Literature summary extracted from
Choi, P.H.; Vu, T.M.N.; Pham, H.T.; Woodward, J.J.; Turner, M.S.; Tong, L.
Structural and functional studies of pyruvate carboxylase regulation by cyclic di-AMP in lactic acid bacteria (2017), Proc. Natl. Acad. Sci. USA, 114, E7226-E7235 .
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
6.4.1.1 |
in complex with cyclic di-3',5'-adenosine monophosphate |
Lactococcus lactis |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
6.4.1.1 |
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 |
6.4.1.1 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
6.4.1.1 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
6.4.1.1 |
Lactococcus lactis |
- |
- |
- |