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GlcNAc-MurNAc tetrapeptide + H2O
?
substrate prepared from purified murein by lysozyme, cleaves specifically between meso-diaminopimelic acid and D-alanine
-
-
?
L-Ala-D-Gln-L-Lys-D-Ala + H2O
L-Ala-D-Gln-L-Lys + D-Ala
L-Ala-D-Glu-(L)-meso-diaminopimelic-acid-(omegaNH2)-(L)-D-Ala + H2O
L-Ala-D-Glu-(L)-meso-diaminopimelic-acid-(omegaNH2) + (L)-D-Ala
L-Ala-gamma-D-Glu-L-Lys-D-Ala + H2O
?
L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
L-Ala-gamma-D-Glu-meso-diaminopimelyl + D-Ala
Modified muropeptides + H2O
?
N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-Lys-D-Ala + H2O
N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-Lys + D-Ala
-
-
-
-
?
N-Acetylglucosamine-N-acetylmuramyl-Ala-D-Glu-Dap-D-Ala + H2O
N-Acetylglucosamine-N-acetylmuramyl-Ala-D-Glu-Dap + D-Ala
-
-
-
?
N-acetylmuramoyl-Ala-D-Glu-Dap-D-Ala + H2O
N-acetylmuramoyl-Ala-D-Glu-Dap + D-Ala
-
-
-
?
N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala + H2O
N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala
N-acetylmuramyl-L-Ala-D-Glu-meso-diaminopimelyl-D-Ala + H2O
N-acetylmuramyl-L-Ala-D-Glu-meso-diaminopimelate + D-Ala
peptidoglycan + H2O
?
the enzyme is involved in peptidoglycan recycling
-
-
?
UDP-N-acetylmuramyl-Ala-D-Glu-Dap-D-Ala + H2O
UDP-N-acetylmuramyl-Ala-D-Glu-Dap + D-Ala
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
UDP-N-acetylmuramyl-L-Ala-D-Glu-meso-diaminopimelate + D-Ala
additional information
?
-
L-Ala-D-Gln-L-Lys-D-Ala + H2O
L-Ala-D-Gln-L-Lys + D-Ala
-
-
-
?
L-Ala-D-Gln-L-Lys-D-Ala + H2O
L-Ala-D-Gln-L-Lys + D-Ala
-
-
-
?
L-Ala-D-Glu-(L)-meso-diaminopimelic-acid-(omegaNH2)-(L)-D-Ala + H2O
L-Ala-D-Glu-(L)-meso-diaminopimelic-acid-(omegaNH2) + (L)-D-Ala
-
-
-
?
L-Ala-D-Glu-(L)-meso-diaminopimelic-acid-(omegaNH2)-(L)-D-Ala + H2O
L-Ala-D-Glu-(L)-meso-diaminopimelic-acid-(omegaNH2) + (L)-D-Ala
-
-
-
?
L-Ala-gamma-D-Glu-L-Lys-D-Ala + H2O
?
-
-
-
-
?
L-Ala-gamma-D-Glu-L-Lys-D-Ala + H2O
?
-
-
-
-
?
L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
L-Ala-gamma-D-Glu-meso-diaminopimelyl + D-Ala
-
-
-
-
?
L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
L-Ala-gamma-D-Glu-meso-diaminopimelyl + D-Ala
-
-
-
?
L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
L-Ala-gamma-D-Glu-meso-diaminopimelyl + D-Ala
-
-
-
?
Modified muropeptides + H2O
?
-
all tested disaccharide-tetrapeptide monomeric muropeptides modified at position 4, monomers with m-lanthionine, but not with L-ornithine, instead of m-diaminopimelic acid at position 3
-
-
?
Modified muropeptides + H2O
?
-
all tested disaccharide-tetrapeptide monomeric muropeptides modified at position 4, monomers with m-lanthionine, but not with L-ornithine, instead of m-diaminopimelic acid at position 3
-
-
?
muropeptides + H2O
?
-
-
incubation of isoform Pgp2 with peptidglucan from the Pgp2 mutant strain results in a 94% reduction of monomeric tetrapeptides, a 68% reduction in dimeric tetrapeptides, and a 47% reduction in trimeric tetrapeptides
-
?
muropeptides + H2O
?
-
incubation of isoform LcdB with peptidoglucan from the LcdB mutant strain leads to almost quantitative digestion of peptidoglucan tetrapeptides with a carboxy-terminal D-Ala producing the tripeptides
-
?
muropeptides + H2O
?
-
incubation of isoform LcdB with peptidoglucan from the LcdB mutant strain leads to almost quantitative digestion of peptidoglucan tetrapeptides with a carboxy-terminal D-Ala producing the tripeptides
-
?
N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala + H2O
N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala
-
-
-
?
N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala + H2O
N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala
-
-
-
?
N-acetylmuramyl-L-Ala-D-Glu-meso-diaminopimelyl-D-Ala + H2O
N-acetylmuramyl-L-Ala-D-Glu-meso-diaminopimelate + D-Ala
-
-
-
?
N-acetylmuramyl-L-Ala-D-Glu-meso-diaminopimelyl-D-Ala + H2O
N-acetylmuramyl-L-Ala-D-Glu-meso-diaminopimelate + D-Ala
-
-
-
?
UDP-N-acetylmuramyl-Ala-D-Glu-Dap-D-Ala + H2O
UDP-N-acetylmuramyl-Ala-D-Glu-Dap + D-Ala
-
-
-
?
UDP-N-acetylmuramyl-Ala-D-Glu-Dap-D-Ala + H2O
UDP-N-acetylmuramyl-Ala-D-Glu-Dap + D-Ala
-
-
-
?
UDP-N-acetylmuramyl-Ala-D-Glu-Dap-D-Ala + H2O
UDP-N-acetylmuramyl-Ala-D-Glu-Dap + D-Ala
-
-
-
?
UDP-N-acetylmuramyl-Ala-D-Glu-Dap-D-Ala + H2O
UDP-N-acetylmuramyl-Ala-D-Glu-Dap + D-Ala
-
enzyme can also replace the terminal D-alanine with a variety of amino acids with D-asymmetric centers for transpeptidation
-
?
UDP-N-acetylmuramyl-Ala-D-Glu-Dap-D-Ala + H2O
UDP-N-acetylmuramyl-Ala-D-Glu-Dap + D-Ala
-
-
-
?
UDP-N-acetylmuramyl-Ala-D-Glu-Dap-D-Ala + H2O
UDP-N-acetylmuramyl-Ala-D-Glu-Dap + D-Ala
-
-
-
?
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
UDP-N-acetylmuramyl-L-Ala-D-Glu-meso-diaminopimelate + D-Ala
-
-
-
?
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
UDP-N-acetylmuramyl-L-Ala-D-Glu-meso-diaminopimelate + D-Ala
-
-
-
?
additional information
?
-
-
enzyme also has D-amino acid exchange activity
-
-
?
additional information
?
-
-
isoform Pgp2 is a LD-carboxypeptidase cleaving monomeric and cross-linked disaccharide tetrapeptides to tripeptides
-
-
?
additional information
?
-
-
no direct effect of LD-carboxypeptidase on macromolecular murein metabolism
-
-
?
additional information
?
-
-
the enzyme is involved in cell wall synthesis
-
-
?
additional information
?
-
-
the enzyme is specific for D-Ala and requires a substrate chain length of 4 monomers, no or poor activity with L-Ala-gamma-D-Glu-L-Lys-L-Ala, D-Glu-L-Lys-D-Ala and L-Lys-D-Ala
-
-
?
additional information
?
-
-
no direct effect of LD-carboxypeptidase on macromolecular murein metabolism
-
-
?
additional information
?
-
-
the enzyme is involved in cell wall synthesis
-
-
?
additional information
?
-
-
the enzyme is specific for D-Ala and requires a substrate chain length of 4 monomers, no or poor activity with L-Ala-gamma-D-Glu-L-Lys-L-Ala, D-Glu-L-Lys-D-Ala and L-Lys-D-Ala
-
-
?
additional information
?
-
-
cleaves the peptide side chain of peptidoglycan between L-Lys and D-Ala
-
-
?
additional information
?
-
-
the enzyme is involved in cell wall synthesis
-
-
?
additional information
?
-
enzyme prefers tetrapeptide substrates and can discriminate between tetrapeptide and pentapeptide substrates, but is less selective toward the N-terminal sugar moiety. No substrate: UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala-D-Ala, poor substrate: N-acetylmuramyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala
-
-
?
additional information
?
-
enzyme prefers tetrapeptide substrates and can discriminate between tetrapeptide and pentapeptide substrates, but is less selective toward the N-terminal sugar moiety. No substrate: UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala-D-Ala, poor substrate: N-acetylmuramyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala
-
-
?
additional information
?
-
-
enzyme prefers tetrapeptide substrates and can discriminate between tetrapeptide and pentapeptide substrates, but is less selective toward the N-terminal sugar moiety. No substrate: UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala-D-Ala, poor substrate: N-acetylmuramyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala
-
-
?
additional information
?
-
-
incorporation of diaminopimelate into cell walls
-
-
?
additional information
?
-
the enzyme is a serine peptidase which cleaves between the L- and D-amino acids of bacterial peptidoglycan
-
-
?
additional information
?
-
-
the enzyme is a serine peptidase which cleaves between the L- and D-amino acids of bacterial peptidoglycan
-
-
?
additional information
?
-
no activity with substrate L-Ala-D-Gln-L-Lys-L-Ala
-
-
?
additional information
?
-
-
no activity with substrate L-Ala-D-Gln-L-Lys-L-Ala
-
-
?
additional information
?
-
no activity with substrate L-Ala-D-Gln-L-Lys-L-Ala
-
-
?
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Metz, R.; Henning, S.; Hammes, W.P.
LD-Carboxypeptidase activity in Escherichia coli. II. Isolation, purification and characterization of the enzyme from E. coli K 12
Arch. Microbiol.
144
181-186
1986
Escherichia coli
brenda
Rousset, A.; Nguyen-Disteche, M.; Minck, R.; Ghuysen, J.M.
Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms
J. Bacteriol.
152
1042-1048
1982
Proteus vulgaris, Proteus vulgaris P18
brenda
DasGupta, H.; Fan, D.P.
Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan
J. Biol. Chem.
254
5672-5683
1979
Priestia megaterium
brenda
Ursinus, A.; Steinhaus, H.; Hltje, J.V.
Purification of a nocardicin A-sensitive LD-carboxypeptidase from Escherichia coli by affinity chromatography
J. Bacteriol.
174
441-446
1992
Escherichia coli, Escherichia coli W3110 / ATCC 27325
brenda
Leguina, J.I.; Quintela, J.C.; de Pedro, M.A.
Substrate specificity of Escherichia coli LD-carboxypeptidase on biosynthetically modified muropeptides
FEBS Lett.
339
249-252
1994
Escherichia coli, Escherichia coli MC6RP1
brenda
Arminjon, F.; Guinand, M.; Vacheron, M.J.; Michel, G.
Specificity profiles of the membrane-bound gamma-D-glutamyl-(L)meso-diaminopimelateendopeptidase and LD-carboxypeptidase from Bacillus sphaericus 9602
Eur. J. Biochem.
73
557-565
1977
Lysinibacillus sphaericus, Lysinibacillus sphaericus 9602
brenda
Hammes, W.P.
The LD-carboxypeptidase activity in Gaffkya homari. The target of the action of D-amino acids or glycine on the formation of wall-bound peptidoglycan
Eur. J. Biochem.
91
501-507
1978
Aerococcus viridans
brenda
Hammes, W.P.; Seidel, H.
The LD-carboxypeptidase activity in Gaffkya homari. The target of the action of certain beta-lactam antibiotics on the formation of wall-bound peptidoglycan
Eur. J. Biochem.
91
509-515
1978
Aerococcus viridans
brenda
Baum, E.Z.; Crespo-Carbone, S.M.; Foleno, B.; Peng, S.; Hilliard, J.J.; Abbanat, D.; Goldschmidt, R.; Bush, K.
Identification of a dithiazoline inhibitor of Escherichia coli L,D-carboxypeptidase A
Antimicrob. Agents Chemother.
49
4500-4507
2005
Escherichia coli, Escherichia coli MG1655
brenda
Severin, A.; Wu, S.W.; Tabei, K.; Tomasz, A.
High-level beta-lactam resistance and cell wall synthesis catalyzed by the mecA homologue of Staphylococcus sciuri introduced into Staphylococcus aureus
J. Bacteriol.
187
6651-6658
2005
Mammaliicoccus sciuri
brenda
Korza, H.J.; Bochtler, M.
Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow
J. Biol. Chem.
280
40802-40812
2005
Pseudomonas aeruginosa (Q9HTZ1), Pseudomonas aeruginosa
brenda
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
brenda
Courtin, P.; Miranda, G.; Guillot, A.; Wessner, F.; Mezange, C.; Domakova, E.; Kulakauskas, S.; Chapot-Chartier, M.
Peptidoglycan structure analysis of Lactococcus lactis reveals the presence of an L,D-carboxypeptidase involved in peptidoglycan maturation
J. Bacteriol.
188
5293-5298
2006
Lactococcus lactis
brenda
Nikoh, N.; Nakabachi, A.
Aphids acquired symbiotic genes via lateral gene transfer
BMC Biol.
7
12
2009
Acyrthosiphon pisum (B9ZYY6)
brenda
Nikoh, N.; McCutcheon, J.P.; Kudo, T.; Miyagishima, S.Y.; Moran, N.A.; Nakabachi, A.
Bacterial genes in the aphid genome: absence of functional gene transfer from Buchnera to its host
PLoS Genet.
6
e1000827
2010
Acyrthosiphon pisum
brenda
Das, D.; Herve, M.; Elsliger, M.A.; Kadam, R.U.; Grant, J.C.; Chiu, H.J.; Knuth, M.W.; Klock, H.E.; Miller, M.D.; Godzik, A.; Lesley, S.A.; Deacon, A.M.; Mengin-Lecreulx, D.; Wilson, I.A.
Structure and function of a novel LD-carboxypeptidase a involved in peptidoglycan recycling
J. Bacteriol.
195
5555-5566
2013
Novosphingobium aromaticivorans (Q2G8F3), Novosphingobium aromaticivorans DSM 12444 (Q2G8F3), Novosphingobium aromaticivorans DSM 12444
brenda
Frirdich, E.; Vermeulen, J.; Biboy, J.; Soares, F.; Taveirne, M.E.; Johnson, J.G.; DiRita, V.J.; Girardin, S.E.; Vollmer, W.; Gaynor, E.C.
Peptidoglycan LD-carboxypeptidase Pgp2 influences Campylobacter jejuni helical cell shape and pathogenic properties and provides the substrate for the DL-carboxypeptidase Pgp1
J. Biol. Chem.
289
8007-8018
2014
Campylobacter jejuni
brenda
Hoyland, C.N.; Aldridge, C.; Cleverley, R.M.; Duchene, M.C.; Minasov, G.; Onopriyenko, O.; Sidiq, K.; Stogios, P.J.; Anderson, W.F.; Daniel, R.A.; Savchenko, A.; Vollmer, W.; Lewis, R.J.
Structure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognition
Structure
22
949-960
2014
Streptococcus pneumoniae (Q8DQQ1), Streptococcus pneumoniae, Streptococcus pneumoniae ATCC BAA-255 (Q8DQQ1)
brenda
Meyer, K.; Addy, C.; Akashi, S.; Roper, D.I.; Tame, J.R.H.
The crystal structure and oligomeric form of Escherichia coli L,D-carboxypeptidase A
Biochem. Biophys. Res. Commun.
499
594-599
2018
Escherichia coli
brenda