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Information on EC 3.4.16.4 - serine-type D-Ala-D-Ala carboxypeptidase and Organism(s) Escherichia coli and UniProt Accession P0AEB2
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3.4.16.4 serine-type D-Ala-D-Ala carboxypeptidaseSpecify your search results
Word Map
- 3.4.16.4
- beta-lactams
- peptidoglycan
- staphylococcus
- aureus
- streptococcus
- pneumonia
-
methicillin-resistant
- cephalosporin
- gg
- methicillin
-
penicillin-resistant
- ampicillin
- bilirubin
-
sortase
-
gamma-glutamyl
- vancomycin
- cefotaxime
- oxacillin
-
transpeptidation
-
pneumococci
- faecium
- ceftriaxone
- carbapenems
- transglycosylase
- imipenem
-
penicillin-susceptible
- ceftazidime
- murein
-
methicillin-susceptible
- benzylpenicillin
- meropenem
- cefoxitin
- acyl-enzyme
- muropeptides
-
mic90s
- cefixime
-
cephems
- piperacillin
-
ampicillin-resistant
-
lpxtg
- cefuroxime
- penicillinase
- aztreonam
-
vancomycin-resistant
- cefaclor
-
beta-lactamase-negative
- synthesis
-
sccmec
-
beta-lactamase-producing
- nitrocefin
- sulbactam
- medicine
- analysis
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
Synonyms
transpeptidase, penicillin-binding protein, pbp2x, pbp1a, pbp1b, penicillin binding proteins, pbp 2, pbp 3, pbp 5, dd-peptidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxypeptidase I
-
-
-
-
CPase
-
-
-
-
D-alanine carboxypeptidase
D-alanine carboxypeptidase I
-
-
-
-
D-alanyl carboxypeptidase
-
-
-
-
D-alanyl-D-alanine carboxypeptidase
-
-
-
-
D-Alanyl-D-alanine hydrolase
-
-
-
-
D-alanyl-D-alanine peptidase
-
-
-
-
D-alanyl-D-alanine-carboxypeptidase
-
-
-
-
D-alanyl-D-alanine-cleaving peptidase
-
-
-
-
D-alanyl-D-alanine-cleaving-peptidase
-
-
-
-
DD-Carboxypeptidase
DD-CPase
DD-peptidase
DD-transpeptidase
-
-
-
-
PBP 5
PBP 6
-
the DD-carboxypeptidase activity of PBP 6 is lower than that of PBP 5
PBP-5*
-
-
-
-
PBP-6B
-
-
-
-
PBP4
PBP5
penicillin binding protein 5
penicillin-binding protein 5
VanX
VanY
-
-
-
-
D-alanine carboxypeptidase
-
-
-
-
DD-Carboxypeptidase
-
-
-
-
DD-peptidase
-
-
-
-
PBP 5
-
the DD-carboxypeptidase activity of PBP 5 is higher than that of PBP 6
PBP5
-
-
-
-
penicillin binding protein 5
-
-
-
-
VanX
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY
9077-67-2
-
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
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O
?
-
only substrate of penicillin-binding protein 5, but not of penicillin-binding protein 6
-
-
?
N-(N-acetyl-1-O-methyl-beta-muramoyl)-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine + H2O
N-(N-acetyl-1-O-methyl-beta-muramoyl)-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanine + D-Ala
-
-
-
?
N-[N-acetyl-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-1-O-methyl-beta-muramoyl]-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine + H2O
N-[N-acetyl-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-1-O-methyl-beta-muramoyl]-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanine + D-Ala
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
N,N'-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-alanine
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-Lys-D-Ala + D-Ala
-
-
-
?
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala + D-Ala
-
-
-
?
additional information
?
-
-
forms a covalent acyl-enzyme complex with beta-lactam antibiotics, high rate of decylation of the acyl-enzyme complex. Direct role for the SXN motif in deacylation of the acyl-enzyme complex. Functioning of this motif is modulated by the 74-90 loop. Ser86 and Ser87 are important for D-alanine carboxypeptidase activity
-
?
additional information
?
-
-
the enzyme forms a covalent acyl-enzyme complex with beta-lactam antibiotics
-
?
additional information
?
-
-
enzyme removes the terminal D-alanine from the pentapeptide side chains of muramic acid in peptidoglycan
-
-
?
additional information
additional information
-
-
the glycosyl transferase of PBP1b catalyzes the assembly of lipid-transported N-acetylglucosaminyl-beta-1,4-N-acetylmuramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala-D-Ala units
linear peptidoglycan chains
-
?
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
additional information
?
-
-
enzyme removes the terminal D-alanine from the pentapeptide side chains of muramic acid in peptidoglycan
-
-
?
additional information
additional information
-
-
the glycosyl transferase of PBP1b catalyzes the assembly of lipid-transported N-acetylglucosaminyl-beta-1,4-N-acetylmuramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala-D-Ala units
linear peptidoglycan chains
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-beta(N-acetyl-L-alanyl-gamma-D-glutamyl-L-alanyl)-aminopenicillanic acid
-
-
Boc-gamma-D-Glu-L-Lys-(Cbz)-D-boroAla-(-)-pinanediol
effective inhibitor of the D-alanine CPase activity of PBP5
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala-D-Ala
-
substrate inhibition above 30 mM
Vancomycin
-
vancomycin derivatives inhibit the glycosyl transferase activity
additional information
-
no significant inhibition by arylakylidene imino-thiazolidin-4-ones 7, 14 and 15 respectively
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.38
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala
-
recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C
3.5
N-(N-acetyl-1-O-methyl-beta-muramoyl)-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.5, 25°C
3.7
N-[N-acetyl-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-1-O-methyl-beta-muramoyl]-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.5, 25°C
additional information
additional information
-
the ratio of turnover number to Km-value for the substrate Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala is 32/M*s for the wild-type enzyme, 3.9/M*s for the S86A mutant, 2.0/M*s for the S87A mutant and 2.6/M*s for the S86A/S87A mutant enzyme
-
1.28
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
recombinant PBP 6, in 50 mM Tris-HCl, pH 8.5, at 37°C
8.98
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.41
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala
-
recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C
0.9
N-(N-acetyl-1-O-methyl-beta-muramoyl)-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.5, 25°C
1.1
N-[N-acetyl-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-1-O-methyl-beta-muramoyl]-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.5, 25°C
additional information
additional information
-
the ratio of turnover number to Km-value for the substrate Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala is 32/M*s for the wild-type enzyme, 3.9/M*s for the S86A mutant, 2.0/M*s for the S87A mutant and 2.6/M*s for the S86A/S87A mutant enzyme
-
0.56
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
recombinant PBP 6, in 50 mM Tris-HCl, pH 8.5, at 37°C
2.7
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 11
-
pH 8: about 50% of maximal activity, pH 11: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
anchored into the outer leaflet of the cytoplasmic membrane
-
additional information
-
in minimal-medium-grown cells, wild-type PBP5 localizes laterally and at the midcell. Isoform PBP6a localization is lateral and intense at the midcell. PBP6b localizes poorly at the midcell and mainly at the lateral sides
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
loss of penicillin-binding protein 5 enhances beta-lactam susceptibility, the observed susceptibilities for ampicillin, piperacillin, amoxicillin, penicillin G, cefadroxil and cefalexin are enhanced by 4fold and for cefalothin and cefaclor the susceptibilities are at least 8fold higher in the mutants
physiological function
physiological function
-
the DD-carboxypeptidase activity of PBP 5 is responsible for maintaining cell shape
physiological function
-
D,D-CPases PBP5, PBP6a, and PBP6b change dimer conformation between resting and active states. The isoforms are not redundant but that their balanced activity is required for robust peptidoglycan synthesis
physiological function
-
in an isoform DacC deletion mutant, the extracellular activities and fluorescence value of recombinant amylase, green fluorescent protein, and alpha-galactosidase are increased by 82.3, 29.1, and 37.7%, respectively, compared with that of control cells. The outer membrane permeability and intracellular soluble peptidoglycan accumulation of the deletion mutant are also enhanced. In the poles of the deletion mutant, local transparent bulges are found
physiological function
-
overexpression of D,D-carboxypeptidase DacA or DacB promotes the accumulation of intracellular soluble peptidoglycan, alters cell morphology (shape and size) and leads to the formation of transparent globular structures in Escherichia coli cells. Extracellular production of recombinant green fluorescent protein is increased by 1.7- and 2.3fold upon overexpression of DacA and DacB, respectively. Extracellular production of recombinant amylase and apha-galactosidase is increased by 4.5- and 2.8fold, respectively, upon overexpression of DacA, and by 11.9- and 2.5fold, respectively, upon overexpression of DacB. Overexpression of DacA or DacB enhances both the outer and inner membrane permeability of Escherichia coli
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 1.6 A resolution of PBP5 in complex with a substrate-like peptide boronic acid, suggesting a hydrogen-bonding network, involving Lys-213, Ser-110, and a bridging water molecule, to polarize the hydrolytic water molecule
three dimensional structure of the G105D mutant enzyme at 2.3 A resolution
-
vapor diffusion hanging drop technique. Three-dimensional structure of a soluble form of wild-type enzyme at 1.85 A resolution and structure of the G105D mutant form at 1.9 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA74-90
-
deletion of the 74-90 loop markedly diminishes the deacylation rate of penicillin G with a minimal impact on acylation, and abolishes D-alanine carboxypeptidase activity
G105D
S44G
-
active site mutant, isoform PBP5, inactive, mutation changes the conformation of the dimeric state. Contrary to wild-type, the mutant only localized laterally in the cell
S63G
-
active site mutant, isoform PBP6b, inactive, mutation changes the conformation of the dimeric state
S66G
-
active site mutant, isoform PBP6a, inactive, mutation changes the conformation of the dimeric state. Contrary to wild-type, the mutant mostly avoids midcell localization
S86A
-
mutation has little effect on the interaction of the protein with penicillin G, acylation rate constants are nearly identical to wild-type enzyme. The ratio of turnover number to Km-value for the substrate N,N-diacetyl-L-Lys-D-Ala-D-Ala is 12% of the wild-type ratio
S86A/S87A
-
mutation has little effect on the interaction of the protein with penicillin G, acylation rate constants are nearly identical to wild-type enzyme. The ratio of turnover number to Km-value for the substrate N,N-diacetyl-L-Lys-D-Ala-D-Ala is 8.1% of the wild-type ratio
S87A
-
mutation has little effect on the interaction of the protein with penicillin G, acylation rate constants are nearly identical to wild-type enzyme. The ratio of turnover number to Km-value for the substrate N,N-diacetyl-L-Lys-D-Ala-D-Ala is 6.3% of the wild-type ratio
additional information
G105D
-
mutation markedly impairs deacylation with only minor effects on acylation, and abolishes D-alanine carboxypeptidase activity
G105D
-
mutation markedly impairs the beta-lactamase activity, with only minor effects on acylation, and promotes accumulation of a covalent complex with peptide substrates
additional information
-
PBP5 mutants produce cells with higher levels of pentapeptides, amidase C mutants produce higher percentage of cells in chains as compared to amidase A mutants and amidase B mutants, lack of PBP5 increases chaining of amidase mutants, reinserting of wild-type PBP5 in amidase mutants exhibits decreased chaining, amidase A mutants and amidase C mutants with lack of PBP5 produce twisted chains, additional deletion of amiB revealed extraordinarily long, convoluted and twisted chains, thus contributing to this phenotype
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
49
-
melting temperature (Tm), reversible denaturation in a two-state manner. The binding of beta-lactam antibiotics cefoxitin, cloxacillin, moxalactam, and imipenem all stabilize the enzyme significantly with DELTATm values as high as 4.6°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the binding of beta-lactam antibiotics cefoxitin, cloxacillin, moxalactam, and imipenem all stabilize the enzyme significantly with an increase in melting temperature of up to 4.6°C
-
without stabilization dilution of the enzyme to 10 nM results in a 97% loss of activity, whereas with stabilization by bovine serum albumin less than 10% loss of activity is observed
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using an amylose affinity column, the MBP-tag is removed by factor Xa cleavage
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
membrane anchor of the protein is removed and the enzyme is obtained as a soluble protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
Forster resonance energy transfer assay that uses the fluorescent-protein donor-acceptor pair mNeonGreen-mCherry to detect periplasmic protein interactions in fixed and in living bacteria, in single samples or in plate reader 96-well format
medicine
medicine
-
bacterial DD-peptidases are still an enticing target for antibacterial agents
medicine
-
VanX, being a required enzyme for bacterial antibiotic resistance, should be a key target in circumventing clinical vancomycin resistance
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Van der Linden, M.P.G.; Mottl, H.; Keck, W.
Cytoplasmic high-level expression of a soluble, enzymatically active form of the Escherichia coli penicillin-binding protein 5 and purification by dye chromatography
Eur. J. Biochem.
204
197-202
1992
Streptomyces sp., Escherichia coli, Streptomyces sp. R39
Stefanova, M.E.; Davies, C.; Nicholas, R.A.; Gutheil, W.G.
pH, inhibitor, and substrate specificity studies on Escherichia coli penicillin-binding protein 5
Biochim. Biophys. Acta
1597
292-300
2002
Escherichia coli
Davies, C.; White, S.W.; Nicholas, R.A.
Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolution
J. Biol. Chem.
276
616-623
2001
Escherichia coli
Nicholas, R.A.; Krings, S.; Tomberg, J.; Nicola, G.; Davies, C.
Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: implications for deacylation of the acyl-enzyme complex
J. Biol. Chem.
278
52826-52833
2003
Escherichia coli
Hesek, D.; Suvorov, M.; Morio, K.; Lee, M.; Brown, S.; Vakulenko, S.B.; Mobashery, S.
Synthetic peptidoglycan substrates for penicillin-binding protein 5 of Gram-negative bacteria
J. Org. Chem.
69
778-784
2004
Escherichia coli
Beadle, B.M.; Nicholas, R.A.; Shoichet, B.K.
Interaction energies between beta-lactam antibiotics and E. coli penicillin-binding protein 5 by reversible thermal denaturation
Protein Sci.
10
1254-1259
2001
Escherichia coli
Zervosen, A.; Lu, W.P.; Chen, Z.; White, R.E.; Demuth Jr., T.P.; Frre, J.M.
Interactions between penicillin-binding proteins (PBPs) and two novel classes of PBP inhibitors, arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones
Antimicrob. Agents Chemother.
48
961-969
2004
Actinomadura sp., Escherichia coli, Streptomyces sp. R61
Nicola, G.; Peddi, S.; Stefanova, M.; Nicholas, R.A.; Gutheil, W.G.; Davies, C.
Crystal structure of Escherichia coli penicillin-binding protein 5 bound to a tripeptide boronic acid inhibitor: A role for Ser-110 in deacylation
Biochemistry
44
8207-8217
2005
Escherichia coli (P0AEB2), Escherichia coli
Priyadarshini, R.; Popham, D.L.; Young, K.D.
Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli
J. Bacteriol.
188
5345-5355
2006
Escherichia coli
Sauvage, E.; Herman, R.; Petrella, S.; Duez, C.; Bouillenne, F.; Frre, J.M.; Charlier, P.
Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins
J. Biol. Chem.
280
31249-31256
2005
Actinomadura sp., Escherichia coli
Fraipont, C.; Sapunaric, F.; Zervosen, A.; Auger, G.; Devreese, B.; Lioux, T.; Blanot, D.; Mengin-Lecreulx, D.; Herdewijn, P.; van Beeumen, J.; Frere, J.M.; Nguyen-Disteche, M.
Glycosyl transferase activity of the Escherichia coli penicillin-binding protein 1b: specificity profile for the substrate
Biochemistry
45
4007-4013
2006
Escherichia coli
Chang, Y.P.; Tseng, M.J.; Chu, Y.H.
Using surface plasmon resonance to directly measure slow binding of low-molecular mass inhibitors to a VanX chip
Anal. Biochem.
359
63-71
2006
Escherichia coli
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
Streptococcus pneumoniae, Escherichia coli, Streptomyces sp. R61, Actinomadura sp. R39
Pratt, R.F.
Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins)
Cell. Mol. Life Sci.
65
2138-2155
2008
Bacillus subtilis, Caulobacter vibrioides, Streptomyces sp., Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Staphylococcus aureus, Neisseria gonorrhoeae, Streptomyces sp. R61, Streptomyces sp. K15
Shi, Q.; Meroueh, S.O.; Fisher, J.F.; Mobashery, S.
Investigation of the mechanism of the cell wall DD-carboxypeptidase reaction of penicillin-binding protein 5 of Escherichia coli by quantum mechanics/molecular mechanics calculations
J. Am. Chem. Soc.
130
9293-9303
2008
Escherichia coli (P0AEB2), Escherichia coli
Ghosh, A.S.; Chowdhury, C.; Nelson, D.E.
Physiological functions of D-alanine carboxypeptidases in Escherichia coli
Trends Microbiol.
16
309-317
2008
Escherichia coli (P0AEB2)
Chowdhury, C.; Nayak, T.R.; Young, K.D.; Ghosh, A.S.
A weak DD-carboxypeptidase activity explains the inability of PBP 6 to substitute for PBP 5 in maintaining normal cell shape in Escherichia coli
FEMS Microbiol. Lett.
303
76-83
2010
Escherichia coli
Sarkar, S.K.; Chowdhury, C.; Ghosh, A.S.
Deletion of penicillin-binding protein 5 (PBP5) sensitises Escherichia coli cells to beta-lactam agents
Int. J. Antimicrob. Agents
35
244-249
2010
Escherichia coli
Daniel, P.I.; Zajicek, J.; Zhang, W.; Shi, Q.; Fisher, J.F.; Mobashery, S.
Elucidation of the structure of the membrane anchor of penicillin-binding protein 5 of Escherichia coli
J. Am. Chem. Soc.
132
4110-4118
2010
Escherichia coli
Yang, H.; Hu, J.; Lu, X.; Wang, F.; Shen, W.; Hu, W.; Wang, L.; Chen, X.; Liu, L.
Improving extracellular protein production in Escherichia coli by overexpressing D,D-carboxypeptidase to perturb peptidoglycan network synthesis and structure
Appl. Microbiol. Biotechnol.
103
793-806
2019
Escherichia coli
Hu, J.; Lu, X.; Wang, H.; Wang, F.; Zhao, Y.; Shen, W.; Yang, H.; Chen, X.
Enhancing extracellular protein production in Escherichia coli by deleting the D-alanyl-D-alanine carboxypeptidase gene dacC
Eng. Life Sci.
19
270-278
2019
Escherichia coli
-
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