EC Number | Application | Comment | Organism |
---|---|---|---|
1.5.1.24 | synthesis | enzymatic biosyntheses of amino acids instead of chemical syntheses provide an attractive alternative to the former procedures since they are efficient and simple to perform. N,N-dialkylation does not occur and the enzyme-catalyzed reactions are both regio-and stereochemically specific | Lactococcus lactis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.1.24 | gene ceo, encoding the tetrameric enzyme, cloned and sequenced, plasmid p493 containing ceo transformed into Escherichia coli TG1 | Lactococcus lactis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.24 | gamma-glutamyl peptide | - |
Lactococcus lactis | |
1.5.1.24 | additional information | anti-NADP+ oxidoreductase IgG | Lactococcus lactis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.1.24 | 0.15 | - |
pyruvate | - |
Lactococcus lactis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.5.1.24 | cytoplasm | - |
Lactococcus lactis | 5737 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.5.1.24 | 35323 | - |
4 * 35323, deduced from amino acid sequence | Lactococcus lactis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.24 | Lactococcus lactis | - |
subsp. lactis | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.5.1.24 | - |
Lactococcus lactis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.24 | lysine + pyruvate + NADPH | - |
Lactococcus lactis | N7-(1-carboxyethyl)lysine + NADP+ + H2O | - |
ir |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.5.1.24 | tetramer | 4 * 35323, deduced from amino acid sequence | Lactococcus lactis |