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Literature summary for 6.3.2.8 extracted from

  • Munshi, T.; Gupta, A.; Evangelopoulos, D.; Guzman, J.D.; Gibbons, S.; Keep, N.H.; Bhakta, S.
    Characterisation of ATP-dependent Mur ligases involved in the biogenesis of cell wall peptidoglycan in Mycobacterium tuberculosis (2013), PLoS ONE, 8, e60143.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.2.8

Cloned(Commentary)

Cloned (Comment) Organism
gene murC, located in the division/cell wall (dcw) cluster, identification of a promoter driving the co-transcription of mur synthetases along with key cell division genes such as ftsQ and ftsW, recombinant expression of His6-tagged enzyme in Escherichia coli BL21(DE3)/pLysS and Pseudomonas putida KT2442, subcloning in Escherichia coli strain DH5alpha. Coexpression of genes murC/D/E/F/nat and genes pknA, pknB, murI, dapF, ddlA, namH, Rv2160c, ftsW, ftsQ, ftsZ, sepF, wag31 in Mycobacterium smegmatis Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0235
-
 UDP-N-acetylmuramate pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
0.043
-
 L-alanine pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
0.0677
-
 ATP pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
0.0997
-
 L-serine pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
0.1465
-
 glycine pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall
-
 Mycobacterium tuberculosis 5618
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can partially substitute for Mg2+ Mycobacterium tuberculosis
Mg2+ required Mycobacterium tuberculosis
Mn2+ can substitute for Mg2+ Mycobacterium tuberculosis
Zn2+ can partially substitute for Mg2+ Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + UDP-N-acetylmuramate + L-alanine Mycobacterium tuberculosis
-
 ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
-
 ?
ATP + UDP-N-acetylmuramate + L-alanine Mycobacterium tuberculosis H37Rv
-
 ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
 gene murC
-
Mycobacterium tuberculosis H37Rv
-
 gene murC
-

Storage Stability

Storage Stability Organism
25°C, purified recombinant His-tagged enzyme, 50% loss of activity, 1 week Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramate + glycine
-
 Mycobacterium tuberculosis ADP + phosphate + UDP-N-acetylmuramoyl-glycine
-
 ?
ATP + UDP-N-acetylmuramate + glycine
-
 Mycobacterium tuberculosis H37Rv ADP + phosphate + UDP-N-acetylmuramoyl-glycine
-
 ?
ATP + UDP-N-acetylmuramate + L-alanine
-
 Mycobacterium tuberculosis ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
-
 ?
ATP + UDP-N-acetylmuramate + L-alanine
-
 Mycobacterium tuberculosis H37Rv ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
-
 ?
ATP + UDP-N-acetylmuramate + L-serine
-
 Mycobacterium tuberculosis ADP + phosphate + UDP-N-acetylmuramoyl-L-serine
-
 ?
ATP + UDP-N-acetylmuramate + L-serine
-
 Mycobacterium tuberculosis H37Rv ADP + phosphate + UDP-N-acetylmuramoyl-L-serine
-
 ?
additional information MurC is able to incorporate glycine and L-Ala to UDP-MurNAc in Mycobacterium tuberculosis, the enzyme is highly specific for ATP and UDP-N-acetylmuramate, poor activity with ADP, GTP, CTP, UTP, and dTTP Mycobacterium tuberculosis ?
-
 ?
additional information MurC is able to incorporate glycine and L-Ala to UDP-MurNAc in Mycobacterium tuberculosis, the enzyme is highly specific for ATP and UDP-N-acetylmuramate, poor activity with ADP, GTP, CTP, UTP, and dTTP Mycobacterium tuberculosis H37Rv ?
-
 ?

Synonyms

Synonyms Comment Organism
Mur ligase
-
 Mycobacterium tuberculosis
MurC
-
 Mycobacterium tuberculosis
MurC synthetase
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35 40
-
 Mycobacterium tuberculosis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
10 70 purified recombinant His-tagged enzyme, stable up to 40°C, MurC activity diminishes at 45-70°C Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1
-
 L-alanine pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
1.2
-
 L-serine pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
1.53
-
 glycine pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
additional information protein-protein interaction network of MurC, D, E, and F synthetases, overview Mycobacterium tuberculosis
physiological function ATP-dependent Mur ligases play essential roles in the biosynthesis of cell wall peptidoglycan as they catalyze the ligation of key amino acid residues to the stem peptide at the expense of ATP hydrolysis Mycobacterium tuberculosis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
10.47
-
 glycine pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
12.5
-
 L-serine pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
15.1
-
 ATP pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
23.9
-
 L-alanine pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
44.8
-
 UDP-N-acetylmuramate pH 8.5, 37°C, recombinant enzyme Mycobacterium tuberculosis