Crystallization (Comment) | Organism |
---|---|
in complex with cyclic di-3',5'-adenosine monophosphate | Lactococcus lactis |
Protein Variants | Comment | Organism |
---|---|---|
G746A | mutation to corresponding Entercoccus faecalis residue. Mutant shows similar activity as wild-type, mutation reduces inhibition by cyclic di-3',5'-adenosine monophosphate to 40%, compared to 60% for wild-type | Lactococcus lactis |
Y715T | mutation to correspoinding human residue. Mutant shows similar activity as wild-type, mutation abolishes inhibition by cyclic di-3',5'-adenosine monophosphate | Lactococcus lactis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
cyclic di-3',5'-adenosine monophosphate | compound is bound at the dimer interface of the carboxyltransferase. domain. The aspartate pool in Lactococcus lactis is negatively regulated by cyclic di-3',5'-adenosine monophosphate, and high aspartate levels can be restored by expression of a cyclic di-3',5'-adenosine monophosphate enzyme. Mutations of residues in the binding site can abolish cyclic di-3',5'-adenosine monophosphate inhibition | Lactococcus lactis |
Organism | UniProt | Comment | Textmining |
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Lactococcus lactis | - |
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