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Literature summary for 2.7.1.59 extracted from

  • Reith, J.; Berking, A.; Mayer, C.
    Characterization of an N-acetylmuramic acid/N-acetylglucosamine kinase of Clostridium acetobutylicum (2011), J. Bacteriol., 193, 5386-5392.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis the kinase is applied for high-sensitive detection of the amino sugars in cell wall preparations by radioactive phosphorylation Clostridium acetobutylicum

Cloned(Commentary)

Cloned (Comment) Organism
expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Clostridium acetobutylicum

Inhibitors

Inhibitors Comment Organism Structure
EDTA a 3fold excess of EDTA compared to the Mg2+ concentration strongly represses the MurK activity. Addition of 2 mM MgCl2 to the reaction mixture partially restores MurK activity Clostridium acetobutylicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.127
-
N-acetyl-D-glucosamine pH 7.5, 37°C Clostridium acetobutylicum

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall
-
Clostridium acetobutylicum 5618
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Clostridium acetobutylicum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34329
-
x * 34329, sequence calculation Clostridium acetobutylicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + N-acetyl-D-glucosamine Clostridium acetobutylicum
-
ADP + N-acetyl-D-glucosamine 6-phosphate
-
?
additional information Clostridium acetobutylicum the enzyme has a unique specificity for both amino sugars of the bacterial cell wall, N-acetylmuramic acid and N-acetylglucosamine, which are phosphorylated at the 6-hydroxyl group, see also EC 2.7.1.170, the kcat value is 1.5fold higher for the latter substrate. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. Product identificsation by nonradioactive and radioactive TLC ?
-
?

Organism

Organism UniProt Comment Textmining
Clostridium acetobutylicum
-
gene murK
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Clostridium acetobutylicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + N-acetyl-D-glucosamine
-
Clostridium acetobutylicum ADP + N-acetyl-D-glucosamine 6-phosphate
-
?
additional information the enzyme has a unique specificity for both amino sugars of the bacterial cell wall, N-acetylmuramic acid and N-acetylglucosamine, which are phosphorylated at the 6-hydroxyl group, see also EC 2.7.1.170, the kcat value is 1.5fold higher for the latter substrate. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. Product identificsation by nonradioactive and radioactive TLC Clostridium acetobutylicum ?
-
?

Subunits

Subunits Comment Organism
? x * 34329, sequence calculation Clostridium acetobutylicum

Synonyms

Synonyms Comment Organism
GlcNAc kinase
-
Clostridium acetobutylicum
MurK
-
Clostridium acetobutylicum
N-acetylmuramic acid/N-acetylglucosamine kinase
-
Clostridium acetobutylicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Clostridium acetobutylicum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
at 30°C, the purified protein loses activity within hours of incubation, regardless of the addition of protease inhibitors Clostridium acetobutylicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
65
-
N-acetyl-D-glucosamine pH 7.5, 37°C Clostridium acetobutylicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 9
-
Clostridium acetobutylicum

pH Range

pH Minimum pH Maximum Comment Organism
6.5 10.5 half maximal activity at about pH 6.5 and pH 10.5, inactive at pH 5.0 and below Clostridium acetobutylicum

Cofactor

Cofactor Comment Organism Structure
ATP
-
Clostridium acetobutylicum

General Information

General Information Comment Organism
evolution the enzyme is a member of the BcrAD/BadFGlike ATPase family Clostridium acetobutylicum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
510.2
-
N-acetyl-D-glucosamine pH 7.5, 37°C Clostridium acetobutylicum