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2-[(ammonioacetyl)amino]-3-[[3-([2-[(1-carboxylatoethyl)amino]-1-methyl-2-oxoethyl]amino)-3-oxopropyl]sulfanyl]propanoate + H2O
?
-
-
-
-
?
2-[(ammonioacetyl)amino]-3-[[3-([2-[(1-carboxylatoethyl)sulfanyl]-1-methyl-2-oxoethyl]amino)-3-oxopropyl]sulfanyl]propanoate + H2O
?
-
-
-
-
?
2-[(ammonioacetyl)amino]-7-([2-[(1-carboxylatoethyl)amino]-1-methyl-2-oxoethyl]amino)-7-oxoheptanoate + H2O
?
-
-
-
-
?
2-[[N-(phenylacetyl)alanyl]sulfanyl]propanoic acid + H2O
?
-
-
-
-
?
3-[[N-(phenylacetyl)alanyl]oxy]benzoic acid + H2O
?
-
-
-
-
?
3-[[N-(phenylacetyl)glycyl]oxy]benzoic acid + H2O
?
-
-
-
-
?
acetyl-Gly-D-Ala-D-Ala + H2O
acetyl-Gly-D-Ala + D-Ala
-
-
-
-
?
acetyl-L-Ala-D-Ala-D-Ala + H2O
acetyl-L-Ala-D-Ala + D-Ala
-
-
-
-
?
diacetyl-L-diaminobutyryl-D-Ala-D-Ala + H2O
diacetyl-L-diaminobutyryl-D-Ala + D-Ala
-
-
-
-
?
diacetyl-L-Lys-D-Ala-D-Ala + H2O
diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
-
?
L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala + H2O
L-Ala-D-gamma-Glu-L-Lys-D-Ala + D-Ala
-
D,D-carboxypeptidase activity of penicillin-binding proteins
-
-
?
methyl N-acetylmuramate-L-Ala-gamma-D-Glu-meso-diaminopimelate-D-Ala-D-Ala + H2O
methyl N-acetylmuramate-L-Ala-gamma-D-Glu-meso-diaminopimelate-D-Ala + D-Ala
muramoylpentapeptide + H2O
muramoyltetrapeptide + D-Ala
-
-
-
-
?
N,N'-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
N,N'-diacetyl-L-lysyl-D-alanine + D-alanine
-
-
-
-
?
Nalpha, Nepsilon-diacetyl L-Lys-D-Ala-Gly + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
penicillin + H2O
a carboxylate + 6-aminopenicillanate
-
very slow hydrolysis
-
?
UDP-MurNAc-pentapeptide + H2O
UDP-MurNAc-tetrapeptide + D-Ala
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanine + D-alanine
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala-D-Ala + H2O
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala + D-Ala
additional information
?
-
methyl N-acetylmuramate-L-Ala-gamma-D-Glu-meso-diaminopimelate-D-Ala-D-Ala + H2O
methyl N-acetylmuramate-L-Ala-gamma-D-Glu-meso-diaminopimelate-D-Ala + D-Ala
-
-
-
?
methyl N-acetylmuramate-L-Ala-gamma-D-Glu-meso-diaminopimelate-D-Ala-D-Ala + H2O
methyl N-acetylmuramate-L-Ala-gamma-D-Glu-meso-diaminopimelate-D-Ala + D-Ala
-
-
-
?
Nalpha, Nepsilon-diacetyl L-Lys-D-Ala-Gly + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + Gly
-
-
-
-
?
Nalpha, Nepsilon-diacetyl L-Lys-D-Ala-Gly + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + Gly
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
-
?
UDP-MurNAc-pentapeptide + H2O
UDP-MurNAc-tetrapeptide + D-Ala
-
i.e. UDP-acetylmuramic acid-L-Ala-D-iGlu-L-Lys-D-Ala-D-Ala
-
-
?
UDP-MurNAc-pentapeptide + H2O
UDP-MurNAc-tetrapeptide + D-Ala
-
i.e. UDP-N-acetylmuramic acid-L-Ala-D-iGlu-L-Lys-D-Ala-D-Ala
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
-
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
-
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
-
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
-
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanine + D-alanine
-
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanine + D-alanine
-
-
-
-
?
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala-D-Ala + H2O
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala + D-Ala
-
-
-
-
?
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala-D-Ala + H2O
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala + D-Ala
-
-
-
-
?
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala-D-Ala + H2O
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala + D-Ala
-
-
-
-
?
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala-D-Ala + H2O
UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala + D-Ala
-
-
-
-
?
additional information
?
-
-
activation of the L,D-transpeptidation pathway can also release inhibition of transglycosylation, leading to cross-resistance to glycopeptides and beta-lactams following extensive hydrolysis of D-Ala5 from the cytoplasmic precursor UDP-MurNAc-pentapeptide by a D,D-carboxypeptidase, mechanism of glycopeptide resistance, overview
-
-
?
additional information
?
-
-
no substrate: UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-serine
-
-
?
additional information
?
-
-
no substrate: UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-serine
-
-
?
additional information
?
-
-
PBP5 performs a DD-carboxypeptidase reaction on the bacterial peptidoglycan, the major constituent of the cell wall
-
-
?
additional information
?
-
-
the enzyme is involved in cell wall formation, overview
-
-
?
additional information
?
-
-
the enzyme is involved in cell wall formation, overview
-
-
?
additional information
?
-
-
the enzyme is involved in cell wall synthesis, the cell wall forming pentapeptide unit of Staphylococcus sciuri consists of a D-alanine and for glycine residues
-
-
?
additional information
?
-
-
influence of residue preceeding C-terminal D-Ala-D-Ala on rate of hydrolysis
-
-
?
additional information
?
-
-
influence of residue preceeding C-terminal D-Ala-D-Ala on rate of hydrolysis
-
-
?
additional information
?
-
enzyme displays both D,D-carboxypeptidase and expanded-spectrum beta-lactamase activities
-
-
?
additional information
?
-
enzyme displays both D,D-carboxypeptidase and expanded-spectrum beta-lactamase activities
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
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D344S
-
the mutant shows highly reduced activity compared to the wild-type
D59A
-
73% decrease in ratio kcat/KM for D-Ala-D-Ala substrate, EC3.4.13.B1 activity
D59S
-
strong increase in ratio kcat/KM for EC 3.4.17.8 activity, 50% increase in ratio kcat/KM for D-Ala-D-Ala substrate, EC3.4.13.B1 activity
D59A
-
73% decrease in ratio kcat/KM for D-Ala-D-Ala substrate, EC3.4.13.B1 activity
-
D59S
-
strong increase in ratio kcat/KM for EC 3.4.17.8 activity, 50% increase in ratio kcat/KM for D-Ala-D-Ala substrate, EC3.4.13.B1 activity
-
K172N/R173N
-
site-directed mutagenesis, M1 mutant, the mutant enzyme shows altered complementation of the pbp3-deficient mutant strain SL2 compared to the wild-type enzyme, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1, overview
K199Q
-
site-directed mutagenesis, M5 mutant, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1
K199Q/K203Q
-
site-directed mutagenesis, M2 mutant, the mutant enzyme shows altered complementation of the pbp3-deficient mutant strain SL2 compared to the wild-type enzyme, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1, overview
K203Q
-
site-directed mutagenesis, M3 mutant, the mutant enzyme shows altered complementation of the pbp3-deficient mutant strain SL2 compared to the wild-type enzyme, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1, overview
R173N
-
site-directed mutagenesis, M4 mutant, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1
S422A
-
site-directed mutagenesis, M6 mutant, inactive mutant
C115S
-
site-directed mutagenesis, truncated mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme
K213C/C115S
-
site-directed mutagenesis, truncated double mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme
K47C/C115S
-
site-directed mutagenesis, truncated double mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme
additional information
-
construction of spontaneous mutants M512, M9, and G9 from mutant D344S with reduced enzyme activity, but less as for the parental mutant D344S, overview
additional information
-
construction of a PBP5-deletion mutant which shows high levels of muramoylpentapeptide, an additional mutation of amiC, encoding muramyl-L-alanine amidase C, leads to long chains of unseparated cells to a higher percentage than with an amiC mutation alone, twisted cell chains appear only when the PBP 5 gene, dacA, is deleted in concert with mutations of amiA and amiC, overview
additional information
-
construction of mutant strains lacking PBP5, strain AV-21-10, or PBP5 and PBP7, strain AV23-1, inhibition of FtsZ and MreB simultaneously in strain AV 23-1results in cells balloon outward but retain conspicuous rod-shaped extensions at sites representing the original poles, phenotypes, overview
additional information
-
exchange of active site residues Lys47 and Lys213 for gamma-thialysine, pH-dependency, kinetics, and activity compared to the wild-type enzyme
additional information
-
construction of mutant strains lacking PBP5, strain AV-21-10, or PBP5 and PBP7, strain AV23-1, inhibition of FtsZ and MreB simultaneously in strain AV 23-1results in cells balloon outward but retain conspicuous rod-shaped extensions at sites representing the original poles, phenotypes, overview
-
additional information
-
expression of mecA, encoding a penicillin-binding protein, in Staphylocccus aureus confers resistance to beta-lactam and leads to increased growth and cell wall synthesis in presence of high concentratin of antibiotic methicillin, the cell wall synthesized is typical for Staphylcoccus aureus and uses the endogenous precursors, but is eventhough completely dependent on the recombinant enzyme from Staphylcoccus sciuri, overview
additional information
expression of recombinant protein as soluble version by deletion of its C-terminal membrane anchor. Under in vitro conditions, the soluble enzyme demonstrates both D,D-carboxypeptidase and expanded-spectrum beta-lactamase activities
additional information
-
expression of recombinant protein as soluble version by deletion of its C-terminal membrane anchor. Under in vitro conditions, the soluble enzyme demonstrates both D,D-carboxypeptidase and expanded-spectrum beta-lactamase activities
-
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Joris, B.; van Beeumen, J.; Casagrande, F.; Gerday, C.; Frere, J.M.; Ghuysen, J.M.
The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G
Eur. J. Biochem.
130
53-69
1983
Streptomyces albus
brenda
Dideberg, O.; Charlier, P.; Dive, G.; Joris, B.; Frere, J.M.; Ghuysen, J.M.
Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution
Nature
299
469-470
1982
Streptomyces albus
brenda
Dideberg, O.; Joris, B.; Frere, J.M.; Ghuysen, J.M.; Weber, G.; Robaye, R.; Delbrouck, J.M.; Roelandts, I.
The exocellular DD-carboxypeptidase of Streptomyces albus G: a metallo (Zn2+) enzyme
FEBS Lett.
117
215-218
1980
Streptomyces albus
brenda
DeCoen, J.L.; Lamotte-Brasseur, J.; Ghuysen, J.M.; Frere, J.M.; Perkins, H.R.
Conformational analysis of peptide substrates and inhibitors of the Zn2+ G and serine R61 D-alanyl-D-alanine peptidases
Eur. J. Biochem.
121
221-232
1981
Streptomyces albus
brenda
Kimura, Y.; Takashima, Y.; Tokumasu, Y.; Sato, M.
Molecular cloning, sequence analysis, and characterization of a penicillin-resistant DD-carboxypeptidase of Myxococcus xanthus
J. Bacteriol.
181
4696-4699
1999
Myxococcus xanthus
brenda
Kelly, J.A.; Kuzin, A.P.
The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 A resolution
J. Mol. Biol.
254
223-236
1995
Streptomyces sp., Streptomyces albus
brenda
Labischinski, H.; Giesbrecht, P.; Fischer, E.; Barnickel, G.; Bradaczeck, H.; Frere, J.M.; Houssier, C.; Charlier, P.; Dideberg, O.; Ghuysen, J.M.
Study of the Zn-containing DD-carboxypeptidase of Streptomyces albus G by small-angle X-ray scattering in solution
Eur. J. Biochem.
138
83-87
1984
Streptomyces albus
brenda
Dideberg, O.; Charlier, P.; Dupont, L.; Vermeire, M.; Frere, J.M.; Ghuysen, J.M.
The 4.5 A resolution structure analysis of the exocellular DD-carboxypeptidase of Streptomyces albus G
FEBS Lett.
117
212-214
1980
Streptomyces albus
brenda
Ghuysen, J.M.; Leyh-Bouille, M.; Bonaly, R.; Nieto, M.; Perkins, H.R.; Schleifer, K.H.; Kandler, O.
Isolation of DD carboxypeptidase from Streptomyces albus G culture filtrates
Biochemistry
9
2955-2960
1970
Streptomyces albus
brenda
Leyh-Bouille, M.; Ghuysen, J.M.; Nieto, M.; Perkins, H.R.; Schleifer, K.H.; Kandler, O.
On the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, vancomycin, and ristocetin
Biochemistry
9
2971-2975
1970
Streptomyces albus
brenda
Nieto, M.; Perkins, H.R.; Leyh-Bouille, M.; Frere, J.M.; Ghuysen, J.M.
Peptide inhibitors of Streptomyces DD-carboxypeptidases
Biochem. J.
131
163-171
1973
Streptomyces albus
brenda
Umbreit, J.N.; Strominger, J.L.
D-Alanine carboxypeptidase from Bacillus subtilis membranes. I. Purification and characterization
J. Biol. Chem.
248
6759-6766
1973
Bacillus subtilis
brenda
Diaz-Maurino, T.; Nieto, M.; Perkins, H.R.
Membrane-bound DD-carboxypeptidases from Bacillus megaterium KM
Biochem. J.
134
391-402
1974
Priestia megaterium, Priestia megaterium KM / ATCC 13632
-
brenda
Podmore, A.H.B.; Reynolds, P.E.
Purification and characterization of VanXYc, a D,D-dipeptidase/D,D-carboxypeptidase in vancomycin-resisitant Enterococcus gallinarium BM4174
Eur. J. Biochem.
269
2740-2746
2002
Enterococcus gallinarum, Enterococcus gallinarum BM4174
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
Adediran, S.A.; Kumar, I.; Pratt, R.F.
Deacylation transition states of a bacterial DD-peptidase
Biochemistry
45
13074-13082
2006
Streptomyces sp.
brenda
Josephine, H.R.; Charlier, P.; Davies, C.; Nicholas, R.A.; Pratt, R.F.
Reactivity of penicillin-binding proteins with peptidoglycan-mimetic beta-lactams: whats wrong with these enzymes?
Biochemistry
45
15873-15883
2006
Escherichia coli
brenda
Zhang, W.; Shi, Q.; Meroueh, S.O.; Vakulenko, S.B.; Mobashery, S.
Catalytic mechanism of penicillin-binding protein 5 of Escherichia coli
Biochemistry
46
10113-10121
2007
Escherichia coli
brenda
Leimanis, S.; Hoyez, N.; Hubert, S.; Laschet, M.; Sauvage, E.; Brasseur, R.; Coyette, J.
PBP5 complementation of a PBP3 deficiency in Enterococcus hirae
J. Bacteriol.
188
6298-6307
2006
Enterococcus faecium, Enterococcus hirae
brenda
Priyadarshini, R.; de Pedro, M.A.; Young, K.D.
Role of peptidoglycan amidases in the development and morphology of the division septum in Escherichia coli
J. Bacteriol.
189
5334-5347
2007
Escherichia coli
brenda
Varma, A.; de Pedro, M.A.; Young, K.D.
FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli
J. Bacteriol.
189
5692-5704
2007
Escherichia coli, Escherichia coli MG1655
brenda
Cremniter, J.; Mainardi, J.; Josseaume, N.; Quincampoix, J.; Dubost, L.; Hugonnet, J.; Marie, A.; Gutmann, L.; Rice, L.B.; Arthur, M.
Novel mechanism of resistance to glycopeptide antibiotics in Enterococcus faecium
J. Biol. Chem.
281
32254-32262
2006
Enterococcus faecium
brenda
Smith, J.D.; Kumarasiri, M.; Zhang, W.; Hesek, D.; Lee, M.; Toth, M.; Vakulenko, S.; Fisher, J.F.; Mobashery, S.; Chen, Y.
Structural analysis of the role of Pseudomonas aeruginosa penicillin-binding protein 5 in beta-lactam resistance
Antimicrob. Agents Chemother.
57
3137-3146
2013
Pseudomonas aeruginosa (G3XD74), Pseudomonas aeruginosa ATCC 15692 (G3XD74)
brenda
Montealegre, M.C.; Roh, J.H.; Rae, M.; Davlieva, M.G.; Singh, K.V.; Shamoo, Y.; Murray, B.E.
Differential penicillin-binding protein 5 (PBP5) levels in the Enterococcus faecium clades with different levels of ampicillin resistance
Antimicrob. Agents Chemother.
61
e02034
2017
Enterococcus faecium (A0A075Q0W3)
brenda
Maryam Pourhajibaghe, M.P.; Yazdi, M.; Bahador, A.
In silico analysis of penicillin-binding protein 5 as an inhibitory target of beta-lactam antibiotics in Enterococcus faecalis
Der Pharma Chem.
7
301-306
2015
Enterococcus faecalis (Q47800)
-
brenda
Pandey, S.; Pal, S.; N, G.; Bansal, A.; Mallick, S.; Ghosh, A.
Two DD-carboxypeptidases from Mycobacterium smegmatis affect cell surface properties through regulation of peptidoglycan cross-linking and glycopeptidolipids
J. Bacteriol.
200
e00760
2018
Mycolicibacterium smegmatis (A0QV34), Mycolicibacterium smegmatis (A0QV35), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0QV34), Mycolicibacterium smegmatis ATCC 700084 (A0QV35)
brenda
Belhaj, M.; Boutiba-Ben Boubaker, I.; Slim, A.
Penicillin-binding protein 5 sequence alteration and levels of plp5 mRNA expression in clinical isolates of Enterococcus faecium with different levels of ampicillin resistance
Microb. Drug Resist.
22
202-210
2016
Enterococcus faecium (A0A075Q0W3)
brenda