | Organism |
---|---|---|
biotechnology | the reaction specificity of acetolactate synthase from Thermus thermophilus can be redirected to catalyze acetaldehyde formation to develop a thermophilic pyruvate decarboxylase. Quadruple mutant Y35N/K139R/V172A/H474R shows 3.1fold higher acetaldehyde-forming activity than the wild-type mainly because of H474R amino acid substitution, which likely generates two new hydrogen bonds near the thiamine diphosphate-binding site | Thermus thermophilus |
Protein Variants | Comment | Organism |
---|---|---|
H747R | mutation leads to 3fold increased acetaldehyde formation, with 30% decrease in acetolactate formation | Thermus thermophilus |
Y35N/K139R/V172A/H474R | shows 3.1fold higher acetaldehyde-forming activity than the wild-type | Thermus thermophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | Q5SJ01 | acetolactate synthase, EC 2.2.1.6 | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | Q5SJ01 | acetolactate synthase, EC 2.2.1.6 | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.45 | - |
wild-type, pH 7.0, 60°C | Thermus thermophilus |
4.51 | - |
mutant Y35N/K139R/V172A/H474R, pH 7.0, 60°C | Thermus thermophilus |
5.52 | - |
mutant H747R, pH 7.0, 60°C | Thermus thermophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | - |
Thermus thermophilus | acetaldehyde + CO2 | in wild-type, about 10% of the acetolactate forming activity | ? | |
pyruvate | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | acetaldehyde + CO2 | in wild-type, about 10% of the acetolactate forming activity | ? |
Synonyms | Comment | Organism |
---|---|---|
TTHA1213 | - |
Thermus thermophilus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
thiamine diphosphate | - |
Thermus thermophilus |