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Literature summary for 6.3.2.8 extracted from

  • Bouhss, A.; Mengin-Lecreulx, D.; Blanot, D.; van Heijenoort, J.; Parquet, C.
    Invariant amino acids in the Mur peptide synthetases of bacterial peptidoglycan synthesis and their modification by site-directed mutagenesis in the UDP-MurNAc;L-alanine ligase from Escherichia coli (1997), Biochemistry, 36, 11556-11563.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
H199A mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates Escherichia coli
K130A mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates Escherichia coli
N293A mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates Escherichia coli
N296A mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates Escherichia coli
R327A mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km-value of wild-type and mutant enzymes Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
wild-type and mutant enzymes
-

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 the binding order of the substrates can be ATP, UDP-N-acetylmuramate, and Ala 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
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