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Information on EC 6.3.2.13 - UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-2,6-diaminopimelate ligase and Organism(s) Escherichia coli and UniProt Accession P22188

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IUBMB Comments
Involved in the synthesis of a cell-wall peptide in bacteria. This enzyme adds diaminopimelate in Gram-negative organisms and in some Gram-positive organisms; in others EC 6.3.2.7 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase) adds lysine instead. It is the amino group of the L-centre of the diaminopimelate that is acylated.
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This record set is specific for:
Escherichia coli
UNIPROT: P22188
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
mur ligase, amide ligase, meso-diaminopimelate-adding enzyme, udp-n-acetylmuramyl tripeptide synthetase, udp-n-acetylmuramoyl-l-alanyl-d-glutamate-2,6-diaminopimelate ligase, mure synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Diaminopimelic-adding enzyme
-
-
-
-
mDAP ligase
-
-
-
-
Meso-diaminopimelate-adding enzyme
-
-
-
-
MurE synthetase
-
-
-
-
Synthetase, uridine diphospho-N-acetylmuramoylalanyl-D-glutamyl-meso-2,6-diaminopimelate
-
-
-
-
UDP-MurNAc-tripeptide synthetase
-
-
-
-
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelate synthetase
-
-
-
-
UDP-N-acetylmuramyl-tripeptide synthetase
-
-
-
-
UDPMurNAc-L-alanyl-D-glutamate:mDAP ligase (ADP-forming)
-
-
-
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Uridine diphosphate N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase
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-
-
-
Uridine-diphosphate-N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
show the reaction diagram
acyl phosphate intermediate
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide formation
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-
-
-
carboxamide formation
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:(L)-meso-2,6-diaminoheptanedioate gamma-ligase (ADP-forming)
Involved in the synthesis of a cell-wall peptide in bacteria. This enzyme adds diaminopimelate in Gram-negative organisms and in some Gram-positive organisms; in others EC 6.3.2.7 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase) adds lysine instead. It is the amino group of the L-centre of the diaminopimelate that is acylated.
CAS REGISTRY NUMBER
COMMENTARY hide
9075-09-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate
show the reaction diagram
ATP + dihydrouridine-5'-diphosphate-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate
ADP + phosphate + dihydrouridine-5'-diphosphate-MurNAc-L-Ala-D-Glu-meso-2,6-diaminoheptanedioate
show the reaction diagram
-
-
-
?
ATP + UDP-MurNAc-L-Ala-D-Glu + D-allo-cystathionine
ADP + phosphate + UDP-MurNAc-L-Ala-D-Glu-D-allo-cystathionine
show the reaction diagram
-
-
-
?
ATP + UDP-MurNAc-L-Ala-D-Glu + L-allo-cystathionine
ADP + phosphate + UDP-MurNAc-L-Ala-D-Glu-L-allo-cystathionine
show the reaction diagram
-
-
-
?
ATP + UDP-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate
show the reaction diagram
ATP + UDP-MurNAc-L-Ala-D-Glu + meso-lanthionine
ADP + phosphate + UDP-MurNAc-L-Ala-D-Glu-meso-lanthionine
show the reaction diagram
-
-
-
?
ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate
show the reaction diagram
ATP + UDP-N-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate
?
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate
show the reaction diagram
part of bacterial cell-wall peptidoglycan biosynthesis
-
r
ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate
show the reaction diagram
-
-
-
?
ATP + UDP-N-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
potassium phosphate increases activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Butylamine
-
500 mM, 88% inhibition
Butyrate
-
500 mM, 44% inhibition
ethylamine
-
500 mM, 73% inhibition
methylamine
-
500 mM, 80% inhibition
MurNAc(alpha-methyl)-L-Ala-D-Glu
-
-
MurNAc(beta-methyl)-L-Ala-D-Glu
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-
Nalpha-Propionyl-L-Ala-2-amino-6-phosphonohexanoate
-
-
Nalpha-Propionyl-L-Ala-3-phosphonoacetamido-Ala
-
-
Nalpha-Propionyl-L-Ala-buthionine sulfoximine
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-
P1-MurNAc-L-Ala-D-Glu
-
-
Propionyl-L-Ala-D-Glu(CH2Cl)-OH
-
-
Propionyl-L-Ala-xi-2-amino-4-phosphonobutanoate
-
-
Propylamine
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500 mM, 87% inhibition
additional information
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.62
ATP
-
-
10
D-allo-cystathionine
-
-
0.097
dihydrouridine-5'-diphosphate-MurNAc-L-Ala-D-Glu
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-
3.9
L-allo-cystathionine
-
-
0.036 - 0.04
meso-2,6-diaminoheptanedioate
1.5
meso-lanthionine
-
-
0.035 - 0.076
UDP-N-MurNAc-L-Ala-D-Glu
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.625
recombinant His-tagged MurE
0.00259
-
-
0.0047
-
K224A mutant
0.0393
-
-
0.078
-
K224A mutant, in the presence of 500 mM propionate
1.24
-
recombinant wild-type MurE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 9.5
-
about 40% of maximal activity at pH 7.2 and 9.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
-
1 * 56000, SDS-PAGE
62000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 56000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of native and selenomethionine MurE are grown in the presence of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate, 0.002 ml of protein solution containing 10 mg/ml enzyme, 20 mM HEPES, pH 7.5 200 mM NaCl, 5 mM dithiothreitol and 1 mM UDP-N-acetylmuramoyl-L-alanyl-D-glutamate, are equilibrated together with 0.002 ml reservoir buffer consisting of 100 mM HEPES, pH 7.5, 13% polyethylene glycol monomethyl ether 5000, 500 mM LiCl, 10% isopropanol and 5 mM dithiothreitol, against 1 ml reservoir buffer, crystals diffract to 2.0 A
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, complete loss of activity after 2 d
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged MurE, Ni2+-nitrilotriacetate agarose
recombinant MurE
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged MurE and selenomethionine-MurE in Escherichia coli
expresision of His-tagged MurE in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abo-Ghalia, M.; Michaud, C.; Blanot D.; van Heijenoort, J.
Specificity of the uridine-diphosphate-N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate synthetase from Escherichia coli
Eur. J. Biochem.
153
81-87
1985
Escherichia coli
Manually annotated by BRENDA team
Mengin-Lecreulx, D.; van Heijenoort, J.; Park, J.T.
Identification of the mpl gene encoding UDP-N-acetylmuramate:L-alanyl-gamma-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan
J. Bacteriol.
178
5347-5352
1996
Escherichia coli
Manually annotated by BRENDA team
Banerjee, R.V.; Shane, B.; McGuire, J.J.; Coward, J.K.
Dihydrofolate synthetase and folylpolyglutamate synthetase: direct evidence for intervention of acyl phosphate intermediates
Biochemistry
27
9062-9070
1988
Escherichia coli
Manually annotated by BRENDA team
le Roux, P.; Auger, G.; van Heijenoort, J.; Blanot, D.
Synthesis of new peptide inhibitors of the meso-diaminopimelate-adding enzyme
Eur. J. Med. Chem.
27
899-907
1992
Escherichia coli
-
Manually annotated by BRENDA team
Abo-Ghalia, M.; Flegel, M.; Blanot, D.; van Heijenoort, J.
Synthesis of inhibitors of the meso-diaminopimelate-adding enzyme from Escherichia coli
Int. J. Pept. Protein Res.
32
208-222
1988
Escherichia coli
Manually annotated by BRENDA team
Mengin-Lecreulx, D.; Blanot, D.; van Heijenoort, J.
Replacement of diaminopimelic acid by cystathionine or lanthionine in the peptidoglycan of Escherichia coli
J. Bacteriol.
176
4321-4327
1994
Escherichia coli
Manually annotated by BRENDA team
Michaud, C.; Mengin-Lecreulx, D.; van Heijenoort, J.; Blanot, D.
Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase from Escherichia coli
Eur. J. Biochem.
194
853-861
1990
Escherichia coli
Manually annotated by BRENDA team
Mengin-Lecreulx, D.; Flouret, B.; Van Heijenoort, J.
Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli
J. Bacteriol.
151
1109-1117
1982
Escherichia coli
Manually annotated by BRENDA team
Dementin, S.; Bouhss, A.; Auger, G.; Parquet, C.; Mengin-Lecreulx, D.; Dideberg, O.; van Heijenoort, J.; Blanot, D.
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as established by chemical rescue experiments
Eur. J. Biochem.
268
5800-5807
2001
Escherichia coli
Manually annotated by BRENDA team
Gordon, E.; Flouret, B.; Chantalat, L.; van Heijenoort, J.; Mengin-Lecreulx, D.; Dideberg, O.
Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-diaminopimelate ligase from Escherichia coli
J. Biol. Chem.
276
10999-11006
2001
Escherichia coli (P22188)
Manually annotated by BRENDA team
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
J. Bacteriol.
189
3987-3995
2007
Escherichia coli
Manually annotated by BRENDA team