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Literature summary for 6.4.1.1 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 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.4.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with cyclic di-3',5'-adenosine monophosphate Lactococcus lactis

Protein Variants

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

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

Organism UniProt Comment Textmining
Lactococcus lactis
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