Information on EC 3.4.17.8 - muramoylpentapeptide carboxypeptidase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
3.4.17.8
-
RECOMMENDED NAME
GeneOntology No.
muramoylpentapeptide carboxypeptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-/-D-alanine
show the reaction diagram
-
-
-
-
cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-/-D-alanine
show the reaction diagram
catalytic mechanism and transition state intermediates
-
cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-/-D-alanine
show the reaction diagram
catalytic mechanism involving active site residues Lys47 and Lys213, Lys47 exists in the free-base form for catalysis, Lys213 serves as an electrostatic anchor for the substrate
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxypeptidase D-alanyl-D-alanine
-
-
-
-
carboxypeptidase I
-
-
-
-
carboxypeptidase, muramoylpentapeptide
-
-
-
-
D-alanine carboxypeptidase
-
-
-
-
D-alanine carboxypeptidase I
-
-
-
-
D-alanine-D-alanine-carboxypeptidase
-
-
-
-
D-alanyl-D-alanine carboxypeptidase
-
-
-
-
D-alanyl-D-alanine peptidase
-
-
-
-
DD-Carboxypeptidase
-
-
-
-
DD-Carboxypeptidase
-
-
DD-Carboxypeptidase
-
-
DD-peptidase
-
-
-
-
DD-peptidase
-
-
DD-peptidase
-
-
EC 3.4.12.6
-
-
formerly
-
Metallo DD-peptidase
-
-
-
-
PdcA
-
-
-
-
penicillin binding protein 5
-
-
-
-
penicillin-binding protein 5
-
-
penicillin-binding protein 5
-
-
UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase
-
-
-
-
VanX
-
-
-
-
VanXYc
Enterococcus gallinarum BM4174
-
-
-
VanY
-
-
-
-
Zn DD-peptidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9077-67-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Bacillus megaterium KM
KM
-
-
Manually annotated by BRENDA team
Enterococcus faecium BM4147
BM4147
-
-
Manually annotated by BRENDA team
strain BM4174, bifunctional enzyme with activities of EC 3.4.17.8 and 3.4.13.B1
-
-
Manually annotated by BRENDA team
Enterococcus gallinarum BM4174
strain BM4174, bifunctional enzyme with activities of EC 3.4.17.8 and 3.4.13.B1
-
-
Manually annotated by BRENDA team
wild-type strain ATCC 9790, gene pbp5
-
-
Manually annotated by BRENDA team
gene dacA
-
-
Manually annotated by BRENDA team
gene pbp5
-
-
Manually annotated by BRENDA team
strain MG1655
-
-
Manually annotated by BRENDA team
Escherichia coli MG1655
strain MG1655
-
-
Manually annotated by BRENDA team
strain ATCC 29062 and other strains, e.g. strain SS1 and SS2, overview
-
-
Manually annotated by BRENDA team
strain R61
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-[(ammonioacetyl)amino]-3-[[3-([2-[(1-carboxylatoethyl)amino]-1-methyl-2-oxoethyl]amino)-3-oxopropyl]sulfanyl]propanoate + H2O
?
show the reaction diagram
-
-
-
-
?
2-[(ammonioacetyl)amino]-3-[[3-([2-[(1-carboxylatoethyl)sulfanyl]-1-methyl-2-oxoethyl]amino)-3-oxopropyl]sulfanyl]propanoate + H2O
?
show the reaction diagram
-
-
-
-
?
2-[(ammonioacetyl)amino]-7-([2-[(1-carboxylatoethyl)amino]-1-methyl-2-oxoethyl]amino)-7-oxoheptanoate + H2O
?
show the reaction diagram
-
-
-
-
?
2-[[N-(phenylacetyl)alanyl]sulfanyl]propanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
3-[[N-(phenylacetyl)alanyl]oxy]benzoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
3-[[N-(phenylacetyl)glycyl]oxy]benzoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Gly-D-Ala-D-Ala + H2O
acetyl-Gly-D-Ala + D-Ala
show the reaction diagram
-
-
-
-
?
acetyl-L-Ala-D-Ala-D-Ala + H2O
acetyl-L-Ala-D-Ala + D-Ala
show the reaction diagram
-
-
-
-
?
D-Ala-D-Ala + H2O
D-Ala + D-Ala + H2O
show the reaction diagram
-
-
-
?
D-Ala-D-Ala + H2O
D-Ala + D-Ala + H2O
show the reaction diagram
-
-
-
?
D-Ala-D-Ala + H2O
D-Ala + D-Ala + H2O
show the reaction diagram
Enterococcus faecium BM4147
-
-
-
?
D-Ala-D-Ala + H2O
D-Ala + D-Ala + H2O
show the reaction diagram
Enterococcus faecium BM4147
-
-
-
?
diacetyl-L-diaminobutyryl-D-Ala-D-Ala + H2O
diacetyl-L-diaminobutyryl-D-Ala + D-Ala
show the reaction diagram
-
-
-
-
?
diacetyl-L-Lys-D-Ala-D-Ala + H2O
diacetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
-
?
muramoylpentapeptide + H2O
muramoyltetrapeptide + D-Ala
show the reaction diagram
-
-
-
-
?
N,N'-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
N,N'-diacetyl-L-lysyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
-
?
Nalpha, Nepsilon-diacetyl L-Lys-D-Ala-Gly + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + Gly
show the reaction diagram
Bacillus megaterium, Bacillus megaterium KM
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
Bacillus megaterium KM
-
-
-
-
?
penicillin + H2O
penicilloate
show the reaction diagram
-
very slow hydrolysis
-
?
UDP-MurNAc-pentapeptide + H2O
UDP-MurNAc-tetrapeptide + D-Ala
show the reaction diagram
-
i.e. UDP-acetylmuramic acid-L-Ala-D-iGlu-L-Lys-D-Ala-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
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
Bacillus megaterium KM
-
-
-
-
-
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
show the reaction diagram
Enterococcus gallinarum, Enterococcus gallinarum BM4174
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
Bacillus megaterium KM
-
-
-
-
?
L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala + H2O
L-Ala-D-gamma-Glu-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
D,D-carboxypeptidase activity of penicillin-binding proteins
-
-
?
additional information
?
-
-
influence of residue preceeding C-terminal D-Ala-D-Ala on rate of hydrolysis
-
-
-
additional information
?
-
-
substrate specificity, 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
?
-
-
no substrate: UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-serine
-
-
-
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
?
-
-
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
?
-
Enterococcus gallinarum BM4174
-
no substrate: UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-serine
-
-
-
additional information
?
-
Escherichia coli MG1655
-
the enzyme is involved in cell wall formation, overview
-
-
-
additional information
?
-
Bacillus megaterium KM
-
influence of residue preceeding C-terminal D-Ala-D-Ala on rate of hydrolysis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-MurNAc-pentapeptide + H2O
UDP-MurNAc-tetrapeptide + D-Ala
show the reaction diagram
-
i.e. UDP-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
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
Bacillus megaterium KM
-
-
-
-
-
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
?
-
-
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
?
-
-
PBP5 performs a DD-carboxypeptidase reaction on the bacterial peptidoglycan, the major constituent of the cell wall
-
-
-
additional information
?
-
Escherichia coli, Escherichia coli MG1655
-
the enzyme is involved in cell wall formation, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activation
Ca2+
-
activation
Co2+
-
activation
Co2+
-
activation
Co2+
-
activation
Fe2+
-
activation
Mg2+
-
activation
Mg2+
-
activation
Ni2+
-
activation
Zn2+
-
metalloenzyme, 1 gatom per mol of enzyme
Zn2+
-
activation
Zn2+
-
activation
Zn2+
-
activation
Mn2+
-
activation
additional information
-
no metalloenzyme
additional information
-
no metalloenzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(5R,6R)-6-[(7-ammonio-7-carboxylatoheptanoyl)amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylate
-
-
3-[(1-aminoethyl)phosphinyl]-2-methyl-propionic acid I
-
kinetic analysis of phosphinate I, II and III
5,5'-dithiobis(2-nitrobenzoate)
-
-
6-beta(D-alpha-aminopimelyl)-aminopenicillanic acid
-
-
6-beta(N-acetyl-L-alanyl-gamma-D-glutamyl-L-alanyl)-aminopenicillanic acid
-
-
7-beta(D-alpha-aminopimelyl)-aminocephalosporanic acid
-
-
Acetyl-D-Ala-D-Glu
-
-
acetyl-Gly-D-Ala-D-Glu
-
-
acetyl-Gly3-D-Ala-D-Asp
-
-
alpha,epsilon-disuccinyl-L-Lys-D-Ala-D-Glu
-
-
-
Ampicillin
-
inhibits the D,D-carboxypeptidase activity of penicillin-binding proteins
benzylpenicillin
-
-
carbenicillin
-
-
Cephalothin
-
-
D-Ala-D-Ser
-
30% inhibition
D-alpha-phenylpropionate
-
-
D-hexahydromandelate
-
-
D-mandelate
-
-
D-Phenyllactate
-
-
Diacetyl-L-Lys-D-Ala-L-Ala
-
-
Diacetyl-L-Lys-l-Ala-D-Ala
-
-
glycolyl-L-Phe
-
-
iodoacetic acid
-
-
p-chloromercuribenzene sulfonic acid
-
-
p-Iodo-7-beta-phenyl-acetylaminocephalosporamic acid
-
-
-
succinyl-D-Ala-D-cycloserine
-
-
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-serine
-
30% inhibition
additional information
-
no inhibition by EDTA
-
additional information
-
no inhibition by PMSF, E-64, pepstatin, o-phenanthroline, EDTA and DTT
-
additional information
-
synthesis and inhibitory potency of beta-lactam derivatives, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no activation by D-lactate or D-phenyllactate
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.1
-
acetyl-Gly-D-Ala-D-Ala
-
-
3.3
-
acetyl-L-Ala-D-Ala-D-Ala
-
-
1
-
D-Ala-D-Ala
-
-
0.33
-
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
-
0.33
-
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
-
0.4
-
UDP-N-acetylmuramoyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala-D-Ala
-
-
0.4
-
UDP-N-acetylmuramoyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala-D-Ala
-
-
0.4
-
UDP-N-acetylmuramoyl-L-Ala-gamma-D-Glu-L-mesodiaminopimelyl-D-Ala-D-Ala
-
-
1.5
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
mutant D59S, pH 7.5, 37C
18.8
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
wild-type, pH 7.5, 37C
0.6
-
diacetyl-L-diaminobutyryl-D-Ala-D-Ala
-
-
additional information
-
additional information
-
kinetics of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.2
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
wild-type, pH 7.5, 37C
23
-
UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
mutant D59S, pH 7.5, 37C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
15.5
-
D-alpha-phenylpropionate
-
pH 7.5, 25C
7
-
D-hexahydromandelate
-
pH 7.5, 25C
11.6
-
D-mandelate
-
pH 7.5, 25C
17.8
-
D-Phenyllactate
-
pH 7.5, 25C
19.3
-
glycolyl-L-Phe
-
pH 7.5, 25C
additional information
-
additional information
-
inhibition kinetics
-
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0076
-
-
mutant D344S
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
8.5
-
-
assay at
9.5
10.5
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
pH profile, wild-type and mutant enzymes
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
30
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Bacillus megaterium KM
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17000
-
-
small-angle X-ray scattering
22080
-
-
amino acid sequence
50000
-
-
gel filtration in presence of guanidine-HCl
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
up to
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, membrane preparation, pH 7.8 or 5.0, 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant wild-type and mutant enzymes from strain BL21(DE3) by ion exchange chromatography, gel filtration, and ultrafiltration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
gene pbp5, complementation of a PBP5-deficient Enterococcus hirae strain SL1 and a PBP3-deficient Enterococcus hirae strain SL2
-
gene pbp5, expression of wild-type and mutant enzymes in Escherichia coli, complementation of the pbp5-deficient mutant strain SL1 and of the pbp3-deficient strain SL2 by wild-type and mutant enzymes, recombinant strains, overview
-
gene pbp5, expression of wild-type and mutant enzymes in strain BL21(DE3)
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Enterococcus gallinarum BM4174
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73% decrease in ratio kcat/KM for D-Ala-D-Ala substrate, EC3.4.13.B1 activity
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D59S
Enterococcus gallinarum BM4174
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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
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K172N/R173N
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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
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site-directed mutagenesis, M5 mutant, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1
K199Q/K203Q
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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
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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
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site-directed mutagenesis, M4 mutant, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1
S422A
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site-directed mutagenesis, M6 mutant, inactive mutant
C115S
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site-directed mutagenesis, truncated mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme
K213C/C115S
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site-directed mutagenesis, truncated double mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme
D344S
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the mutant shows highly reduced activity compared to the wild-type
additional information
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construction of spontaneous mutants M512, M9, and G9 from mutant D344S with reduced enzyme activity, but less as for the parental mutant D344S, overview
K47C/C115S
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site-directed mutagenesis, truncated double mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme
additional information
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exchange of active site residues Lys47 and Lys213 for gamma-thialysine, pH-dependency, kinetics, and activity compared to the wild-type enzyme
additional information
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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
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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
Escherichia coli MG1655
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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
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additional information
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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