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Literature summary for 6.3.2.45 extracted from

  • Herve, M.; Boniface, A.; Gobec, S.; Bianot, D.; Mengin-Lecreulx, D.
    Biochemical characterization and physiological properties of Escherichia coli UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (2007), J. Bacteriol., 189, 3987-3995.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overproduction as a His6-tagged protein Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.051
-
L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanyl-D-alanine pH 8.4, 37°C Escherichia coli
0.1
-
L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate pH 8.4, 37°C Escherichia coli
0.1
-
L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine pH 8.4, 37°C Escherichia coli
0.19
-
ATP pH 8.4, 37°C Escherichia coli
0.25
-
UDP-N-alpha-D-acetylmuramate pH 8.4, 37°C Escherichia coli
3.9
-
L-Ala-gamma-D-Glu-L-Lys-D-Ala pH 8.4, 37°C Escherichia coli
4.1
-
L-Ala-gamma-D-Glu-L-Lys pH 8.4, 37°C Escherichia coli
19
-
L-Ala-D-Glu pH 8.4, 37°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ absolute requirement for a divalent cation. The optimal concentration for Mg2+ is 15 mM Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
x * 50000, SDS-PAGE Escherichia coli
50940
-
x * 50940, calculated from sequence Escherichia coli
50961
-
x * 50961, MALDI-TOF mass spectrometry Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + UDP-N-alpha-D-acetylmuramate + L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate Escherichia coli the recycling enzyme allows reincorporation into peptidoglycan (murein) of the tripeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate released during the maturation and constant remodeling of this bacterial cell wall polymer that occur during cell growth and division. The enzyme adds this peptide to UDP-N-acetylmuramate, thereby providing an economical additional source of UDP-MurNAc-tripeptide available for de novo peptidoglycan biosynthesis ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.6
-
pH 8.4, 37°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-alpha-D-acetylmuramate + L-Ala-D-Glu
-
Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu
-
?
ATP + UDP-N-alpha-D-acetylmuramate + L-Ala-gamma-D-Glu-L-Lys
-
Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-gamma-D-Glu-L-Lys
-
?
ATP + UDP-N-alpha-D-acetylmuramate + L-Ala-gamma-D-Glu-L-Lys-D-Ala
-
Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala
-
?
ATP + UDP-N-alpha-D-acetylmuramate + L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
-
Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate
-
?
ATP + UDP-N-alpha-D-acetylmuramate + L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate the recycling enzyme allows reincorporation into peptidoglycan (murein) of the tripeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate released during the maturation and constant remodeling of this bacterial cell wall polymer that occur during cell growth and division. The enzyme adds this peptide to UDP-N-acetylmuramate, thereby providing an economical additional source of UDP-MurNAc-tripeptide available for de novo peptidoglycan biosynthesis Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate
-
?
ATP + UDP-N-alpha-D-acetylmuramate + L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine
-
Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine
-
?
ATP + UDP-N-alpha-D-acetylmuramate + L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanyl-D-alanine
-
Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanyl-D-alanine
-
?

Subunits

Subunits Comment Organism
? x * 50000, SDS-PAGE Escherichia coli
? x * 50940, calculated from sequence Escherichia coli
? x * 50961, MALDI-TOF mass spectrometry Escherichia coli

Synonyms

Synonyms Comment Organism
Mpl
-
Escherichia coli
murein peptide ligase
-
Escherichia coli
UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase
-
Escherichia coli
UDP-N-alpha-D-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate (ADP-forming)
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.01 1 L-Ala-D-Glu pH 8.4, 37°C Escherichia coli
0.27
-
L-Ala-gamma-D-Glu-L-Lys pH 8.4, 37°C Escherichia coli
0.32
-
L-Ala-gamma-D-Glu-L-Lys-D-Ala pH 8.4, 37°C Escherichia coli
2.83
-
L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanyl-D-alanine pH 8.4, 37°C Escherichia coli
3.17
-
L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine pH 8.4, 37°C Escherichia coli
4.83
-
ATP pH 8.4, 37°C Escherichia coli
4.83
-
UDP-N-alpha-D-acetylmuramate pH 8.4, 37°C Escherichia coli
4.83
-
L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate pH 8.4, 37°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7.6 9.2 pH 7.6: about 75% of maximal activity, pH 9.2: about 75% of maximal activity Escherichia coli

General Information

General Information Comment Organism
physiological function the recycling enzyme allows reincorporation into peptidoglycan (murein) of the tripeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate released during the maturation and constant remodeling of this bacterial cell wall polymer that occur during cell growth and division. The enzyme adds this peptide to UDP-N-acetylmuramic acid, thereby providing an economical additional source of UDP-MurNAc-tripeptide available for de novo peptidoglycan biosynthesis Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00058
-
L-Ala-D-Glu pH 8.4, 37°C Escherichia coli
0.065
-
L-Ala-gamma-D-Glu-L-Lys pH 8.4, 37°C Escherichia coli
0.082
-
L-Ala-gamma-D-Glu-L-Lys-D-Ala pH 8.4, 37°C Escherichia coli
20
-
UDP-N-alpha-D-acetylmuramate pH 8.4, 37°C Escherichia coli
25
-
ATP pH 8.4, 37°C Escherichia coli
32
-
L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine pH 8.4, 37°C Escherichia coli
48
-
L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate pH 8.4, 37°C Escherichia coli
55
-
L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanyl-D-alanine pH 8.4, 37°C Escherichia coli