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Literature summary for 6.3.2.8 extracted from

  • Falk, P.J.; Ervin, K.M.; Volk, K.S.; Ho, H.T.
    Biochemical evidence of the formation of a covalent acyl-phosphate linkage between UDP-N-acetylmuramate and ATP in the Escherichia coli UDP-N-acetylmuramate:L-alanine ligase-catalyzed reaction (1996), Biochemistry, 35, 1417-1422.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.024
-
 L-Ala
-
 Escherichia coli
0.039
-
 UDP-N-acetylmuramate
-
 Escherichia coli
0.14
-
 ATP
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 maltose binding-protein-UDP-N-acetylmuramyl:L-alanine ligase fusion protein is overproduced in Escherichia coli/pMal::murC
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine ligase-catalyzed peptide formation proceeds through an activated acyl-phosphate linkage during the reaction process. ATP assists in this process of the peptide bond formation by donating its gamma-phosphoryl group to activate the carboxyl group of UDP-N-acetylmuramate Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramate + L-Ala
-
 Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala
-
 ?