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Literature summary extracted from

  • Hadi, T.; Dahl, U.; Mayer, C.; Tanner, M.E.
    Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling (2008), Biochemistry, 47, 11547-11558.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.126 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.126 D115N the mutant exhibits a 7fold reduction in the value of kcat Escherichia coli
4.2.1.126 E114Q the mutant shows a dramatic reduction in the value of kcat (2000fold) and a modest decrease in the value of KM (4fold) Escherichia coli
4.2.1.126 E83A the mutant is essentially inactive, the mutant shows a very low, but measurable, level of activity with a kcat value that wis 10000fold lower than that of the wild type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.126 EDTA 5 mM EDTA results in only weak inhibition (25% reduction in rate) Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.126 0.32
-
 N-acetylmuramate 6-phosphate mutant enzyme E114Q, at 30°C in 60 mM Trien-HCl buffer (pH 8.0) Escherichia coli
4.2.1.126 0.83
-
 N-acetylmuramate 6-phosphate mutant enzyme D115N, at 30°C in 60 mM Trien-HCl buffer (pH 8.0) Escherichia coli
4.2.1.126 1.2
-
 N-acetylmuramate 6-phosphate wild type enzyme, at 30°C in 60 mM Trien-HCl buffer (pH 8.0) Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.126 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.126 Ni2+-chelating Sepharose column chromatography, gel filtration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.126 3-chloro-3-deoxy-N-acetylglucosamine 6-phosphate slow conversion, 2% activity compared to N-acetylmuramate 6-phosphate Escherichia coli (2E)-2-(acetylamino)-2,3-dideoxy-6-O-phosphono-D-erythro-hex-2-enose + HCl
-
 ?
4.2.1.126 N-acetylmuramate 6-phosphate + H2O
-
 Escherichia coli (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.126 MurNAc 6-phosphate etherase
-
 Escherichia coli
4.2.1.126 MurNAc 6-phosphate etherase lyase
-
 Escherichia coli
4.2.1.126 MurNAc 6-phosphate hydrolase
-
 Escherichia coli
4.2.1.126 MurQ
-
 Escherichia coli
4.2.1.126 N-acetylmuramic acid 6-phosphate hydrolase
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.126 0.0005
-
 N-acetylmuramate 6-phosphate mutant enzyme E83A, at 30°C in 60 mM Trien-HCl buffer (pH 8.0) Escherichia coli
4.2.1.126 0.0028
-
 N-acetylmuramate 6-phosphate mutant enzyme E114Q, at 30°C in 60 mM Trien-HCl buffer (pH 8.0) Escherichia coli
4.2.1.126 0.79
-
 N-acetylmuramate 6-phosphate mutant enzyme D115N, at 30°C in 60 mM Trien-HCl buffer (pH 8.0) Escherichia coli
4.2.1.126 5.7
-
 N-acetylmuramate 6-phosphate wild type enzyme, at 30°C in 60 mM Trien-HCl buffer (pH 8.0) Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.2.1.126 0.0088
-
 N-acetylmuramate 6-phosphate mutant enzyme E114Q, at 30°C in 60 mM Trien-HCl buffer (pH 8.0) Escherichia coli
4.2.1.126 0.95
-
 N-acetylmuramate 6-phosphate mutant enzyme D115N, at 30°C in 60 mM Trien-HCl buffer (pH 8.0) Escherichia coli
4.2.1.126 4.8
-
 N-acetylmuramate 6-phosphate wild type enzyme, at 30°C in 60 mM Trien-HCl buffer (pH 8.0) Escherichia coli