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Literature summary for 4.2.1.126 extracted from

  • Jaeger, T.; Arsic, M.; Mayer, C.
    Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli etherase (2005), J. Biol. Chem., 280, 30100-30106.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
MurQ-His fusion protein is expressed in Escherichia coli BL21 cells Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap chelating HP column chromatography, gel filtration Escherichia coli

Storage Stability

Storage Stability Organism
-20°C, imidazole buffer (pH 8.0) by adding 20% glycerol and 1 mM dithiothreitol, at least several weeks, activity is retained Escherichia coli
4°C, purified etherase is only active for a few days Escherichia coli
temperature, storage medium, duration, loss of activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information N-acetylmuramate is not a substrate nor are anhydro-N-acetylmuramate or muramic acid Escherichia coli ?
-
?
N-acetylmuramate 6-phosphate + H2O
-
Escherichia coli D-lactate + N-acetyl-D-glucosamine 6-phosphate
-
?

Synonyms

Synonyms Comment Organism
MurNAc etherase
-
Escherichia coli
MurQ
-
Escherichia coli

General Information

General Information Comment Organism
malfunction a murQ deletion mutant cannot grow on N-acetylmuramic acid as the sole source of carbon Escherichia coli
physiological function MurQ is required for growth on N-acetylmuramic acid Escherichia coli