Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Burkholderia cepacia |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1-aminocyclopropane 1-carboxylate | - |
Burkholderia cepacia | |
Li+ | - |
Burkholderia cepacia | |
Na+ | - |
Burkholderia cepacia |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.12 | - |
2-aminoisobutanoate | enzyme with Na+ in the metal binding site | Burkholderia cepacia | |
2 | - |
2-aminoisobutanoate | enzyme with K+ in the metal binding site | Burkholderia cepacia | |
8.7 | - |
2-aminoisobutanoate | enzyme with Na+ in the metal binding site | Burkholderia cepacia |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | activates | Burkholderia cepacia | |
K+ | the K+-activated enzyme in solution exists in two conformations differing in catalytic competence | Burkholderia cepacia | |
additional information | hysteretic enzyme whose conformational distribution is controlled by the identity of the alkali metal ion bound near the active site | Burkholderia cepacia | |
Rb+ | activates | Burkholderia cepacia |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Burkholderia cepacia | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine | cooperativity does not play a role in catalysis or regulation | Burkholderia cepacia |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.29 | - |
2-aminoisobutanoate | enzyme with Na+ in the metal binding site | Burkholderia cepacia | |
4.47 | - |
2-aminoisobutanoate | enzyme with Rb+ in the metal binding site | Burkholderia cepacia | |
13.1 | - |
2-aminoisobutanoate | enzyme with K+ in the metal binding site | Burkholderia cepacia |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | dependent on | Burkholderia cepacia |