Application | Comment | Organism |
---|---|---|
analysis | development of a coupled assay, employing (R)-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans as an auxiliary enzyme, to provide accurate and reliable kinetic constants | Escherichia coli |
synthesis | enzyme can be used for asymmetric synthesis of a range of non-natural amino acids such as L-norleucine, L-norvaline and L-neopentylglycine | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
molecular modelling of substrate binding. The inner side of the active site pocket binds the hydrophobic side chain and the alpha-carboxylate group of the substrates | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.07 | - |
3-methyl-2-oxopentanoate | pH 8.0, 37°C | Escherichia coli | |
0.08 | - |
2-oxoisocaproate | pH 8.0, 37°C | Escherichia coli | |
0.08 | - |
4,4-dimethyl-2-oxopentanoate | pH 8.0, 37°C | Escherichia coli | |
0.2 | - |
2-oxoisovalerate | pH 8.0, 37°C | Escherichia coli | |
0.22 | - |
2-Oxohexanoate | pH 8.0, 37°C | Escherichia coli | |
0.6 | - |
2-oxovalerate | pH 8.0, 37°C | Escherichia coli | |
20.9 | - |
L-glutamate | cosubstrate 4,4-dimethyl-2-oxopentanoate, pH 8.0, 37°C | Escherichia coli | |
21.8 | - |
L-glutamate | cosubstrate 2-oxoisocaproate, pH 8.0, 37°C | Escherichia coli | |
26.5 | - |
L-glutamate | cosubstrate 2-oxohexanoate, pH 8.0, 37°C | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
35000 | - |
x * 35000, SDS-PAGE | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AB80 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | bibi ping-pong mechanism. For good 2-oxoacid substrates, release of 2-oxoglutarate is much slower than release of the product amino acid during the transamination reaction | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxohexanoate + L-glutamate | - |
Escherichia coli | L-norleucine + 2-oxoglutarate | - |
? | |
2-oxoisocaproate + L-glutamate | - |
Escherichia coli | L-leucine + 2-oxoglutarate | - |
? | |
2-oxoisovalerate + L-glutamate | - |
Escherichia coli | L-valine + 2-oxoglutarate | - |
? | |
2-oxovalerate + L-glutamate | - |
Escherichia coli | L-norvaline + 2-oxoglutarate | - |
? | |
3-methyl-2-oxopentanoate + L-glutamate | - |
Escherichia coli | L-isoleucine + 2-oxoglutarate | - |
? | |
4,4-dimethyl-2-oxopentanoate + L-glutamate | - |
Escherichia coli | L-neopentylglycine + 2-oxoglutarate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 35000, SDS-PAGE | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
IlvE | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
10.5 | - |
2-oxoisovalerate | pH 8.0, 37°C | Escherichia coli | |
12.4 | - |
4,4-dimethyl-2-oxopentanoate | pH 8.0, 37°C | Escherichia coli | |
23 | - |
3-methyl-2-oxopentanoate | pH 8.0, 37°C | Escherichia coli | |
23.1 | - |
2-Oxohexanoate | pH 8.0, 37°C | Escherichia coli | |
24.7 | - |
2-oxoisocaproate | pH 8.0, 37°C | Escherichia coli | |
25.9 | - |
2-oxovalerate | pH 8.0, 37°C | Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
43.2 | - |
2-oxovalerate | pH 8.0, 37°C | Escherichia coli | |
52.5 | - |
2-oxoisovalerate | pH 8.0, 37°C | Escherichia coli | |
105 | - |
2-Oxohexanoate | pH 8.0, 37°C | Escherichia coli | |
155 | - |
4,4-dimethyl-2-oxopentanoate | pH 8.0, 37°C | Escherichia coli | |
309 | - |
2-oxoisocaproate | pH 8.0, 37°C | Escherichia coli | |
329 | - |
3-methyl-2-oxopentanoate | pH 8.0, 37°C | Escherichia coli |