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Information on EC 6.3.2.B2 - murein peptide ligase
for references in articles please use BRENDA:EC6.3.2.B2preliminary BRENDA-supplied EC number
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EC Tree
6.3.2.B2 murein peptide ligaseSpecify your search results
The expected taxonomic range for this enzyme is: Psychrobacter arcticus
Reaction Schemes
Synonyms
Mpl, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Mpl
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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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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
ATP + L-alanyl-gamma-D-glutamyl-L-lysine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
ATP + L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-L-lysyl-D-alanine
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-
-
?
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
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-
-
?
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
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-
?
ATP + L-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
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-
-
?
ATP + L-alanine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
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-
-
?
ATP + L-alanyl-gamma-D-glutamate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamate
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-
-
?
ATP + L-alanyl-gamma-D-glutamate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamate
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-
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?
ATP + L-alanyl-gamma-D-glutamyl-L-lysine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
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-
-
?
ATP + L-alanyl-gamma-D-glutamyl-L-lysine + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
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-
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
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-
-
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
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additional information
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substrate specificity of Mpl, overview. No activity with L-Ala-c-D-Glu-L-Lys-D-Ala-D-Ala
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?
additional information
?
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substrate specificity of Mpl, overview. No activity with L-Ala-c-D-Glu-L-Lys-D-Ala-D-Ala
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?
additional information
?
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substrate specificity of Mpl, overview. No activity with L-Ala-c-D-Glu-L-Lys-D-Ala-D-Ala
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
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-
-
?
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + UDP-MurNAc
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
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?
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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
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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
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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
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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). 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
?
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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
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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
purified enzyme, X-ray diffraction structure determination and analysis at 1.65 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain MLD2502 by nickel and cobalt affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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