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Literature summary for 6.3.2.7 extracted from

  • Patin, D.; Boniface, A.; Kovac, A.; Hervé, M.; Dementin, S.; Barreteau, H.; Mengin-Lecreulx, D.; Blanot, D.
    Purification and biochemical characterization of Mur ligases from Staphylococcus aureus (2010), Biochimie, 92, 1793-1800.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Staphylococcus aureus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.087
-
UDP-N-acetylmuramoyl-L-Ala-D-Glu pH 8.6, 37°C Staphylococcus aureus
0.53
-
ATP pH 8.6, 37°C Staphylococcus aureus
0.55
-
L-Lys pH 8.6, 37°C Staphylococcus aureus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, optimal concentration 15 mM Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Staphylococcus aureus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu + L-Lys
-
Staphylococcus aureus ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys
-
?
additional information enzyme is specific for L-lysine and does not accept meso-diaminopimelic acid as substrate. The inverse and strict substrate specificities of the two MurE orthologues are responsible for the presence of exclusively mesodiaminopimelic acid and L-lysine at the third position of the peptide in the peptidoglycans of Escherichia coli and Staphylococcus aureus, respectively Staphylococcus aureus ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4 9.2
-
Staphylococcus aureus