Information on EC 3.4.16.4 - serine-type D-Ala-D-Ala carboxypeptidase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
3.4.16.4
-
RECOMMENDED NAME
GeneOntology No.
serine-type D-Ala-D-Ala carboxypeptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
show the reaction diagram
VanY, carboxypeptidase activity exclusively
-
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
show the reaction diagram
VanY, carboxypeptidase activity exclusively
Enterococcus faecium BM4147
-
-
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
-
-
hydrolysis of amide bond
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
transpeptidation
-
-
transpeptidation
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
peptidoglycan biosynthesis II (staphylococci)
-
-
peptidoglycan biosynthesis IV (Enterococcus faecium)
-
-
peptidoglycan maturation (meso-diaminopimelate containing)
-
-
peptidoglycan biosynthesis
-
-
Peptidoglycan biosynthesis
-
-
Metabolic pathways
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxypeptidase I
-
-
-
-
CPase
-
-
-
-
D,D-carboxypeptidase
-
-
D,D-carboxypeptidase R39
-
D,D-dipeptidase
-
-
D-Ala-D-Ala carboxypeptidase
-
-
D-Ala-D-Ala peptidase
-
-
D-Ala-D-Ala(D,D) carboxypeptidase
Streptomyces pneumoniae
-
-
D-alanine carboxypeptidase
-
-
-
-
D-alanine carboxypeptidase
-
-
D-alanine carboxypeptidase I
-
-
-
-
D-alanine-carboxypeptidase
-
-
D-alanyl carboxypeptidase
-
-
-
-
D-alanyl-D-alanine carboxypeptidase
-
-
-
-
D-alanyl-D-alanine carboxypeptidase
-
-
D-alanyl-D-alanine carboxypeptidase/transpeptidase
-
-
D-Alanyl-D-alanine hydrolase
-
-
-
-
D-alanyl-D-alanine peptidase
-
-
-
-
D-alanyl-D-alanine transpeptidase
-
D-alanyl-D-alanine-carboxypeptidase
-
-
-
-
D-alanyl-D-alanine-carboxypeptidase
-
-
D-alanyl-D-alanine-cleaving peptidase
-
-
-
-
D-alanyl-D-alanine-cleaving-peptidase
-
-
-
-
D-alanyl-D-alanine-transpeptidase
-
-
D-amino acid amidase
lacks peptidase activity
DacA-1
Vibrio cholerae ATCC 39315
-
-
Dbv7
Nonomuraea sp.
gene name
DD-Carboxypeptidase
-
-
-
-
DD-Carboxypeptidase
-
-
DD-Carboxypeptidase
Bacillus megaterium KM
-
-
-
DD-Carboxypeptidase
-
-
DD-Carboxypeptidase
-
DD-Carboxypeptidase
-
-
DD-Carboxypeptidase
-
-
DD-Carboxypeptidase
-
-
DD-peptidase
-
-
-
-
DD-peptidase
-
-
DD-peptidase
-
DD-peptidase
-
-
DD-peptidase
-
-
DD-transpeptidase
-
-
-
-
DD-transpeptidase
-
-
DD-transpeptidase
-
-
DD-transpeptidase/penicillin-binding protein
-
-
low molecular mass penicillin binding protein
-
PBP 5
-
the DD-carboxypeptidase activity of PBP 5 is higher than that of PBP 6
PBP 6
-
the DD-carboxypeptidase activity of PBP 6 is lower than that of PBP 5
PBP-5*
-
-
-
-
PBP-6B
-
-
-
-
PBP3
Streptomyces pneumoniae
-
-
PBP5
-
-
-
-
penicillin binding protein 4
-
penicillin binding protein 5
-
-
-
-
penicillin binding protein 5
-
-
penicillin binding protein 5
-
penicillin binding proteins
-
penicillin-binding protein
-
-
penicillin-binding protein
-
-
penicillin-binding protein
-
-
penicillin-binding protein
-
-
penicillin-binding protein
-
-
penicillin-binding protein
-
-
penicillin-binding protein
-
-
penicillin-binding protein
Streptomyces pneumoniae
-
-
penicillin-binding protein
-
-
penicillin-binding protein
-
-
penicillin-binding protein
-
-
penicillin-binding protein 1B
-
-
penicillin-binding protein 4a
-
-
penicillin-binding protein 5
-
-
penicillin-binding protein 5
Bacillus megaterium KM
-
-
-
penicillin-binding protein 5
-
-
penicillin-binding protein 5a
-
-
penicillin-binding protein 5a
Bacillus megaterium KM
-
-
-
serine type D-alanyl-D-alanine carboxypeptidase/transpeptidase
-
-
serine-type D-Ala-D-Ala carboxypeptidase
-
-
serine-type-D-Ala-D-Ala carboxypeptidase
-
transpeptidase
-
-
VanX
-
-
-
-
VanY
-
-
-
-
VanY(D) DD-carboxypeptidase
-
-
VanY(D) DD-carboxypeptidase
Enterococcus faecium BM4339
-
-
-
VanYD
Enterococcus faecium BM4339
-
-
-
VanYn
Nonomuraea sp.
-
VC_0947
gene name
VC_0947
Vibrio cholerae ATCC 39315
gene name
-
zinc D-Ala-D-Ala carboxypeptidase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9077-67-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KM, two isozymes penicillin-binding protein 5 and penicillin-binding protein 5a
-
-
Manually annotated by BRENDA team
Bacillus megaterium KM
KM
-
-
Manually annotated by BRENDA team
Bacillus megaterium KM
strain KM, two isozymes penicillin-binding protein 5 and penicillin-binding protein 5a
-
-
Manually annotated by BRENDA team
544 Brucella abortus biovar 1 strain and strain K23
-
-
Manually annotated by BRENDA team
Enterococcus faecium BM4147
BM 4147
-
-
Manually annotated by BRENDA team
Enterococcus faecium BM4339
BM4339
-
-
Manually annotated by BRENDA team
ATCC 9790
-
-
Manually annotated by BRENDA team
strain K-12
-
-
Manually annotated by BRENDA team
strains K-12 and 2443
-
-
Manually annotated by BRENDA team
wild type strain CS109
-
-
Manually annotated by BRENDA team
Nonomuraea sp.
-
UniProt
Manually annotated by BRENDA team
Ochrobactrum anthropi SV3
UniProt
Manually annotated by BRENDA team
Streptomyces pneumoniae
-
-
-
Manually annotated by BRENDA team
K11; R39; R61
-
-
Manually annotated by BRENDA team
R39; R61
-
-
Manually annotated by BRENDA team
R61; sp. K15
-
-
Manually annotated by BRENDA team
sp. K15
Uniprot
Manually annotated by BRENDA team
strain K15
-
-
Manually annotated by BRENDA team
strain R61
Uniprot
Manually annotated by BRENDA team
Streptomyces sp. R39
R39
-
-
Manually annotated by BRENDA team
Vibrio cholerae ATCC 39315
-
UniProt
Manually annotated by BRENDA team
KP+, serotype O3:K6
UniProt
Manually annotated by BRENDA team
KP+, serotype O3:K6
UniProt
Manually annotated by BRENDA team
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
-
the DD-carboxypeptidase activity of PBP 5 is responsible for maintaining cell shape
physiological function
-
the beta-lactam-sensitive D,D-carboxypeptidase activity of Pbp4 controls the L,D and D,D transpeptidation pathways in Corynebacterium jeikeium
physiological function
when the viable but nonculturable state of the bacterium is induced, the rod-shaped cells become coccoid, and various aberrantly shaped intermediates are formed in the initial stage. Among several genes, the expression of dacB, which encodes D-alanyl-D-alanine carboxypeptidase, is enhanced the most. The proportion of aberrantly shaped cells is significantly lower in the dacB mutant strain than in the parent strain, but the proportion is restored in the presence of the complementary dacB gene
physiological function
Nonomuraea sp.
-
enzyme has a role in removing the last D-Ala from the pentapeptide peptidoglycan precursors and reprogramming cell wall biosynthesis. Isoform C-His6-VanYn over-expression confers glycopeptide resistance to Streptomyces venezuelae. The addition of His6-tag at the N-terminus of the protein abolishes its biological activity either in vitro or in vivo assays
physiological function
Vibrio cholerae lacking isoform DacA-1 displays slow growth, aberrant morphology and altered peptidoglycan homeostasis in Luria-Bertani medium, as well as a profound plating defect. DacA-1 alone among Vibrio choleraes low molecular weight penicillin-binding proteins is critical for bacterial growth. The growth and morphology of the dacA-1 mutant are unimpaired in Luria-Bertani media containing reduced concentrations of NaCl of 100 mM or less, and also within suckling mice, a model host for the study of cholera pathogenesis. Peptidoglycan from the dacA-1 mutant contains elevated pentapeptidelevels in standard and low salt media
physiological function
Vibrio cholerae ATCC 39315
-
Vibrio cholerae lacking isoform DacA-1 displays slow growth, aberrant morphology and altered peptidoglycan homeostasis in Luria-Bertani medium, as well as a profound plating defect. DacA-1 alone among Vibrio choleraes low molecular weight penicillin-binding proteins is critical for bacterial growth. The growth and morphology of the dacA-1 mutant are unimpaired in Luria-Bertani media containing reduced concentrations of NaCl of 100 mM or less, and also within suckling mice, a model host for the study of cholera pathogenesis. Peptidoglycan from the dacA-1 mutant contains elevated pentapeptidelevels in standard and low salt media
-
physiological function
-
when the viable but nonculturable state of the bacterium is induced, the rod-shaped cells become coccoid, and various aberrantly shaped intermediates are formed in the initial stage. Among several genes, the expression of dacB, which encodes D-alanyl-D-alanine carboxypeptidase, is enhanced the most. The proportion of aberrantly shaped cells is significantly lower in the dacB mutant strain than in the parent strain, but the proportion is restored in the presence of the complementary dacB gene
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-2-[[N-(phenylacetyl)glycyl]sulfanyl]propanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(R)-[2-(benzoylamino)propionylsulfanyl]acetic acid + H2O
?
show the reaction diagram
-
-
-
-
?
2-(N-glycyl-L-cysteinyl)acetyl-D-alanyl-D-alanine + H2O
2-(N-glycyl-L-cysteinyl)acetyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
3-(N-acetyl-L-cysteinyl)propanoyl-D-alanyl-D-alanine + H2O
3-(N-acetyl-L-cysteinyl)propanoyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
3-(N-glycyl-cysteaminyl)propanoyl-D-alanyl-D-alanine + H2O
3-(N-glycyl-cysteaminyl)propanoyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
3-(N-glycyl-L-cysteinyl)-propanoyl-D-alanyl-D-thiolactate + H2O
3-(N-glycyl-L-cysteinyl)-propanoyl-D-alanine + D-thiolactate
show the reaction diagram
-
very efficient substrate for R61 DD-peptidase
-
?
3-(N-glycyl-L-cysteinyl)butanoyl-D-alanyl-D-alanine + H2O
3-(N-glycyl-L-cysteinyl)butanoyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
3-(N-glycyl-L-cysteinyl)propanoyl-D-alanyl-D-alanine + H2O
3-(N-glycyl-L-cysteinyl)propanoyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate + H2O
(2R)-N-(phenylacetyl)-2-hydroxyglycine + 3-hydroxybenzoate
show the reaction diagram
-
no reaction with (S)-enantiomer
substrate for both beta-lactamases and D,D-peptidases. Both prefer the same enantiomer, the (R)-form
?
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
(2R)-N-(phenylacetyl)-2-methoxyglycine + 3-hydroxybenzoate
show the reaction diagram
-
no reaction with (S)-enantiomer
substrate for both beta-lactamases and D,D-peptidases. Both prefer the same enantiomer, the (R)-form
?
3-carboxyphenyl N-(phenylacetyl)-alpha-methoxyglycinate + H2O
?
show the reaction diagram
-
-
-
-
?
3-carboxyphenyl N-(phenylacetyl)-alpha-serinate + H2O
?
show the reaction diagram
-
-
-
-
?
3-[[N-(phenylacetyl)-D-alanyl]oxy]benzoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
3-[[N-(phenylacetyl)glycyl]oxy]benzoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
Ac2-L-Lys-D-Ala-Gly-L-Ala
?
show the reaction diagram
-
poor substrate, but hydrolysis was significant
-
-
?
Ac2-L-Lys-D-Ala-Gly-L-Gln
?
show the reaction diagram
-
poor substrate, but hydrolysis was significant
-
-
?
Ac2-L-Lys-D-Ala-Gly-L-Gln + Gly-L-Ala
Ac2-L-Lys-D-Ala-Gly-L-Ala + ?
show the reaction diagram
-
transpeptidation
-
r
Ac2-L-Lys-D-Ala-Gly-L-Leu
?
show the reaction diagram
-
poor substrate, but hydrolysis was significant
-
-
?
Ac2-L-Lys-D-Ala-Gly-L-Leu + D-alanine
Ac2-L-Lys-D-Ala-D-Ala + ?
show the reaction diagram
-
transpeptidation
-
r
acetyl-L-Lys-D-Ala-D-Ala + H2O
acetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
Nonomuraea sp.
-
-
?
acetyl-L-Lys-D-Ala-D-Ala + H2O
acetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
Nonomuraea sp.
-
-
-
?
benzoyl-D-Ala-thioglycolate + H2O
?
show the reaction diagram
-
-
-
?
benzoyl-Gly-thioglycolate + H2O
?
show the reaction diagram
-
-
-
?
benzoyl-Gly-thiolactate + H2O
?
show the reaction diagram
-
-
-
?
Boc-gamma-D-Glu-L-Lys-(Cbz)-D-Ala-D-Ala
?
show the reaction diagram
-
-
-
?
bocillin FL
?
show the reaction diagram
-
-
-
-
?
D-Ala-D-Ala + H2O
D-Ala + D-Ala
show the reaction diagram
-
-
-
?
D-Ala-D-Ala + H2O
D-Ala + D-Ala
show the reaction diagram
-
-
-
?
D-Ala-D-Ala + H2O
D-Ala + D-Ala
show the reaction diagram
Nonomuraea sp.
-
-
?
D-Ala-D-Ala + H2O
D-Ala + D-Ala
show the reaction diagram
Nonomuraea sp.
-
-
-
?
D-Ala-D-Phe + H2O
D-Ala + D-Phe
show the reaction diagram
-
-
-
?
D-Ala-D-Trp + H2O
D-Ala + D-Trp
show the reaction diagram
-
-
-
?
D-Ala-D-Tyr + H2O
D-Ala + D-Tyr
show the reaction diagram
-
-
-
?
D-amino acid amide + H2O
D-amino acid + ammonia
show the reaction diagram
-
-
?
GlcNAc-MurNAc-L-Ala-D-iGluNH2-meso-diaminopimelic acid-NH2-D-Ala-D-Ala + H2O
GlcNAc-MurNAc-L-Ala-D-iGluNH2-meso-diaminopimelic acid-NH2-D-Ala + D-Ala
show the reaction diagram
-
-
-
?
Gly-gamma-L-Glu-D-Ala-D-Ala + H2O
Gly-gamma-L-Glu-D-Ala + D-Ala
show the reaction diagram
-
-
-
?
Gly-L-alpha-amino-epsilon-pimelyl-D-Ala-D-Ala + H2O
Gly-L-alpha-amino-epsilon-pimelyl-D-Ala + D-Ala
show the reaction diagram
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine + H2O
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine + H2O
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-leucine + H2O
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine + D-leucine
show the reaction diagram
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-norleucine + H2O
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine + D-norleucine
show the reaction diagram
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-glycine + H2O
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine + glycine
show the reaction diagram
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-glycyl-L-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-glycyl-L-leucine + H2O
?
show the reaction diagram
-
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-glycyl-L-phenylalanine + H2O
?
show the reaction diagram
-
-
-
-
?
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]amino]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
hippuryl-mercaptoacetic acid
hippuric acid + mercaptoacetate
show the reaction diagram
-
-
-
?
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O
?
show the reaction diagram
-
only substrate of penicillin-binding protein 5, but not of penicillin-binding protein 6
-
-
?
N,N'-diacetyl-L-Lys-D-Ala-D-Ala + H2O
?
show the reaction diagram
Streptomyces pneumoniae
-
-
-
-
?
N,N'-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
N-acetyl-D-Ala-D-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-D-Ala-D-Ala + H2O
N-acetyl-D-Ala + D-Ala
show the reaction diagram
-
-
-
?
N-acetyl-L-Lys-D-Ala-D-Ala + H2O
N-acetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
?
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + H2O
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanine + D-alanine
show the reaction diagram
-
-
?
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine + H2O
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
?
N-alpha-acetyl-L-Lys-D-Ala-thiolactate + H2O
?
show the reaction diagram
-
-
-
?
N-benzoyl-D-Ala + H2O
benzoate + D-Ala
show the reaction diagram
-
substrate binding structure
-
?
N-benzoyl-D-Ala-thio-D-lactate
?
show the reaction diagram
-
-
-
?
N-benzoyl-D-Ala-thioglycolate
?
show the reaction diagram
-
-
-
?
N-[(6S)-6-carboxy-6-(glycylamino)hexanoyl]-D-alanyl-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
show the reaction diagram
-
acceptors in transpeptidase reaction
-
-
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
show the reaction diagram
-
acceptors in transpeptidase reaction
-
-
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
show the reaction diagram
-
acceptors in transpeptidase reaction
-
-
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
show the reaction diagram
-
acceptors in transpeptidase reaction
-
-
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
show the reaction diagram
-
acceptors in transpeptidase reaction
-
-
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
show the reaction diagram
-
acceptors in transpeptidase reaction
-
ir
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
show the reaction diagram
-
acceptors in transpeptidase reaction
-
ir
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
show the reaction diagram
-
acceptors in transpeptidase reaction
-
ir
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
show the reaction diagram
Streptomyces sp. R39
-
acceptors in transpeptidase reaction
-
-
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
show the reaction diagram
Bacillus megaterium KM
-
acceptors in transpeptidase reaction
-
-
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
-
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
-
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
Streptomyces sp. R39
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
show the reaction diagram
Streptomyces sp. R39
-
-
-
-
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
Nonomuraea sp.
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
Nonomuraea sp.
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
N,N'-diacetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-lactate + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-lactate
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
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate + H2O
?
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
D-alanine + Nalpha,Nepsilon-diacetyl-L-lysyl-D-alanine
show the reaction diagram
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
-
substrate in DD-carboxypeptidase activity assay
-
-
?
Nalpha,Nepsilon-diacetyl-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
?
Nalpha,Neta-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
-
substrate for assay of DD-carboxypeptidase activity
-
-
?
Nalpha-(beta-1,4-acetylglucosaminyl-N-acetylmuramyl-L-alanyl-D-isoglutaminyl)-Nepsilon-(D-isoasparaginyl)-L-lysyl-D-alanyl-D-alanine + H2O
Nalpha-(beta-1,4-acetylglucosaminyl-N-acetylmuramyl-L-alanyl-D-isoglutaminyl)-Nepsilon-(D-isoasparaginyl)-L-lysyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha-Acetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
?
Nalpha-acetyl-L-Lys-D-Ala-D-Ala + H2O
?
show the reaction diagram
substrate is used to detect the hydrolyzing activity of PBP4a
-
-
?
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
?
phenylacetyl-D-Ala-thioglycolate + H2O
?
show the reaction diagram
-
-
-
?
phenylacetyl-D-Ala-thiolactate + H2O
?
show the reaction diagram
-
-
-
?
S2a + D-alanine
?
show the reaction diagram
-
-
-
-
?
S2a + D-leucine
?
show the reaction diagram
-
-
-
-
?
S2a + D-phenylalanine
?
show the reaction diagram
-
-
-
-
?
S2a + Gly-Gly
?
show the reaction diagram
-
-
-
-
?
S2a + Gly-Gly-Gly
?
show the reaction diagram
-
-
-
-
?
S2a + Gly-L-Ala
?
show the reaction diagram
-
-
-
-
?
S2a + Gly-L-Gln
?
show the reaction diagram
-
-
-
-
?
S2a + Gly-L-Leu
?
show the reaction diagram
-
one of the most efficient acceptors
-
-
?
S2d thiolester
?
show the reaction diagram
-
-
-
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala + D-Ala
show the reaction diagram
Enterococcus faecium, Enterococcus faecium BM4339
-
-
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O
D-Ala + UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala
show the reaction diagram
Bacillus megaterium, Bacillus megaterium KM
-
i.e. UDP-N-acetylmuraminoyl-pentapeptide, release of D-alanine from UDPMurNAc-pentapeptide substrate
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
Streptomyces sp. R39
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
Enterococcus faecium BM4147
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
Bacillus megaterium KM
-
-
-
-
-
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
Streptomyces sp. R39
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
Streptomyces sp. R39
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
Streptomyces sp. R39
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
Streptomyces sp. R39, Streptomyces sp. K11
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
Enterococcus faecium BM4147
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
Bacillus megaterium KM
-
-
-
?
X-D-Ala-D-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
L-Lys-D-Ala-D-Ala + H2O
L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
?
additional information
?
-
-
influence of substrate conformation
-
-
-
additional information
?
-
-
not D-Ala-D-lactate
-
-
-
additional information
?
-
-
requirement for D-Ala in P1 position
-
-
-
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
?
-
-
penicillin-binding protein
-
-
?
additional information
?
-
specific substrate binding to the peptidase induces a conformational change in the active site that places Ser62 in an optimal position for catalysis. This activated conformation relaxes as the reaction proceeds
-
-
?
additional information
?
-
-
the enzyme forms a covalent acyl-enzyme complex with beta-lactam antibiotics
-
-
?
additional information
?
-
the enzyme is responsible for the final peptidoglycan cross-linking step in bacterial cell wall biosynthesis
-
-
?
additional information
?
-
-
low molecular mass PBPs can exert carboxypeptidase and/or endopeptidase activities and play auxiliary roles in the peptidoglycan metabolism process, the serine protease catalyzes glycosyl transfer, i.e. polymerization of glycan chains, and transpeptidation, i.e. cross-linking of stem peptides, which are essential for peptidoglycan stability in bacterial cell wall synthesis, and for the cell division process, overview
-
-
-
additional information
?
-
-
enzyme removes the terminal D-alanine from the pentapeptide side chains of muramic acid in peptidoglycan
-
-
-
additional information
?
-
-
the enzyme cleaves the C-terminal D-Ala5 of stem pentapeptides and forms the essential tetrapeptide substrate of a beta-lactam-insensitive L,D-transpeptidase
-
-
-
additional information
?
-
-
bifunctional enzyme catalyzing the reactions of D-Ala-D-Ala-carboxypeptidase EC 3.4.16.4 and D-Ala-D-Ala-dipeptidase EC 3.4.13.22
-
-
-
additional information
?
-
Nonomuraea sp.
-
on substrates mimicking peptidoglycan precursors, isoform VanYn shows D,D-carboxypeptidase and D,D-dipeptidase activity, but lacks D,D-carboxyesterase ability on D-Ala-D-Lac-terminating peptides
-
-
-
additional information
?
-
Enterococcus faecium BM4339
-
penicillin-binding protein
-
-
?
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 SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Ala-D-Ala + H2O
D-Ala + D-Ala
show the reaction diagram
-
-
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O
D-Ala + UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala
show the reaction diagram
-
i.e. UDP-N-acetylmuraminoyl-pentapeptide, release of D-alanine from UDPMurNAc-pentapeptide substrate
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala + D-Ala
show the reaction diagram
Enterococcus faecium BM4339
-
-
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O
D-Ala + UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala
show the reaction diagram
Bacillus megaterium KM
-
i.e. UDP-N-acetylmuraminoyl-pentapeptide, release of D-alanine from UDPMurNAc-pentapeptide substrate
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
P15555
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
Streptomyces sp. R39
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
Enterococcus faecium BM4147
-
-
-
-
-
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
Bacillus megaterium KM
-
-
-
-
-
D-amino acid amide + H2O
D-amino acid + ammonia
show the reaction diagram
Q9LCC8
-
-
?
additional information
?
-
P15555
the enzyme is responsible for the final peptidoglycan cross-linking step in bacterial cell wall biosynthesis
-
-
?
additional information
?
-
-
low molecular mass PBPs can exert carboxypeptidase and/or endopeptidase activities and play auxiliary roles in the peptidoglycan metabolism process
-
-
-
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
Zn2+
-
tetrahedrally coordinated by two histidines, an aspartate, and a water molecule
Zn2+
Nonomuraea sp.
-
presence of 8 mM Zn2+ restores the activity of EDTA-treated enzyme
Mg2+
-
required
additional information
-
no cation requirement
additional information
-
no cation requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2,3)-alpha-methylene benzylpenicillin
-
modeling of enzyme-inhibitor complex
(2-phenylethyl)boronic acid
-
91% residual activity at 1 mM
(2R)-2-amino-7-oxo-7-[(4,4,4-trifluoro-3-oxobutan-2-yl)amino]heptanoic acid
-
i.e. D-alpha-aminopimelyl-(1,1,1-trifluoro-3-amino)butan-2-one
(3-aminophenyl)boronic acid
-
20% residual activity at 1 mM
(3-nitrophenyl)boronic acid
-
82% residual activity at 1 mM
(3H)benzylpenicillin
Streptomyces pneumoniae
-
-
(3R,5R)-3-(furyl-2')-4-dethia-4-oxa-penam
-
-
(3R,5R,6R)-6-methyl-3-(furyl-2')-4-dethia-4-oxa-penam
-
-
(3R,5R,6S)-6-methyl-3-(furyl-2')-4-dethia-4-oxa-penam
-
-
(3R,5S)-3-(furyl-2')-4-dethia-4-oxa-penam
-
-
(3R,5S,6R)-3-benzyloxycarbonyl-6-methyl-4-dethia-4-oxa-penam
-
-
(3R,5S,6R)-6-methyl-3-(furyl-2')-4-dethia-4-oxa-penam
-
-
(3S,5R)-3-(furyl-2')-4-dethia-4-oxa-penam
-
-
(3S,5R,6S)-3-benzyloxycarbonyl-6-methyl-4-dethia-4-oxa-penam
-
-
(3S,5R,6S)-6-methyl-3-(furyl-2')-4-dethia-4-oxa-penam
-
-
(3S,5S)-3-(furyl-2')-4-dethia-4-oxa-penam
-
-
(3S,5S,6R)-6-methyl-3-(furyl-2')-4-dethia-4-oxa-penam
-
-
(4-phenoxyphenyl)boronic acid
-
98% residual activity at 1 mM
(5-acetylthiophen-2-yl)boronic acid
-
88% residual activity at 1 mM
(5-chlorothiophen-2-yl)boronic acid
-
91% residual activity at 1 mM
(5-cyanothiophen-2-yl)boronic acid
-
95% residual activity at 1 mM
(5-formylthiophen-2-yl)boronic acid
-
99% residual activity at 1 mM
(5R,6R)-6-[[(6S)-6-carboxy-6-(glycylamino)hexanoyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
-
-
(6R,7R)-3-[(acetyloxy)methyl]-7-[(6S)-6-carboxy-6-(glycylamino)hexanoyl]amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
1,2-Ethanedithiol
-
-
1,3-propanedithiol dithiothreitol
-
-
-
1-benzothiophen-2-ylboronic acid
-
86% residual activity at 1 mM
2,1-benzoxaborol-1(3H)-ol
-
45% residual activity at 1 mM
2,3-dimercapto-1-propane-sulfonic acid
-
-
2,3-dimercapto-1-propanol
-
-
2-Methylpenem
-
-
2-Phenylpenems
-
-
-
3-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)benzoic acid
-
38% residual activity at 0.5 mM
3-(acetylamino)-5-(dihydroxyboranyl)benzoic acid
-
50% residual activity at 1 mM
3-(benzoylamino)-5-(dihydroxyboranyl)benzoic acid
-
9% residual activity at 1 mM
3-(dihydroxyboranyl)-4-[(phenylacetyl)amino]benzoic acid
-
80% residual activity at 1 mM
3-(dihydroxyboranyl)-5-[(2,6-dimethoxybenzoyl)amino]benzoic acid
-
84% residual activity at 1 mM
3-(dihydroxyboranyl)-5-[(phenoxyacetyl)amino]benzoic acid
-
2% residual activity at 1 mM
3-(dihydroxyboranyl)-5-[(thiophen-2-ylacetyl)amino]benzoic acid
-
5% residual activity at 1 mM
3-(dihydroxyboranyl)-5-[(thiophen-2-ylcarbonyl)amino]benzoic acid
-
18% residual activity at 1 mM
3-(dihydroxyboryl)-5-(2-methoxybenzamido)benzoic acid
-
10% residual acvtivity at 1 mM
3-(dihydroxyboryl)-5-(2-phenylacetamido)benzoic acid
-
3% residual acvtivity at 1 mM
3-(dihydroxyboryl)benzoic acid
-
20% residual acvtivity at 1 mM
3-(N-glycyl-L-cysteinyl)-N-ethylpropionamide
-
-
3-(trifluoroacetyl)benzoic acid
-
60% residual activity at 1 mM
3-formylbenzoic acid
-
77% residual activity at 1 mM
4-(dihydroxyboranyl)benzoic acid
-
85% residual activity at 1 mM
4-chloromercuribenzoate
-
complete inhibition at 1 mM
4-[(phenylacetyl)amino]-3-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)benzoic acid
-
81% residual activity at 1 mM
5-(dihydroxyboranyl)thiophene-2-carboxylic acid
-
57% residual activity at 1 mM
6-beta(alpha-N-acetyl-L-lysyl)-aminopenicillanic acid
-
-
6-beta(D-alpha-aminopimelyl)-aminopenicillanic acid
-
-
6-beta(D-alpha-aminosuberyl)-aminopenicillanic acid
-
-
6-beta(N-acetyl-L-alanyl-gamma-D-glutamyl-L-alanyl)-aminopenicillanic acid
-
-
7-(phenoxyacetamido)-3-desacetoxycephalosporamic acid
-
-
7-beta(alpha-N-acetyl-L-lysyl)-aminocephalosporanic acid
-
-
7-beta(D-alpha-aminopimelyl)-aminocephalosporanic acid
-
-
alpha-N-glycyl-epsilon-N-acetyl-L-lysine
-
inhibits hydrolysis of 3-(N-glycyl-L-cysteinyl)-propanoyl-D-alanyl-D-thiolactate
amoxicillin
-
-
ampicillin
-
-
ampicillin
-
-
ampicillin
-
complete inhibition at 0.57 mM, 95% inhibition at 0.285 mM
arylakylidene imino-thiazolidin-4-ones 10
-
86% inhibition
arylakylidene imino-thiazolidin-4-ones 11
-
82% inhibition
arylakylidene imino-thiazolidin-4-ones 12
-
64% inhibition
arylakylidene imino-thiazolidin-4-ones 13
-
83% inhibition
arylakylidene imino-thiazolidin-4-ones 16
-
100% inhibition
arylakylidene imino-thiazolidin-4-ones 17
-
100% inhibition
arylakylidene imino-thiazolidin-4-ones 18
-
96% inhibition
arylakylidene imino-thiazolidin-4-ones 19
-
84% inhibition
arylakylidene imino-thiazolidin-4-ones 5
-
89% inhibition
arylakylidene imino-thiazolidin-4-ones 6
-
92% inhibition
arylakylidene imino-thiazolidin-4-ones 8
-
99% inhibition
arylakylidene imino-thiazolidin-4-ones 9
-
85% inhibition
arylalkylidene rhodanine derivative 1
-
88% inhibition
arylalkylidene rhodanine derivative 2
-
95% inhibition
arylalkylidene rhodanine derivative 2
-
94% inhibition
arylalkylidene rhodanine derivative 2
-
75% inhibition
arylalkylidene rhodanine derivative 3
-
83% inhibition
arylalkylidene rhodanine derivative 4
-
95% inhibition
benzylpenicillin
-
-
benzylpenicillin
-
ester-linked to serins
benzylpenicillin
-
-
benzylpenicillin
-
IC50: 0.00002 mg/ml, inhibition of the enzyme influences production of peptidoglycan precursors internally
benzylpenicillin
-
classical non-specific beta-lactam
benzylpenicillin
-
80% inhibition at 0.1 mg/ml
benzylpenicllin
-
dipeptide-releasing activity is penicillin sensitive
-
beta-lactam
-
R39 has a high beta-lactam binding activity
beta-lactam
-
-
beta-Lactams
-
kinetic constants
-
beta-Lactams
-
-
-
biphenyl-4,4'-diyldiboronic acid
-
97% residual activity at 0.1 mM
Boc-gamma-D-Glu-L-Lys-(Cbz)-D-boroAla-(-)-pinanediol
-
effective inhibitor of the D-alanine CPase activity of PBP5
Ca2+
Nonomuraea sp.
-
1 mM, no residual activty
carbenicillin
-
-
cefaclor
-
-
cefadroxil
-
-
cefalexin
-
-
cefalothin
-
-
cefmetazole
-
-
cephalexin
-
-
Cephalosporidin
-
-
Cephalosporin
-
-
Cephalosporin
-
with glycyl-L-alpha-amino-epsilon-pimelyl side-chain, this beta lactam might be a better antibiotic than a non-specific counterpart
cephalosporin C
-
classical non-specific beta-lactam
Cephalothin
-
-
Cetyltrimethylammonium bromide
-
-
Cloxacillin
-
-
D-Ala(P,O)D-Ala
-
acts as slow binding inhibitor
D-Ala(P,O)D-Phe
-
acts as slow binding inhibitor
D-alpha-phenylpropionate
-
-
D-Cysteine
-
-
D-hexahydromandelate
-
-
D-mandelate
-
-
D-phenyllactate
-
-
Delta2-(and Delta3)-Deacetoxy-7-phenylacetamidocephalosporanates
-
-
-
depsipeptides
-
-
-
diacetyl-L-Lys-D-Ala
-
-
Dicloxacillin
-
-
diisopropyl fluorophosphate
-
1 mM, 28% inhibition
dithiothreitol
-
-
EDTA
Nonomuraea sp.
-
4 mM, complete loss of activity. Ativity may be restored in presence of 8 mM Zn2+
epsilon-N-glycyl-alpha-N-acetyl-L-alanyl-D-isoglutaminyl-L-lysine
-
inhibits hydrolysis of 3-(N-glycyl-L-cysteinyl)-propanoyl-D-alanyl-D-thiolactate
formaldehyde
-
1 mM, 53% inhibition
glycolyl-L-Phe
-
-
iodoacetamide
-
1 mM, 20% inhibition
L-cysteine
-
-
Mercaptosuccinic acid
-
-
Methicillin
-
-
Methicillin
-
-
Mg2+
Nonomuraea sp.
-
1 mM, no residual activty
Moenomycin
-
inhibits the glycosyl transferase activity
N,N-diacetyl-L-Lys-D-Ala-D-Ala
Streptomyces pneumoniae
-
inhibition of PBP3 by its own substrate above a ligand concentration of 15 mM
N-(glycyl)-D,L-alpha-aminocaprylic acid
-
inhibits hydrolysis of 3-(N-glycyl-L-cysteinyl)-propanoyl-D-alanyl-D-thiolactate
N-benzoyl-beta-sultam
-
time-dependent, irreversible active site directed inhibitor, the rate of inactivation is first order with respect to beta-sultam concentration and second order rate constants show dependence on pH
N-Chlorosuccinimide
-
1 mM, 50% inhibition
N-p-chloro-beta-sultam
-
-
N-p-methoxy-beta-sultam
-
least effective inhibitor
N-p-nitro-beta-sultam
-
-
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala-D-Ala
-
substrate inhibition above 30 mM
NEM
-
1 mM, complete inhibition
nocardicin A
-
-
Oxyimino-DELTA3-cephalosporins
-
syn- and anti-isomers
-
p-hydroxymercuribenzoate
-
1 mM, complete inhibition
Penicillanate
-
-
penicillin
-
kinetic model of interaction
penicillin
-
binds covalently to Ser36, Bacillus subtilis, Bacillus stearothermophilus
penicillin
Streptomyces pneumoniae
-
-
penicillin
-
having the glycyl-L-alpha-amino-epsilon-pimelyl side-chain of Streptomyces strain R61 peptidoglycan, this beta lactam might be the perfect antibiotic as compared to a non-specific counterpart
penicillin
-
the enzyme is sensitive to inhibition, penicillin-binding profile during development of spores, overview
penicillin G
-
-
penicillin G
-
-
penicillin G
-
-
Penicillin V
-
-
phenoxymethylpenicillin
-
-
phenyl glycyl-L-alpha-aminopimelyl-epsilon-(D-2-aminoethyl)phosphonate
-
-
phenylboronic acid
-
1 mM, 26% inhibition
phenylboronic acid
-
50% residual activity at 0.5 mM
piperacillin
-
-
piperacillin
-
-
thiophen-2-ylboronic acid
-
88% residual activity at 1 mM
thiosalicylic acid
-
-
Vancomycin
-
vancomycin derivatives inhibit the glycosyl transferase activity
Zn2+
Nonomuraea sp.
-
1 mM, no residual activty
[3-([[5-(dimethylamino)naphthalen-1-yl]sulfonyl]amino)phenyl]boronic acid
-
60% residual activity at 0.5 mM
[3-[(2,6-dimethoxybenzoyl)amino]-5-(methoxycarbonyl)thiophen-2-yl]boronic acid
-
98% residual activity at 1 mM
Moenomycin
-
-
additional information
-
serine enzyme not inhibited by PMSF
-
additional information
-
no inhibition: EDTA
-
additional information
-
no inhibition: EDTA
-
additional information
-
no inhibition: penicillin G, ampicillin, cephalosporin C
-
additional information
-
inhibition studies
-
additional information
-
inhibition studies
-
additional information
-
no significant inhibition by arylalkylidene rhodanine derivative 1 and 3 respectively and arylakylidene imino-thiazolidin-4-ones 6, 8, 13, 16, 17 and 19 respectively
-
additional information
-
no significant inhibition by arylakylidene imino-thiazolidin-4-ones 7, 14 and 15 respectively
-
additional information
-
no significant inhibition by arylalkylidene rhodanine derivative 1, 3 and 4 respectively and arylakylidene imino-thiazolidin-4-ones 5 to 19
-
additional information
-
not inhibited by methyl 3-(dihydroxyboryl)-5-(2-phenylacetamido)benzoate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activation
aminomalon-(N-ethyl)amide
-
dual function acceptor, which is particularly effective
aminomalon-(N-phenethyl)amide
-
dual function acceptor, which is particularly effective
D-phenylalanine
-
most effective D-amino acid and dipeptide acceptor, respectively
Gly-L-Phe
-
most effective D-amino acid and dipeptide acceptor, respectively
N-ethyl-D-asparagine
-
less effective acceptor
p-chloromercuribenzoate
-
stimulation of hydrolase reaction, no influence on transpeptidase
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
(2R)-2-[[N-(phenylacetyl)glycyl]sulfanyl]propanoic acid
-
-
0.86
2-(N-glycyl-L-cysteinyl)acetyl-D-alanyl-D-alanine
-
-
1.28
3-(N-acetyl-L-cysteinyl)propanoyl-D-alanyl-D-alanine
-
-
3
3-(N-glycyl-cysteaminyl)propanoyl-D-alanyl-D-alanine
-
-
0.004
3-(N-glycyl-L-cysteinyl)-propanoyl-D-alanyl-D-thiolactate
-
-
0.48
3-(N-glycyl-L-cysteinyl)butanoyl-D-alanyl-D-alanine
-
-
0.26
3-(N-glycyl-L-cysteinyl)propanoyl-D-alanyl-D-alanine
-
-
0.36
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
-
pH 7.5, 25C
4.3
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
-
pH 7.5, 25C
0.2
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
-
pH 7.5, 25C
0.45
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
-
pH 7.5, 25C
0.2
3-carboxyphenyl N-(phenylacetyl)-alpha-methoxyglycinate
-
-
0.45
3-carboxyphenyl N-(phenylacetyl)-alpha-methoxyglycinate
-
-
0.35
3-carboxyphenyl N-(phenylacetyl)-alpha-serinate
-
-
0.85
3-carboxyphenyl N-(phenylacetyl)-alpha-serinate
-
-
1.8
3-carboxyphenyl N-(phenylacetyl)-alpha-serinate
-
-
1.37
3-[[N-(phenylacetyl)-D-alanyl]oxy]benzoic acid
-
-
0.76
3-[[N-(phenylacetyl)glycyl]oxy]benzoic acid
-
-
7.5
acetyl-L-Ala-D-Glu-L-Lys(Ac)-D-Ala-D-Ala
-
-
8
acetyl-L-Lys-D-Ala-D-Ala
Nonomuraea sp.
-
pH 7.4, 25C
-
1.3
benzoyl-D-Ala-thioglycolate
pH 7.2, 37C, mutant enzyme C98A
1.5
benzoyl-D-Ala-thioglycolate
pH 7.2, 37C, wild-type enzyme
0.8
benzoyl-Gly-thioglycolate
pH 7.2, 37C, mutant enzyme C98A
3
benzoyl-Gly-thioglycolate
above, pH 7.2, 37C, wild-type enzyme
0.22
benzoyl-Gly-thiolactate
pH 7.2, 37C, wild-type enzyme
0.3
benzoyl-Gly-thiolactate
pH 7.2, 37C, mutant enzyme C98A
1
benzoyl-Gly-thiolactate
pH 7.2, 37C, mutant enzyme K38H
6.4
Boc-gamma-D-Glu-L-Lys-(Cbz)-D-Ala-D-Ala
-
-
20
D-Ala-D-Ala
Nonomuraea sp.
-
pH 7.4, 25C
0.86
Gly-gamma-L-Glu-D-Ala-D-Ala
-
-
0.0079
Gly-L-alpha-amino-epsilon-pimelyl-D-Ala-D-Ala
-
-
0.0079
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine
-
-
0.26
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]amino]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
-
-
0.0041
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
-
-
0.12
hippuryl-mercaptoacetic acid
-
crystal and solution
9.8
N,N'-diacetyl-L-lysyl-D-alanyl-D-alanine
-
-
3.5
N-(N-acetyl-1-O-methyl-beta-muramoyl)-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.5, 25C
0.675
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant Q422S
0.678
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant Q422A
0.682
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant wild type enzyme
0.712
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant R361H
0.744
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant R361A
0.913
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant F160A
0.0178
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant R361H
0.0204
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
wild type enzyme
0.0344
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant F160A
0.116
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant Q422S
0.222
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant D155A
0.237
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant Q422A
0.401
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant R361A
0.4
N-alpha-acetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37C, wild-type enzyme
0.0079
N-[(6S)-6-carboxy-6-(glycylamino)hexanoyl]-D-alanyl-D-alanine
-
-
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, 25C
12
Nalpha, Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
lysozyme releasable enzyme
0.1
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
54000 MW enzyme
0.35
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
above, pH 7.2, 37C, mutant enzyme C98A
1.28
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
recombinant PBP 6, in 50 mM Tris-HCl, pH 8.5, at 37C
3.8
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
-
6.2
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
pH 7.2, 37C, wild-type enzyme
8.98
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37C
14
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
-
14
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
-
2
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37C, mutant enzyme C98A
3
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate
above, pH 7.2, 37C, wild-type enzyme
1.45
Nalpha-(beta-1,4 acetylglucosaminyl-N-acetylmuramyl-L-alanyl-D-isoglutaminyl)-Nepsilon-(D-isoasparaginyl)L-Lys-D-Ala-D-Ala
-
-
-
9.4
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala
pH 7.2, 37C, wild-type enzyme
30
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala
pH 7.2, 37C, mutant enzyme C98A
0.6
Nalpha-acetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37C, mutant enzyme C98A
2.4
phenylacetyl-D-Ala-thioglycolate
pH 7.2, 37C, mutant enzyme K38H
3
phenylacetyl-D-Ala-thioglycolate
above, pH 7.2, 37C, mutant enzyme C98A; above, pH 7.2, 37C, wild-type enzyme
1.2
phenylacetyl-D-Ala-thiolactate
pH 7.2, 37C, mutant enzyme C98A; pH 7.2, 37C, wild-type enzyme
1.4
UDP-N-acetylmuramyl-L-Ala-D-Glu-mesodiaminopimelyl-D-Ala-D-Ala
-
-
5 - 20
X-D-Ala-D-Ala
-
value depending on X
-
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 37C
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
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.7
(2R)-2-[[N-(phenylacetyl)glycyl]sulfanyl]propanoic acid
Streptomyces sp. R61
-
-
0.17
2-(N-glycyl-L-cysteinyl)acetyl-D-alanyl-D-alanine
Streptomyces sp. R61
-
-
0.25
3-(N-acetyl-L-cysteinyl)propanoyl-D-alanyl-D-alanine
Streptomyces sp. R61
-
-
2.4
3-(N-glycyl-cysteaminyl)propanoyl-D-alanyl-D-alanine
Streptomyces sp. R61
-
-
42
3-(N-glycyl-L-cysteinyl)-propanoyl-D-alanyl-D-thiolactate
Streptomyces sp. R61
-
-
0.27
3-(N-glycyl-L-cysteinyl)butanoyl-D-alanyl-D-alanine
Streptomyces sp. R61
-
-
48
3-(N-glycyl-L-cysteinyl)propanoyl-D-alanyl-D-alanine
Streptomyces sp. R61
-
-
6.9
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
Streptomyces sp.
-
pH 7.5, 25C
10.4
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
Actinomadura sp.
-
pH 7.5, 25C
4
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
Streptomyces sp.
-
pH 7.5, 25C
114
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
Actinomadura sp.
-
pH 7.5, 25C
44
3-carboxyphenyl N-(phenylacetyl)-alpha-methoxyglycinate
Streptomyces sp. R61
-
-
106
3-carboxyphenyl N-(phenylacetyl)-alpha-methoxyglycinate
Neisseria gonorrhoeae
-
-
114
3-carboxyphenyl N-(phenylacetyl)-alpha-methoxyglycinate
Actinomadura sp. R39
-
-
0.65
3-carboxyphenyl N-(phenylacetyl)-alpha-serinate
Actinomadura sp. R39
-
-
2.2
3-carboxyphenyl N-(phenylacetyl)-alpha-serinate
Streptomyces sp. R61
-
-
22
3-carboxyphenyl N-(phenylacetyl)-alpha-serinate
Neisseria gonorrhoeae
-
-
31
3-[[N-(phenylacetyl)-D-alanyl]oxy]benzoic acid
Streptomyces sp. R61
-
-
1.51
3-[[N-(phenylacetyl)glycyl]oxy]benzoic acid
Streptomyces sp. R61
-
-
12.5
acetyl-L-Lys-D-Ala-D-Ala
Nonomuraea sp.
-
pH 7.4, 25C
-
0.11
benzoyl-D-Ala-thioglycolate
Streptomyces sp.
P39042
pH 7.2, 37C, wild-type enzyme
0.3
benzoyl-D-Ala-thioglycolate
Streptomyces sp.
P39042
pH 7.2, 37C, mutant enzyme C98A
0.024
benzoyl-Gly-thioglycolate
Streptomyces sp.
P39042
above, pH 7.2, 37C, wild-type enzyme
0.08
benzoyl-Gly-thioglycolate
Streptomyces sp.
P39042
pH 7.2, 37C, mutant enzyme C98A
0.006
benzoyl-Gly-thiolactate
Streptomyces sp.
P39042
pH 7.2, 37C, mutant enzyme K38H
0.017
benzoyl-Gly-thiolactate
Streptomyces sp.
P39042
pH 7.2, 37C, wild-type enzyme
0.08
benzoyl-Gly-thiolactate
Streptomyces sp.
P39042
pH 7.2, 37C, mutant enzyme C98A
8.3
D-Ala-D-Ala
Nonomuraea sp.
-
pH 7.4, 25C
17.5
diacetyl-L-Lys-D-Ala-D-Ala
Streptomyces sp.
-
Streptomyces sp. R39
55
diacetyl-L-Lys-D-Ala-D-Ala
Streptomyces sp.
-
Streptomyces sp. R61
267
diacetyl-L-Lys-D-Ala-D-Ala
Streptomyces sp.
-
54000 MW enzyme
350
diacetyl-L-Lys-D-Ala-D-Ala
Streptomyces sp.
-
40000 MW enzyme
12.8
Gly-gamma-L-Glu-D-Ala-D-Ala
Streptomyces sp. R61
-
-
69
Gly-L-alpha-amino-epsilon-pimelyl-D-Ala-D-Ala
Streptomyces sp. R61
-
-
69
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine
Streptomyces sp. R61
-
-
48
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]amino]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
Streptomyces sp. R61
-
-
81
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
Streptomyces sp. R61
-
-
34.5
N,N'-diacetyl-L-lysyl-D-alanyl-D-alanine
Streptomyces sp. R61
-
-
0.9
N-(N-acetyl-1-O-methyl-beta-muramoyl)-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
Escherichia coli
-
pH 7.5, 25C
2.51
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant F160A
2.68
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant R361H
2.87
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant R361A
3.02
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant Q422S
3.13
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
wild type enzyme
3.18
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant Q422A
2.42
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant R361H
2.78
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant R361A
2.91
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant Q422A
2.97
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant Q422S
2.98
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant D155A
3.01
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
mutant F160A
3.47
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
Escherichia coli K-12
P24228
wild type enzyme
0.1
N-alpha-acetyl-L-Lys-D-Ala-thiolactate
Streptomyces sp.
P39042
pH 7.2, 37C, wild-type enzyme
0.8
N-alpha-acetyl-L-Lys-D-Ala-thiolactate
Streptomyces sp.
P39042
pH 7.2, 37C, mutant enzyme C98A
69
N-[(6S)-6-carboxy-6-(glycylamino)hexanoyl]-D-alanyl-D-alanine
Streptomyces sp. R61
-
-
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
Escherichia coli
-
pH 7.5, 25C
0.2
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
Streptomyces sp.
P39042
above, pH 7.2, 37C, mutant enzyme C98A
0.3
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
Streptomyces sp.
P39042
pH 7.2, 37C, wild-type enzyme
0.56
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
Escherichia coli
-
recombinant PBP 6, in 50 mM Tris-HCl, pH 8.5, at 37C
2.7
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
Escherichia coli
-
recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37C
0.43
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate
Streptomyces sp.
P39042
above, pH 7.2, 37C, wild-type enzyme
1.1
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate
Streptomyces sp.
P39042
pH 7.2, 37C, mutant enzyme C98A
0.13
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala
Streptomyces sp.
P39042
pH 7.2, 37C, mutant enzyme C98A
0.45
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala
Streptomyces sp.
P39042
pH 7.2, 37C, wild-type enzyme
0.015
phenylacetyl-D-Ala-thioglycolate
Streptomyces sp.
P39042
pH 7.2, 37C, mutant enzyme K38H
0.5
phenylacetyl-D-Ala-thioglycolate
Streptomyces sp.
P39042
above, pH 7.2, 37C, wild-type enzyme
0.87
phenylacetyl-D-Ala-thioglycolate
Streptomyces sp.
P39042
above, pH 7.2, 37C, mutant enzyme C98A
6.08
phenylacetyl-D-Ala-thioglycolate
Streptomyces sp.
P39042
above, pH 7.2, 37C, mutant enzyme C98A
0.6
phenylacetyl-D-Ala-thiolactate
Streptomyces sp.
P39042
pH 7.2, 37C, wild-type enzyme
2.2
phenylacetyl-D-Ala-thiolactate
Streptomyces sp.
P39042
pH 7.2, 37C, mutant enzyme C98A
1.41
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala
Escherichia coli
-
recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37C
additional information
additional information
Escherichia coli
-
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
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
Streptomyces sp.
-
pH 7.5, 25C
199236
24
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
Actinomadura sp.
-
pH 7.5, 25C
199236
98
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
Streptomyces sp.
-
pH 7.5, 25C
199237
570
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
Actinomadura sp.
-
pH 7.5, 25C
199237
1.56
acetyl-L-Lys-D-Ala-D-Ala
Nonomuraea sp.
-
pH 7.4, 25C
202289
0.415
D-Ala-D-Ala
Nonomuraea sp.
-
pH 7.4, 25C
1348
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00037
(2R)-2-amino-7-oxo-7-[(4,4,4-trifluoro-3-oxobutan-2-yl)amino]heptanoic acid
-
pH not specified in the publication, temperature not specified in the publication
1.02
3-(N-glycyl-L-cysteinyl)-N-ethylpropionamide
-
-
0.013
Boc-gamma-D-Glu-L-Lys-(Cbz)-D-boroAla-(-)-pinanediol
-
-
15.5
D-alpha-phenylpropionate
-
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
7
D-hexahydromandelate
-
substrate glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
11.6
D-mandelate
-
substrate (2R)-2-[[N-(phenylacetyl)glycyl]sulfanyl]propanoic acid; substrate 3-[[N-(phenylacetyl)-D-alanyl]oxy]benzoic acid; substrate 3-[[N-(phenylacetyl)glycyl]oxy]benzoic acid; substrate glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
17.8
D-phenyllactate
-
substrate glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
19.3
glycolyl-L-Phe
-
substrate glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
additional information
additional information
-
Ki 6-beta(D-alpha-aminopimelyl)-aminopenicillanic acid, 6800000 s-1 * M-1; Ki 6-beta(D-alpha-aminosuberyl)-aminopenicillanic acid, 2850000 s-1 * M-1; Ki 7-beta(D-alpha-aminopimelyl)-aminocephalosporanic acid, 11000000 s-1 * M-1; Ki benzylpenicillin, 300000 s-1 * M-1; Ki cephalothin, 65000 s-1 * M-1
-
additional information
additional information
-
Ki 6-beta(alpha-N-acetyl-L-lysyl)-aminopenicillanic acid, 12000 s-1 * M-1; Ki 6-beta(alpha-N-acetyl-L-lysyl)-aminopenicillanic acid, 3900 s-1 * M-1; Ki 6-beta(alpha-N-acetyl-L-lysyl)-aminopenicillanic acid, 95 s-1 * M-1; Ki 7-beta(alpha-N-acetyl-L-lysyl)-aminocephalosporanic acid, 34 s-1 * M-1; Ki benzylpenicillin, 13000 s-1 * M-1; Ki benzylpenicillin, 30000 s-1 * M-1; Ki cephalothin, 91000 s-1 * M-1
-
additional information
additional information
-
Ki (5R,6R)-6-[[(6S)-6-carboxy-6-(glycylamino)hexanoyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid, 15000000 s-1 * M-1; Ki (6R,7R)-3-[(acetyloxy)methyl]-7-[(6S)-6-carboxy-6-(glycylamino)hexanoyl]amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, 560000 s-1 * M-1; Ki benzylpenicillin, 13700 s-1 * M-1; Ki cephalothin, 1400 s-1 * M-1
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
28
(3R,5R)-3-(furyl-2')-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
1
(3R,5R,6R)-6-methyl-3-(furyl-2')-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
25
(3R,5R,6S)-6-methyl-3-(furyl-2')-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
6.6
(3R,5S)-3-(furyl-2')-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
4.5
(3R,5S,6R)-3-benzyloxycarbonyl-6-methyl-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
3.4
(3R,5S,6R)-6-methyl-3-(furyl-2')-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
1.3
(3S,5R)-3-(furyl-2')-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
16
(3S,5R,6S)-3-benzyloxycarbonyl-6-methyl-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
5.4
(3S,5R,6S)-6-methyl-3-(furyl-2')-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
3
(3S,5S,6R)-6-methyl-3-(furyl-2')-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
1
3-(acetylamino)-5-(dihydroxyboranyl)benzoic acid
Actinomadura sp. R39
-
in 10 mM sodium phosphate buffer (pH 7.2) with 100 mM NaCl, 100 mM D-alanine, and 0.01 mg/ml bovine serum albumin for 60 min at 25C
0.034
3-(benzoylamino)-5-(dihydroxyboranyl)benzoic acid
Actinomadura sp. R39
-
in 10 mM sodium phosphate buffer (pH 7.2) with 100 mM NaCl, 100 mM D-alanine, and 0.01 mg/ml bovine serum albumin for 60 min at 25C
0.028
3-(dihydroxyboranyl)-5-[(phenoxyacetyl)amino]benzoic acid
Actinomadura sp. R39
-
in 10 mM sodium phosphate buffer (pH 7.2) with 100 mM NaCl, 100 mM D-alanine, and 0.01 mg/ml bovine serum albumin for 60 min at 25C
0.078
3-(dihydroxyboranyl)-5-[(thiophen-2-ylacetyl)amino]benzoic acid
Actinomadura sp. R39
-
in 10 mM sodium phosphate buffer (pH 7.2) with 100 mM NaCl, 100 mM D-alanine, and 0.01 mg/ml bovine serum albumin for 60 min at 25C
0.032
3-(dihydroxyboranyl)-5-[(thiophen-2-ylcarbonyl)amino]benzoic acid
Actinomadura sp. R39
-
in 10 mM sodium phosphate buffer (pH 7.2) with 100 mM NaCl, 100 mM D-alanine, and 0.01 mg/ml bovine serum albumin for 60 min at 25C
0.023
3-(dihydroxyboryl)-5-(2-methoxybenzamido)benzoic acid
Actinomadura sp. R39
-
in 10 mM sodium phosphate buffer (pH 7.2) with 100 mM NaCl, 100 mM D-alanine, and 0.01 mg/ml bovine serum albumin for 60 min at 25C
0.088
3-(dihydroxyboryl)-5-(2-phenylacetamido)benzoic acid
Actinomadura sp. R39
-
in 10 mM sodium phosphate buffer (pH 7.2) with 100 mM NaCl, 100 mM D-alanine, and 0.01 mg/ml bovine serum albumin for 60 min at 25C
0.4
3-(dihydroxyboryl)benzoic acid
Actinomadura sp. R39
-
in 10 mM sodium phosphate buffer (pH 7.2) with 100 mM NaCl, 100 mM D-alanine, and 0.01 mg/ml bovine serum albumin for 60 min at 25C
0.06
ampicillin
Corynebacterium jeikeium
-
-
0.5
phenylboronic acid
Actinomadura sp. R39
-
in 10 mM sodium phosphate buffer (pH 7.2) with 100 mM NaCl, 100 mM D-alanine, and 0.01 mg/ml bovine serum albumin for 60 min at 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
Nonomuraea sp.
-
substrate Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala , pH 7.4, 25C
18
Nonomuraea sp.
-
substrate D-Ala-D-Ala, pH 7.4, 25C
40
Nonomuraea sp.
-
substrate acetyl-L-Lys-D-Ala-D-Ala, pH 7.4, 25C
additional information
-
assay method
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4
-
vegetative and stage-V forespore membrane DD-carboxypeptidase
6
-
sodium cacodylate buffer
6 - 8
-
hydrolysis, value increased by high ionic strength
7
-
sodium barbital buffer
7.5
-
kinetic measurements
7.5
-
kinetic assay
7.6
activity assay
7.7
-
kinetic assay
8
-
transpeptidation, Streptomyces sp. R61
8
-
DD-carboxypeptidase activity assay
8.5
-
kinetic assay
9.5
-
transpeptidation, Streptomyces sp. R39
additional information
-
ratio of hydrolysis/transpeptidation depending on pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6 - 8.9
-
effectiveness of D-alanine as an acceptor increases with pH
8 - 11
-
pH 8: about 50% of maximal activity, pH 11: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
kinetic measurements
37
-
assay at
37
-
DD-carboxypeptidase activity assay
37
activity assay
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
during endospore development in Bacillus megaterium strain KM, unique sporulation-specific penicillin-binding proteins are synthesized and inserted into the forespore membranes, vegetative and stage-V forespore membrane DD-carboxypeptidase, penicillin-binding profile, overview
Manually annotated by BRENDA team
additional information
Bacillus megaterium KM
-
during endospore development in Bacillus megaterium strain KM, unique sporulation-specific penicillin-binding proteins are synthesized and inserted into the forespore membranes, vegetative and stage-V forespore membrane DD-carboxypeptidase, penicillin-binding profile, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
loosely associated with the cell membrane
-
Manually annotated by BRENDA team
-
PBP3 is evenly distributed on both hemispheres but absent at the equator, the site of future division
Manually annotated by BRENDA team
-
GFP-PBP5 localizes to the septum and in concentrated spots along the lateral wall
Manually annotated by BRENDA team
Nonomuraea sp.
-
enzyme preferentially accumulates in the cell wall fractions obtained by the step of spheroplast preparation
Manually annotated by BRENDA team
mutant enzyme S96A is produced in cytoplasm of Escherichia coli
Manually annotated by BRENDA team
-
anchored into the outer leaflet of the cytoplasmic membrane
-
Manually annotated by BRENDA team
mutant enzymes K38H, C98A and C98N are produced in culture medium of Streptomyces lividans
-
Manually annotated by BRENDA team
Streptomyces sp. R39
-
;
-
-
Manually annotated by BRENDA team
-
lysozyme releasable
Manually annotated by BRENDA team
-
membrane-bound, the active site is present on the outside surface of the membrane
Manually annotated by BRENDA team
-
membrane anchoring
Manually annotated by BRENDA team
-
localized in the outer leaflet of the cytosolic membrane
Manually annotated by BRENDA team
Bacillus megaterium KM
-
-
-
Manually annotated by BRENDA team
Enterococcus faecium BM4339
-
membrane-bound, the active site is present on the outside surface of the membrane
-
Manually annotated by BRENDA team
Streptomyces sp. R39
-
-
-
Manually annotated by BRENDA team
Nonomuraea sp.
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Actinomadura sp. (strain R39)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Pseudomonas aeruginosa (strain UCBPP-PA14)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Streptomyces sp. (strain K15)
Streptomyces sp. (strain K15)
Streptomyces sp. (strain K15)
Streptomyces sp. (strain K15)
Streptomyces sp. (strain K15)
Streptomyces sp. (strain K15)
Streptomyces sp. (strain K15)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Streptomyces sp. (strain R61)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
-
determined by SDS-PAGE
683065
27000
-
gel filtration
36307
39000
-
purified recombinant PBP 6
708523
40000
-
purified recombinant PBP 5
708523
40800
-
-
701353
41300
-
-
701353
43000
-
-
701353
49600
-
-
701353
53000
-
gel filtration + mercaptoethanol, SDS-PAGE
28888, 36281
53000
-
microdensitometry
36287
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 43000, SDS-PAGE
?
-
x * 46500, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
Nonomuraea sp.
-
x * 25000, SDS-PAGE of His-tagged protein, x * 22100, calculated for native protein
?
Nonomuraea sp.
-
x * 25000, SDS-PAGE
?
Enterococcus faecium BM4147
-
x * 35000, SDS-PAGE
-
monomer
Streptomyces pneumoniae
-
multiwavelength anomalous diffraction
additional information
-
enzyme peptide mapping
additional information
-
PBP1b structure analysis, overview
additional information
Bacillus megaterium KM
-
enzyme peptide mapping
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by hanging drop vapor diffusion, at 1.8 A and 2.4 A resolution, R39 structure is composed of one penicillin binding domain and two unknown domains, the R39 active site does not undergo a great structural deformation upon beta-lactam binding
-
in complex with inhibitor (2R)-2-amino-7-oxo-7-[(4,4,4-trifluoro-3-oxobutan-2-yl)amino]heptanoic acid. The inhibitor is covalently bonded to the active serine Ser49, the carbonyl carbon is now tetrahedral, and the ketone oxygen occupies the oxyanion hole, defined by the backbone NH groups of Ser49 and Thr413. The D-methyl group is directed into a hydrophobic pocket comprised residues Gly148, Leu 349 and Met414. Branching from the tetrahedral carbon bonded to Ser49Ogamma, the CF3 group occupies the likely position of a leaving group in the tetrahedral intermediate of a peptidase substrate
-
the structure of the R39 DD-peptidase bound to cephalosporin is refined to 2.4 A and the structure with a further peptidoglycan-mimetic ligand is refined to 2.25 A
-
the crystal structure of the protein alone is solved at a resolution of 2.1 A, and in complex with D-alpha-aminopymelyl-eta-D-alanyl-D-alanine at a resolution of 2.8 A
crystal structures of VanXY mutant D59S and VanXY wild-type in apo and transition state analog-bound forms and of the mutant in complex with the D-Ala-D-Ala substrate and D-Ala product. Structural and biochemical analysis identifies the molecular determinants of VanXY dual specificity acting on dipeptide D-Ala-D-Ala or pentapeptide UDP-MurNac-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala, respectively. VanXY residues 110-115 form a mobile cap over the catalytic site, whose flexibility is involved in the switch between di- and pentapeptide hydrolysis. VanY pentapeptidases lack this element, which promotes binding of the penta- rather than that of the dipeptide
-
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
-
the structure in complex with cephalosporin is refined to 1.6 A and with penicillin to 2.0 A
the crystal structures of native D-amino acid amidase and of the D-phenylalanine/D-amino acid amidase complex are determined at 2.1 and at 2.4 A resolution, respectively
purified Pbp1b in complex with N-benzoyl-D-Ala or pseudo-substrate N-benzoyl-D-alanylmercaptoacetic acid thioester, hanging drop vapor diffusion method, mixing of 0.001 ml of 6-10 mg/ml protein and 5 mM N-benzoyl-D-alanylmercaptoacetic acid thioester, with 0.001 ml of well solution containing 50 mM HEPES, pH 7.0, 0.8 M (NH4)2SO4, 2.8 M NaCl at 15C, X-ray difraction structure determination and analysis at 2.5 A resolution, molecular replacement
-
by hanging drop vapor diffusion, to 2.8 A resolution, PBP3 folds into an NH2-terminal,D,D-carboxypeptidase-like domain and a COOH-terminal, elongated beta-rich region
Streptomyces pneumoniae
-
1.2 A resolution X-ray structure of cephalosporin bound to the active site of the bifunctional serine type D-alanyl-D-alanine carboxypeptidase/transpeptidase
characterization of the noncovalent interactions based on cocrystallized structures of benzylpenicillin and perfect penicillin covalently bound to DD-peptidase by computational methods. Benzylpenicillins phenyl group forms an extended pi?pi network with Phe120 and Trp233 that contributes significantly to its efficacy in DD-peptidase. This aromatic stabilization is conserved in beta-lactamases. Interactions between the protein and the peptidomimetic tail region, particularly carboxylate 2 and the terminal N4H3+ unit, form unique hydrogen bonding and strong electrostatic interactions. Between Asp217 and the N4H3+ there is a water mediated salt bridge
-
hanging drop vapor diffusion method. Mutant enzymes S96A, K38H, C98A and C98N are produced in culture medium of Streptomyces lividans
hanging drop vapor diffusion, crystal structure of the phosphonal enzyme. The 1.1 A resolution structure of the enzyme in complex with phenyl glycyl-L-alpha-aminopimelyl-epsilon-(D-2-aminoethyl)phosphonate shows that the inhibitor is phosphorylated by the catalytic Ser62
-
X-ray structure, the energetically most stable configuration has a neutral Lys213 residue, the K15 active site is characterized by a dense hydrogen-bonding network that interconnects the catalytically relevant residues and some solvent molecules, the hydroxyl group of the nucleophilic serine (Ser35) is located in the oxy-anion-hole formed by the backbone NH groups of Ser35 and Ser216
-
by hanging drop vapor diffusion, to 1.1 A resolution
-
by hanging-drop, vapor-diffusion method, to 1.5 A resolution, X-ray structure of non-covalent and covalent complexes of beta-lactams with DD-peptidase
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
inactivation above
36296
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 4.6C
653782
50
-
10 min
36307
60
half-lives: 120 min for mutant S96A, 220 min for mutant C98A, 30 min for mutant C98N and 170 min for the wild-type enzyme
650206
72
half-lives: 3.5 min for mutant K38H, 8 min for mutant S96A, 6 min for mutant C98A, 13 min for mutant enzyme C98A and 10 min for the wild-type enzyme
650206
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 4.6C
-
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
-20C, Tris-HCl buffer, pH 7.5, 0.7% CHAPS, 0.5 M NaCl
-
4C, purified enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using a Heparin-Sepharose CL-6B column
by RNA purification kit
-
ampicillin-affinity chromatography
-
ampicillin-coupled activated CH-Sepharose 4B resin column chromatography
-
ampicillin/CH-Sepharose 4B resin column chromatography
-
using an amylose affinity column, the MBP-tag is removed by factor Xa cleavage
-
using Ni-NTA affinity chromatography
-
-
Streptomyces pneumoniae
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coliDH5alpha
-
a soluble fragment of Pbp4 lacking the putative membrane anchor of the protein is expressed in Escherichia coli
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21 Star cells
-
expressed in Escherichia coli BL21(DE3) cells
-
for expression in Escherichia coli BL21DE3 cells
-
into the pMAL-c2X vector for expression in Escherichia coli JM109 cells
-
membrane anchor of the protein is removed and the enzyme is obtained as a soluble protein
-
overexpression of truncated enzyme
-
into the vector pET21b
expression in Escherichia coli
-
expression in Escherichia coli
Nonomuraea sp.
-
expression in Streptomyces spp.
Nonomuraea sp.
-
into the pET15b vector for expression in Escherichia coli cells
expression in Escherichia coli MC1061
-
mutant enzyme S96A is produced in cytoplasm of Escherichia coli. Mutant enzymes K38H, C98A and C98N are produced in culture medium of Streptomyces lividans
overexpression in Streptomyces lividans
-
ENGINEERING
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
-
mutation markedly impairs the beta-lactamase activity, with only minor effects on acylation, and promotes accumulation of a covalent complex with peptide substrates
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
D155A
mutant, constructed for the demonstration of the relative importance of residue Asp155
F160A
mutant, constructed for the demonstration of the relative importance of residue Phe160
Q422A
mutant, constructed for the demonstration of the relative importance of residue Gln422
Q422S
mutant, constructed for the demonstration of the relative importance of residue Gln422
R361A
mutant, constructed for the demonstration of the relative importance of residue Arg361
C98A
half-life at 72C increases to 13 min, compared to 10 min for the wild-type enzyme. Half-life at 60C increases to 220 min compared to 170 min for the wild-type enzyme. The value of the second-order acylation rate constant is not very different from those of the wild-type enzyme with the exception of the cephalotin, oxacillin and piperacillin values which are increased 5-10fold
C98N
half-life at 72C decreases to 6 min, compared to 10 min for the wild-type enzyme. Half-life at 60C decreases to 30 min compared to 170 min for the wild-type enzyme. The acylation rate constants by most of the beta-lactams are increased 10-70fold compared to the wild-type enzyme. The deacylation rate constant values als increases
K38H
half-life at 72C decreases to 3.5 min, compared to 10 min for the wild-type enzyme. The mutant enzyme fails to bind beta-lactams
S96A
half-life at 72C decreases to 8 min, compared to 10 min for the wild-type enzyme. Half-life at 60C decreases to 120 min compared to 170 min for the wild-type enzyme. The mutant enzyme is inactive in terms of beta-lactam binding with the exception of cefoxitin, for which a residual activity is detected.The value of the second-order acylation rate constant is decreased by a factor of 3000, and that of the deacylation rate constant is decreased 120fold
W271L
-
exchanging of tryptophan 271 shows no particular modification of the proteins biophysical and kinetic charcteristics
G105D
-
mutation markedly impairs deacylation with only minor effects on acylation, and abolishes D-alanine carboxypeptidase activity
additional information
-
truncated forms of the enzyme
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
R361H
mutant, constructed for the demonstration of the relative importance of residue Arg361
additional information
Nonomuraea sp.
-
the addition of His6-tag at the N-terminus of the protein abolishes its biological activity either in vitro or in vivo assays. The addition of His6-tag at the C-terminus of the protein leads to a functional protein
additional information
-
PBP3 mutant, rings of high-molecular-weight PBPs and that of FtsZ are no longer co-localized, the co-ordination is necessary for membrane invagination
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
bacterial DD-peptidases are still an enticing target for antibacterial agents
medicine
-
Brucella spp. cause abortion in domestic animals and undulant fever in humans, DAP contributes to resistance against NO, which is required for the intracellular growth of the bacterium
medicine
-
bacterial DD-peptidases are still an enticing target for antibacterial agents
medicine
-
PBP1b could be a target for antibacterial agents
medicine
-
VanX, being a required enzyme for bacterial antibiotic resistance, should be a key target in circumventing clinical vancomycin resistance
medicine
-
bacterial DD-peptidases are still an enticing target for antibacterial agents
synthesis
Nonomuraea sp.
-
highest yield of protein expression and purification from 12 mg of protein per liter of culture at 3 l bioreactor-scale is achieved in Streptomyces venezuelae ATCC 10595, a fast growing Streptomyces susceptible to glycopeptides. The addition of His6-tag at the N-terminus of the protein abolishes its biological activity either in vitro or in vivo assays. The addition of His6-tag at the C-terminus of the protein leads to a functional protein
medicine
-
bacterial DD-peptidases are still an enticing target for antibacterial agents
medicine
-
clinical defense against bacterial infections, DD-peptidases are the killing targets of beta-lactams
medicine
-
DD-peptidases are targets for antibiotic designs
medicine
-
bacterial DD-peptidases are still an enticing target for antibacterial agents