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Literature summary for 6.3.2.8 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
Search for more literature for 6.3.2.8

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
0.28
-
 UDP-N-acetylmuramate pH 8.6, 37°C Staphylococcus aureus
0.44
-
 L-Ala pH 8.6, 37°C Staphylococcus aureus
2
-
 ATP pH 8.6, 37°C Staphylococcus aureus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, optimal concentration 5 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-acetylmuramate + 2-amino-N-butyric acid
-
 Staphylococcus aureus ADP + phosphate + UDP-N-acetylmuramoyl-2-amino-N-butyric acid
-
 ?
ATP + UDP-N-acetylmuramate + L-Ala accepts L-Ala, L-Ser and Gly as substrates, with a strong preference for L-Ala Staphylococcus aureus ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2 8.8
-
 Staphylococcus aureus