Application | Comment | Organism |
---|---|---|
synthesis | individual overexpression of ASPDH, aspartate-semialdehyde dehydrogenase from Tistrella mobilis, dihydrodipicolinate reductase from Escherichia coli, and diaminopimelate dehydrogenase from Pseudothermotoga thermarum in Corynebacterium glutamicum LC298, a basic lysine producer, increases the production of lysine by 30.7%, 32.4%, 17.4%, and 36.8%, respectively. The highest increase of lysine production (30.7%) is observed for a triple-mutant strain (27.7 g/L, 0.35 g/g glucose) expressing ASPDH, aspartate-semialdehyde dehydrogenase from Tistrella mobilis, dihydrodipicolinate reductase from Escherichia coli. A quadruple-mutant strain expressing all of the four NADH-utilizing enzymes allows high lysine production (24.1 g/l, 0.30 g/g glucose) almost independent of the oxidative pentose phosphate pathway | Pseudomonas aeruginosa |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.042 | - |
NADH | pH 8.2, 37°C | Pseudomonas aeruginosa | |
0.057 | - |
NADPH | pH 8.2, 37°C | Pseudomonas aeruginosa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
oxaloacetate + NH3 + NADH + H+ | - |
Pseudomonas aeruginosa | L-aspartate + H2O + NAD+ | - |
? | |
oxaloacetate + NH3 + NADPH + H+ | - |
Pseudomonas aeruginosa | L-aspartate + H2O + NADP+ | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
68.4 | - |
NADH | pH 8.2, 37°C | Pseudomonas aeruginosa | |
80.2 | - |
NADPH | pH 8.2, 37°C | Pseudomonas aeruginosa |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1407 | - |
NADPH | pH 8.2, 37°C | Pseudomonas aeruginosa | |
1629 | - |
NADH | pH 8.2, 37°C | Pseudomonas aeruginosa |