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Information on EC 6.3.2.B2 - murein peptide ligase
for references in articles please use BRENDA:EC6.3.2.B2
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preliminary BRENDA-supplied EC number
EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.2 Acid—amino-acid ligases (peptide synthases)
6.3.2.B2 murein peptide ligase
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
showSynonyms
murein peptide ligase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Mpl
pMurE
pseudomurein peptide ligase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + UDP-N-acetylmuramate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
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-
-
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SYSTEMATIC NAME
IUBMB Comments
L-alanyl-gamma-D-glutamyl-meso-diaminopimelate:UDP-N-acetylmuramate ligase (ADP-forming)
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-alanyl-gamma-D-glutamate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-alanyl-gamma-D-glutamyl-L-lysine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
Substrates: -
Products: -
Products: -
?
ATP + L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-L-lysyl-D-alanine
Substrates: -
Products: -
Products: -
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine
ATP + L-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
Substrates: -
Products: -
Products: -
?
ATP + L-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
Substrates: -
Products: -
Products: -
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
Substrates: -
Products: -
Products: -
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
Substrates: -
Products: -
Products: -
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine
Substrates: -
Products: -
Products: -
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine
Substrates: -
Products: -
Products: -
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine
Substrates: -
Products: -
Products: -
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine
Substrates: -
Products: -
Products: -
?
ATP + pentapeptide + UDP-muramate
ADP + phosphate + UDP-muramyl-pentapeptide
-
Substrates: -
Products: -
Products: -
?
ATP + pentapeptide + UDP-muramate
ADP + phosphate + UDP-muramyl-pentapeptide
-
Substrates: -
Products: -
Products: -
?
ATP + pentapeptide + UDP-muramate
ADP + phosphate + UDP-muramyl-pentapeptide
-
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: substrate specificity of Mpl, overview. No activity with L-Ala-c-D-Glu-L-Lys-D-Ala-D-Ala
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity of Mpl, overview. No activity with L-Ala-c-D-Glu-L-Lys-D-Ala-D-Ala
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of Mpl, overview. No activity with L-Ala-c-D-Glu-L-Lys-D-Ala-D-Ala
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
Substrates: -
Products: -
Products: -
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0117
L-alanine
pH 8.4, temperature not specified in the publication, recombinant His-tagged enzyme
0.023
L-alanyl-gamma-D-glutamate
pH 8.4, temperature not specified in the publication, recombinant His-tagged enzyme
0.0042
L-alanyl-gamma-D-glutamyl-L-lysine
pH 8.4, temperature not specified in the publication, recombinant His-tagged enzyme
0.0017
L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanine
pH 8.4, temperature not specified in the publication, recombinant His-tagged enzyme
4.33
L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
pH 8.4, temperature not specified in the publication, recombinant His-tagged enzyme
0.098
L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine
pH 8.4, temperature not specified in the publication, recombinant His-tagged enzyme
0.088
L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine
pH 8.4, temperature not specified in the publication, recombinant His-tagged enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
Mpl and MurC-F enzymes have three domains that are classified in Pfam families, PF01225 Mur ligase catalytic domain, PF08245 Mur ligase middle domain, and PF02875 Mur ligase glutamate binding/C-terminal domain, structure comparisons, overview
evolution
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Mpl and MurC-F enzymes have three domains that are classified in Pfam families, PF01225 Mur ligase catalytic domain, PF08245 Mur ligase middle domain, and PF02875 Mur ligase glutamate binding/C-terminal domain, structure comparisons, overview
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physiological function
in Gram-negative bacteria, 30-60% of the bacterial cell wall is recycled during each generation. Part of this recycling process involves the murein peptide ligase, which attaches the breakdown product, the tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate, to UDP-MurNAc
physiological function
-
in Gram-negative bacteria, 30-60% of the bacterial cell wall is recycled during each generation. Part of this recycling process involves the murein peptide ligase, which attaches the breakdown product, the tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate, to UDP-MurNAc
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additional information
unique sequence-structure relationships of Mpl proteins, overview, Residues Arg357, Arg358, Phe374, Ala375, His376, His377, Glu402, Pro403, Arg404, Ser405, Asn406, Thr407, Ser483, Asn484 and Gly485 may be important in binding tri, tetra, and pentapeptide substrates
additional information
-
unique sequence-structure relationships of Mpl proteins, overview, Residues Arg357, Arg358, Phe374, Ala375, His376, His377, Glu402, Pro403, Arg404, Ser405, Asn406, Thr407, Ser483, Asn484 and Gly485 may be important in binding tri, tetra, and pentapeptide substrates
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). E3GZ29_METFV
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
476
0
53546
TrEMBL
-
Q4FVQ2_PSYA2
Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4)
505
0
54888
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57000
x * 57187, His-tagged enzyme, sequence calculation, x * 57000, recombinant His-tagged enzyme, SDS-PAGE
57187
x * 57187, His-tagged enzyme, sequence calculation, x * 57000, recombinant His-tagged enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 57187, His-tagged enzyme, sequence calculation, x * 57000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 57187, His-tagged enzyme, sequence calculation, x * 57000, recombinant His-tagged enzyme, SDS-PAGE
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additional information
PaMpl can be divided into 3 distinct domains: the N-terminal UDPMurNAc-binding domain (residues 1-102), the middle ATP-binding domain (residues 103-357) and the C-terminal tripeptide-binding domain (residues 358-505)
additional information
-
PaMpl can be divided into 3 distinct domains: the N-terminal UDPMurNAc-binding domain (residues 1-102), the middle ATP-binding domain (residues 103-357) and the C-terminal tripeptide-binding domain (residues 358-505)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme, randomised microseed matrix screening, using 0.1 M buffer system 6, pH 8.5, 50% (v/v) precipitant mix of 25% (w/v) PEG 4000 and 40% (w/v) 1,2,6-hexanetriol
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apoenzyme and UDP-bound enzyme, sitting drop vapor diffusion method, using 0.2 M ammonium sulfate and 30% (w/v) PEG 4000 at pH 5.4
purified enzyme, X-ray diffraction structure determination and analysis at 1.65 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D254G
-
the mutant is resistant to piperacillin-tazobactam, while minimal inhibitory concentration of several other beta-lactams increases 4-32fold compared to the wild type enzyme
L16fs
-
the mutant is resistant to piperacillin-tazobactam, while minimal inhibitory concentration of several other beta-lactams increases 4-32fold compared to the wild type enzyme
N185fs
-
the mutant is resistant to piperacillin-tazobactam, while minimal inhibitory concentration of several other beta-lactams increases 4-32fold compared to the wild type enzyme
R180fs
-
the mutant is resistant to piperacillin-tazobactam, while minimal inhibitory concentration of several other beta-lactams increases 4-32fold compared to the wild type enzyme
T111P
-
the mutant is resistant to piperacillin-tazobactam, while minimal inhibitory concentration of several other beta-lactams increases 4-32fold compared to the wild type enzyme
T340P
-
the mutant is resistant to piperacillin-tazobactam, while minimal inhibitory concentration of several other beta-lactams increases 4-32fold compared to the wild type enzyme
W236R
-
the mutant is resistant to piperacillin-tazobactam, while minimal inhibitory concentration of several other beta-lactams increases 4-32fold compared to the wild type enzyme
L184fs
-
the mutant is resistant to piperacillin-tazobactam, while minimal inhibitory concentration of several other beta-lactams increases 4-32fold compared to the wild type enzyme
L305Q
-
the mutant is resistant to piperacillin-tazobactam, while minimal inhibitory concentration of several other beta-lactams increases 4-32fold compared to the wild type enzyme
R153H
-
the mutant is resistant to piperacillin-tazobactam, while minimal inhibitory concentration of several other beta-lactams increases 4-32fold compared to the wild type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
recombinant His-tagged enzyme from Escherichia coli strain MLD2502 by nickel and cobalt affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
gene mpl, chromosomal mpl gene, DNA and mino acid sequence determination and analysis, expression of His-tagged enzyme in an Escherichia coli chromosomal mpl gene-deficient mutant strain MLD2502
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Das, D.; Herve, M.; Feuerhelm, J.; Farr, C.; Chiu, H.; Elsliger, M.; Knuth, M.; Klock, H.; Miller, M.; Godzik, A.; Lesley, S.; Deacon, A.; Mengin-Lecreulx, D.; Wilson, I.
Structure and function of the first full-length murein peptide ligase (Mpl) cell wall recycling protein
PLoS ONE
6
e17624
2011
Psychrobacter arcticus (Q4FVQ2), Psychrobacter arcticus 273-4 (Q4FVQ2), Psychrobacter arcticus 273-4
brenda
Subedi, B.P.; Schofield, L.R.; Carbone, V.; Wolf, M.; Martin, W.F.; Ronimus, R.S.; Sutherland-Smith, A.J.
Structural characterisation of methanogen pseudomurein cell wall peptide ligases homologous to bacterial MurE/F murein peptide ligases
Microbiology
168
001235
2022
Methanothermus fervidus (E3GZ29), Methanothermobacter thermautotrophicus, Methanothermus fervidus DSM 1088 (E3GZ29), Methanothermobacter thermautotrophicus B69198
brenda
Andersen, C.; Gabrielaite, M.; Norskov-Lauritsen, N.
Induction of broad beta-lactam resistance in Achromobacter ruhlandii by exposure to ticarcillin is primarily linked to substitutions in murein peptide ligase Mpl
Microorganisms
10
420
2022
Achromobacter insuavis, Achromobacter ruhlandii, Achromobacter xylosoxidans
brenda
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