Crystallization (Comment) | Organism |
---|---|
- |
Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NaCl | 1 M, 45% inhibition | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
80000 | - |
x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Lys | Escherichia coli | inducible enzyme | ? | - |
? | |
L-Lys | Escherichia coli B / ATCC 11303 | inducible enzyme | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli B / ATCC 11303 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1018 | - |
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
delta-Hydroxylysine | 25% of the activity with L-Lys | Escherichia coli | 1,5-Diamino-2-hydroxypentane + CO2 | - |
? | |
delta-Hydroxylysine | 25% of the activity with L-Lys | Escherichia coli B / ATCC 11303 | 1,5-Diamino-2-hydroxypentane + CO2 | - |
? | |
L-Lys | - |
Escherichia coli | Cadaverine + CO2 | - |
? | |
L-Lys | - |
Escherichia coli B / ATCC 11303 | Cadaverine + CO2 | - |
? | |
L-Lys | inducible enzyme | Escherichia coli | ? | - |
? | |
L-Lys | inducible enzyme | Escherichia coli B / ATCC 11303 | ? | - |
? | |
S-Aminoethyl-L-Cys | 15% of the activity with L-Lys | Escherichia coli | 1-Amino-2-(S-aminoethyl)mercaptoethane + CO2 | - |
? | |
S-Aminoethyl-L-Cys | 15% of the activity with L-Lys | Escherichia coli B / ATCC 11303 | 1-Amino-2-(S-aminoethyl)mercaptoethane + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.7 | - |
- |
Escherichia coli |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4.7 | 6.6 | 50% of maximal activity at pH 4.7 and 6.6 | Escherichia coli |