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Literature summary for 6.3.2.8 extracted from

  • Nosal, F.; Masson, A.; Legrand, R.; Blanot, D.; Schoot, B.; van Heijenoort, J.; Parquet, C.
    Site-directed mutagenesis and chemical modification of the two cysteine residues of the UDP-N-acetylmuramoyl:L-alanine ligase of Escherichia coli (1998), FEBS Lett., 426, 309-313.
    View publication on PubMed
Search for more literature for 6.3.2.8

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM83 and PC2453 Escherichia coli

Protein Variants

Protein Variants Comment Organism
C230A activity completely lost at 42°C Escherichia coli
C426A Km increased 3fold for ATP and 10fold for UDP-MurNAc and L-alanine, with respect to the wild-type Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 UDP-N-acetylmuramate wild-type enzyme Escherichia coli
0.04
-
 L-alanine wild-type enzyme Escherichia coli
0.3
-
 L-alanine C230A mutant Escherichia coli
0.45
-
 ATP wild-type enzyme Escherichia coli
1.1
-
 UDP-N-acetylmuramate C230A mutant Escherichia coli
1.4
-
 ATP C230A mutant Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53640
-
 mass spectrometry Escherichia coli
53750
-
 trifluoroacetic adduct by mass spectrometry Escherichia coli
53880
-
 trifluoroacetic adduct by mass spectrometry Escherichia coli
53990
-
 trifluoroacetic adduct by mass spectrometry Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
 28% loss of activity with previous remove of dithiothreitol Escherichia coli