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Information on EC 3.4.16.4 - serine-type D-Ala-D-Ala carboxypeptidase
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3.4.16.4 serine-type D-Ala-D-Ala carboxypeptidaseSpecify your search results
Word Map
- 3.4.16.4
- peptidoglycan
- beta-lactams
- aureus
- staphylococcus
- streptococcus
- pneumonia
-
methicillin-resistant
- cephalosporin
- gg
-
penicillin-resistant
- methicillin
- ampicillin
- bilirubin
- cefotaxime
-
gamma-glutamyl
- vancomycin
-
sortase
-
transpeptidation
- oxacillin
- imipenem
-
penicillin-susceptible
- transglycosylase
- ceftriaxone
-
pneumococci
- faecium
- carbapenems
- benzylpenicillin
- muropeptides
- murein
- ceftazidime
- cefoxitin
-
methicillin-susceptible
- meropenem
- acyl-enzyme
-
lpxtg
-
cephems
-
ampicillin-resistant
- cefixime
- cefuroxime
- piperacillin
-
mic90s
-
vancomycin-resistant
- penicillinase
- aztreonam
- cefaclor
- sulbactam
-
beta-lactamase-negative
-
sccmec
- nitrocefin
- analysis
- synthesis
- medicine
-
beta-lactamase-producing
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
Synonyms
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, D-alanine carboxypeptidase, D-alanine carboxypeptidase I, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxypeptidase I
-
-
-
-
CPase
-
-
-
-
D-alanine carboxypeptidase
D-alanine carboxypeptidase I
-
-
-
-
D-alanyl carboxypeptidase
-
-
-
-
D-alanyl-D-alanine carboxypeptidase
D-Alanyl-D-alanine hydrolase
-
-
-
-
D-alanyl-D-alanine peptidase
-
-
-
-
D-alanyl-D-alanine transpeptidase
D-alanyl-D-alanine-carboxypeptidase
D-alanyl-D-alanine-cleaving peptidase
-
-
-
-
D-alanyl-D-alanine-cleaving-peptidase
-
-
-
-
DacA-1
DacB
Dbv7
DD-Carboxypeptidase
DD-CPase
DD-CPase1
DD-peptidase
DD-transpeptidase
PBP
PBP 5
PBP 6
-
the DD-carboxypeptidase activity of PBP 6 is lower than that of PBP 5
PBP-5*
-
-
-
-
PBP-6B
-
-
-
-
PBP1b
PBP3
PBP4
PBP4a
PBP5
penicillin binding protein 5
penicillin-binding protein
penicillin-binding protein 5
penicillin-binding protein 5a
SCO4439
transpeptidase
VanX
VanY
-
-
-
-
VanY(D) DD-carboxypeptidase
VanYD
VanYn
VC_0947
D-alanine carboxypeptidase
-
-
-
-
D-alanyl-D-alanine carboxypeptidase
-
-
-
-
D-alanyl-D-alanine-carboxypeptidase
-
-
-
-
DD-Carboxypeptidase
-
-
-
-
DD-peptidase
-
-
-
-
DD-peptidase
-
-
DD-transpeptidase
-
-
-
-
PBP 5
-
the DD-carboxypeptidase activity of PBP 5 is higher than that of PBP 6
PBP5
-
-
-
-
penicillin binding protein 5
-
-
-
-
VanX
-
-
-
-
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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
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
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
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of peptide bond
transpeptidation
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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CAS REGISTRY NUMBER
COMMENTARY
9077-67-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2R)-2-[[N-(phenylacetyl)glycyl]sulfanyl]propanoic acid + H2O
?
-
-
-
-
?
(R)-[2-(benzoylamino)propionylsulfanyl]acetic acid + H2O
?
-
-
-
?
2-(N-glycyl-L-cysteinyl)acetyl-D-alanyl-D-alanine + H2O
2-(N-glycyl-L-cysteinyl)acetyl-D-alanine + D-alanine
-
-
-
-
?
3-(N-acetyl-L-cysteinyl)propanoyl-D-alanyl-D-alanine + H2O
3-(N-acetyl-L-cysteinyl)propanoyl-D-alanine + D-alanine
-
-
-
-
?
3-(N-glycyl-cysteaminyl)propanoyl-D-alanyl-D-alanine + H2O
3-(N-glycyl-cysteaminyl)propanoyl-D-alanine + D-alanine
-
-
-
-
?
3-(N-glycyl-L-cysteinyl)-propanoyl-D-alanyl-D-thiolactate + H2O
3-(N-glycyl-L-cysteinyl)-propanoyl-D-alanine + D-thiolactate
-
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
-
-
-
-
?
3-(N-glycyl-L-cysteinyl)propanoyl-D-alanyl-D-alanine + H2O
3-(N-glycyl-L-cysteinyl)propanoyl-D-alanine + D-alanine
-
-
-
-
?
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate + H2O
(2R)-N-(phenylacetyl)-2-hydroxyglycine + 3-hydroxybenzoate
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
(2R)-N-(phenylacetyl)-2-methoxyglycine + 3-hydroxybenzoate
Ac2-L-Lys-D-Ala-Gly-L-Ala
?
-
poor substrate, but hydrolysis was significant
-
-
?
Ac2-L-Lys-D-Ala-Gly-L-Gln
?
-
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 + ?
-
transpeptidation
-
-
r
Ac2-L-Lys-D-Ala-Gly-L-Leu
?
-
poor substrate, but hydrolysis was significant
-
-
?
Ac2-L-Lys-D-Ala-Gly-L-Leu + D-alanine
Ac2-L-Lys-D-Ala-D-Ala + ?
-
transpeptidation
-
-
r
acetyl-L-Ala-D-Glu-L-Lys(Ac)-D-Ala-D-Ala + H2O
acetyl-L-Ala-D-Glu-L-Lys(Ac)-D-Ala + D-Ala
-
-
-
-
?
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
-
-
-
-
?
Gly-gamma-L-Glu-D-Ala-D-Ala + H2O
Gly-gamma-L-Glu-D-Ala + D-Ala
-
-
-
?
Gly-L-alpha-amino-epsilon-pimelyl-D-Ala-D-Ala + H2O
Gly-L-alpha-amino-epsilon-pimelyl-D-Ala + D-Ala
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine + H2O
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine + D-alanine
-
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-leucine + H2O
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine + D-leucine
-
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-norleucine + H2O
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine + D-norleucine
-
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-glycine + H2O
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine + glycine
-
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-glycyl-L-alanine + H2O
?
-
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-glycyl-L-leucine + H2O
?
-
-
-
-
?
glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-glycyl-L-phenylalanine + H2O
?
-
-
-
-
?
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]amino]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine + H2O
?
-
-
-
-
?
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine + H2O
?
-
-
-
-
?
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O
?
-
only substrate of penicillin-binding protein 5, but not of penicillin-binding protein 6
-
-
?
N-(N-acetyl-1-O-methyl-beta-muramoyl)-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine + H2O
N-(N-acetyl-1-O-methyl-beta-muramoyl)-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanine + D-Ala
-
-
-
?
N-acetyl-L-Lys-D-Ala-D-Ala + H2O
N-acetyl-L-Lys-D-Ala + D-Ala
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
N-benzoyl-D-Ala + H2O
benzoate + D-Ala
-
substrate binding structure
-
-
?
N-[(6S)-6-carboxy-6-(glycylamino)hexanoyl]-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-alanyl-D-alanine + H2O
N-[N-acetyl-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-1-O-methyl-beta-muramoyl]-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanine + D-Ala
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
N,N'-diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-lactate + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-lactate
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + Gly
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate + H2O
?
-
-
?
Nalpha,Nepsilon-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
?
-
substrate in DD-carboxypeptidase activity assay
-
-
?
Nalpha,Nepsilon-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
D-alanine + Nalpha,Nepsilon-diacetyl-L-lysyl-D-alanine
Nalpha,Nepsilon-diacetyl-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-Lys-D-Ala + D-Ala
-
-
-
?
Nalpha,Neta-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
?
-
substrate for assay of DD-carboxypeptidase activity
-
-
?
Nalpha-(beta-1,4 acetylglucosaminyl-N-acetylmuramyl-L-alanyl-D-isoglutaminyl)-Nepsilon-(D-isoasparaginyl)L-Lys-D-Ala-D-Ala + H2O
Nalpha-(beta-1,4 acetylglucosaminyl-N-acetylmuramyl-L-alanyl-D-isoglutaminyl)-Nepsilon-(D-isoasparaginyl)L-Lys-D-Ala + D-Ala
-
-
-
-
?
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
-
-
-
-
?
Nalpha-acetyl-L-Lys-D-Ala-D-Ala + H2O
?
substrate is used to detect the hydrolyzing activity of PBP4a
-
-
?
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha-Acetyl-L-Lys-D-Ala + D-Ala
-
-
?
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala + D-Ala
-
-
-
?
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
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate + H2O
(2R)-N-(phenylacetyl)-2-hydroxyglycine + 3-hydroxybenzoate
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-hydroxyglycinate + H2O
(2R)-N-(phenylacetyl)-2-hydroxyglycine + 3-hydroxybenzoate
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
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
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
?
-
-
-
-
?
3-carboxyphenyl N-(phenylacetyl)-alpha-methoxyglycinate + H2O
?
-
-
-
-
?
3-carboxyphenyl N-(phenylacetyl)-alpha-methoxyglycinate + H2O
?
-
-
-
-
?
acetyl-L-Lys-D-Ala-D-Ala + H2O
acetyl-L-Lys-D-Ala + D-Ala
-
-
-
?
acetyl-L-Lys-D-Ala-D-Ala + H2O
acetyl-L-Lys-D-Ala + D-Ala
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala
-
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
-
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
Priestia megaterium KM / ATCC 13632
-
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
-
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
-
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
-
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
-
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
-
acceptors in transpeptidase reaction
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
substrate mimics the terminal portions of the peptidoglycan pentapeptide precursors
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
substrate mimics the terminal portions of the peptidoglycan pentapeptide precursors
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
D-alanine + Nalpha,Nepsilon-diacetyl-L-lysyl-D-alanine
-
-
-
-
?
Nalpha,Nepsilon-diacetyl-L-lysyl-D-alanyl-D-alanine + H2O
D-alanine + Nalpha,Nepsilon-diacetyl-L-lysyl-D-alanine
-
-
-
-
?
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
-
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
D-Ala + UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala
Priestia megaterium KM / ATCC 13632
-
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
-
-
-
?
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
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
Priestia megaterium KM / ATCC 13632
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
28888, 36276, 36277, 36278, 36279, 36280, 36281, 36282, 36283, 36284, 36285, 36286, 36287, 36289, 36290, 36291, 36297, 36301, 36302, 36303, 36304
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
Priestia megaterium KM / ATCC 13632
-
-
-
-
?
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
-
-
28888, 36276, 36277, 36278, 36279, 36280, 36281, 36282, 36283, 36284, 36285, 36286, 36287, 36289, 36290, 36291, 36297, 36301, 36302, 36303, 36304
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
?
-
-
penicillin-binding protein
-
?
additional information
?
-
-
forms a covalent acyl-enzyme complex with beta-lactam antibiotics, high rate of decylation of the acyl-enzyme complex. Direct role for the SXN motif in deacylation of the acyl-enzyme complex. Functioning of this motif is modulated by the 74-90 loop. Ser86 and Ser87 are important for D-alanine carboxypeptidase activity
-
?
additional information
?
-
-
the enzyme forms a covalent acyl-enzyme complex with beta-lactam antibiotics
-
?
additional information
?
-
-
enzyme removes the terminal D-alanine from the pentapeptide side chains of muramic acid in peptidoglycan
-
-
?
additional information
?
-
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
?
-
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
?
-
-
low molecular mass PBPs can exert carboxypeptidase and/or endopeptidase activities and play auxiliary roles in the peptidoglycan metabolism process
-
-
?
additional information
?
-
-
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
?
-
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 is responsible for the final peptidoglycan cross-linking step in bacterial cell wall biosynthesis
-
?
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
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
D-Ala + UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala
Priestia megaterium KM / ATCC 13632
-
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
-
-
-
?
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
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
Priestia megaterium KM / ATCC 13632
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
28888, 36276, 36277, 36278, 36279, 36280, 36281, 36282, 36283, 36284, 36285, 36286, 36287, 36289, 36290, 36291, 36297, 36301, 36302, 36303, 36304
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
-
-
-
-
?
additional information
?
-
-
enzyme removes the terminal D-alanine from the pentapeptide side chains of muramic acid in peptidoglycan
-
-
?
additional information
?
-
-
low molecular mass PBPs can exert carboxypeptidase and/or endopeptidase activities and play auxiliary roles in the peptidoglycan metabolism process
-
-
?
additional information
?
-
the enzyme is responsible for the final peptidoglycan cross-linking step in bacterial cell wall biosynthesis
-
?
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
Zn2+
presence of 8 mM Zn2+ restores the activity of EDTA-treated enzyme
Zn2+
-
tetrahedrally coordinated by two histidines, an aspartate, and a water molecule
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2,3)-alpha-methylene benzylpenicillin
-
modeling of enzyme-inhibitor complex
(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
(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-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
-
-
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
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(N-acetyl-L-alanyl-gamma-D-glutamyl-L-alanyl)-aminopenicillanic acid
-
-
alpha-N-glycyl-epsilon-N-acetyl-L-lysine
-
inhibits hydrolysis of 3-(N-glycyl-L-cysteinyl)-propanoyl-D-alanyl-D-thiolactate
Boc-gamma-D-Glu-L-Lys-(Cbz)-D-boroAla-(-)-pinanediol
effective inhibitor of the D-alanine CPase activity of PBP5
EDTA
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
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
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala-D-Ala
-
substrate inhibition above 30 mM
phenyl glycyl-L-alpha-aminopimelyl-epsilon-(D-2-aminoethyl)phosphonate
-
Vancomycin
-
vancomycin derivatives inhibit the glycosyl transferase activity
[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
ampicillin
-
complete inhibition at 0.57 mM, 95% inhibition at 0.285 mM
benzylpenicillin
-
IC50: 0.00002 mg/ml, inhibition of the enzyme influences production of peptidoglycan precursors internally
cephalosporin
with glycyl-L-alpha-amino-epsilon-pimelyl side-chain, this beta lactam might be a better antibiotic than a non-specific counterpart
penicillin
-
binds covalently to Ser36, Bacillus subtilis, Bacillus stearothermophilus
penicillin
-
binds covalently to Ser36, Bacillus subtilis, Bacillus stearothermophilus
penicillin
-
the enzyme is sensitive to inhibition, penicillin-binding profile during development of spores, overview
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
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
not inhibited by methyl 3-(dihydroxyboryl)-5-(2-phenylacetamido)benzoate
-
additional information
-
no inhibition: penicillin G, ampicillin, cephalosporin C
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
p-chloromercuribenzoate
-
stimulation of hydrolase reaction, no influence on transpeptidase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
-
1.38
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala
-
recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C
3.5
N-(N-acetyl-1-O-methyl-beta-muramoyl)-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.5, 25°C
0.0178 - 0.401
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
0.4
N-alpha-acetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37°C, 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, 25°C
12
Nalpha, Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
lysozyme releasable enzyme
1.45
Nalpha-(beta-1,4 acetylglucosaminyl-N-acetylmuramyl-L-alanyl-D-isoglutaminyl)-Nepsilon-(D-isoasparaginyl)L-Lys-D-Ala-D-Ala
-
-
0.6
Nalpha-acetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37°C, mutant enzyme C98A
1.4
UDP-N-acetylmuramyl-L-Ala-D-Glu-mesodiaminopimelyl-D-Ala-D-Ala
-
-
0.36
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
pH 7.5, 25°C
4.3
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
pH 7.5, 25°C
0.2
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
pH 7.5, 25°C
0.45
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
pH 7.5, 25°C
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
0.35
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
above, pH 7.2, 37°C, 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 37°C
6.2
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
pH 7.2, 37°C, 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 37°C
2
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37°C, mutant enzyme C98A
3
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate
above, pH 7.2, 37°C, wild-type enzyme
2.4
phenylacetyl-D-Ala-thioglycolate
pH 7.2, 37°C, mutant enzyme K38H
3
phenylacetyl-D-Ala-thioglycolate
above, pH 7.2, 37°C, mutant enzyme C98A
3
phenylacetyl-D-Ala-thioglycolate
above, pH 7.2, 37°C, wild-type enzyme
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
48
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]amino]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
-
-
81
glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
-
-
1.41
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala
-
recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C
0.9
N-(N-acetyl-1-O-methyl-beta-muramoyl)-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.5, 25°C
2.42 - 3.47
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
1.1
N-[N-acetyl-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-1-O-methyl-beta-muramoyl]-L-alanyl-D-gamma-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.5, 25°C
6.9
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
pH 7.5, 25°C
10.4
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
pH 7.5, 25°C
4
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
pH 7.5, 25°C
114
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
pH 7.5, 25°C
0.024
benzoyl-Gly-thioglycolate
above, pH 7.2, 37°C, wild-type enzyme
2.51
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant F160A
2.68
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant R361H
2.87
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant R361A
3.02
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant Q422S
3.13
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
wild type enzyme
3.18
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
mutant Q422A
2.42
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant R361H
2.78
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant R361A
2.91
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant Q422A
2.97
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant Q422S
2.98
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant D155A
3.01
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
mutant F160A
3.47
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine
wild type enzyme
0.1
N-alpha-acetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37°C, wild-type enzyme
0.8
N-alpha-acetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37°C, mutant enzyme C98A
0.2
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
above, pH 7.2, 37°C, mutant enzyme C98A
0.3
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
pH 7.2, 37°C, wild-type enzyme
0.56
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
recombinant PBP 6, in 50 mM Tris-HCl, pH 8.5, at 37°C
2.7
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C
0.43
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate
above, pH 7.2, 37°C, wild-type enzyme
1.1
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37°C, mutant enzyme C98A
0.13
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala
pH 7.2, 37°C, mutant enzyme C98A
0.015
phenylacetyl-D-Ala-thioglycolate
pH 7.2, 37°C, mutant enzyme K38H
0.5
phenylacetyl-D-Ala-thioglycolate
above, pH 7.2, 37°C, wild-type enzyme
0.87
phenylacetyl-D-Ala-thioglycolate
above, pH 7.2, 37°C, mutant enzyme C98A
6.08
phenylacetyl-D-Ala-thioglycolate
above, pH 7.2, 37°C, mutant enzyme C98A
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
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
pH 7.5, 25°C
24
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
pH 7.5, 25°C
98
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
pH 7.5, 25°C
570
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
pH 7.5, 25°C
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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
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
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
11.6
D-mandelate
-
substrate (2R)-2-[[N-(phenylacetyl)glycyl]sulfanyl]propanoic acid
11.6
D-mandelate
-
substrate 3-[[N-(phenylacetyl)-D-alanyl]oxy]benzoic acid
11.6
D-mandelate
-
substrate 3-[[N-(phenylacetyl)glycyl]oxy]benzoic acid
11.6
D-mandelate
-
substrate glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
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
-
additional information
additional information
-
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
-
additional information
additional information
-
Ki 6-beta(alpha-N-acetyl-L-lysyl)-aminopenicillanic acid, 12000 s-1 * M-1
-
additional information
additional information
-
Ki 6-beta(alpha-N-acetyl-L-lysyl)-aminopenicillanic acid, 3900 s-1 * M-1
-
additional information
additional information
-
Ki 6-beta(alpha-N-acetyl-L-lysyl)-aminopenicillanic acid, 95 s-1 * M-1
-
additional information
additional information
-
Ki 6-beta(D-alpha-aminopimelyl)-aminopenicillanic acid, 6800000 s-1 * M-1
-
additional information
additional information
-
Ki 6-beta(D-alpha-aminosuberyl)-aminopenicillanic acid, 2850000 s-1 * M-1
-
additional information
additional information
-
Ki 7-beta(alpha-N-acetyl-L-lysyl)-aminocephalosporanic acid, 34 s-1 * M-1
-
additional information
additional information
-
Ki 7-beta(D-alpha-aminopimelyl)-aminocephalosporanic acid, 11000000 s-1 * M-1
-
additional information
additional information
-
Ki benzylpenicillin, 13000 s-1 * M-1
-
additional information
additional information
-
Ki benzylpenicillin, 13700 s-1 * M-1
-
additional information
additional information
-
Ki benzylpenicillin, 30000 s-1 * M-1
-
additional information
additional information
-
Ki benzylpenicillin, 300000 s-1 * M-1
-
additional information
additional information
-
Ki cephalothin, 1400 s-1 * M-1
-
additional information
additional information
-
Ki cephalothin, 65000 s-1 * M-1
-
additional information
additional information
-
Ki cephalothin, 91000 s-1 * M-1
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.5
(3R,5S,6R)-3-benzyloxycarbonyl-6-methyl-4-dethia-4-oxa-penam
Saccharopolyspora erythraea
-
-
16
(3S,5R,6S)-3-benzyloxycarbonyl-6-methyl-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 25°C
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 25°C
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 25°C
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 25°C
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 25°C
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 25°C
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 25°C
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 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
substrate Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala , pH 7.4, 25°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
7.5
7.7
8.5
additional information
additional information
-
ratio of hydrolysis/transpeptidation depending on pH
additional information
-
ratio of hydrolysis/transpeptidation depending on pH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 11
-
pH 8: about 50% of maximal activity, pH 11: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Priestia megaterium KM / ATCC 13632
two isozymes penicillin-binding protein 5 and penicillin-binding protein 5a
-
-
brenda
Priestia megaterium KM / ATCC 13632
two isozymes penicillin-binding protein 5 and penicillin-binding protein 5a
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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
brenda
additional information
Priestia megaterium KM / ATCC 13632
-
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
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
PBP3 is evenly distributed on both hemispheres but absent at the equator, the site of future division
brenda
mutant enzyme S96A is produced in cytoplasm of Escherichia coli
brenda
anchored into the outer leaflet of the cytoplasmic membrane
-
brenda
additional information
-
in minimal-medium-grown cells, wild-type PBP5 localizes laterally and at the midcell. Isoform PBP6a localization is lateral and intense at the midcell. PBP6b localizes poorly at the midcell and mainly at the lateral sides
-
brenda
-
attached to the outer leaflet of the cell membrane
-
brenda
-
attached to the outer leaflet of the cell membrane
-
brenda
-
attached to the outer leaflet of the cell membrane
-
brenda
-
GFP-PBP5 localizes to the septum and in concentrated spots along the lateral wall
brenda
enzyme preferentially accumulates in the cell wall fractions obtained by the step of spheroplast preparation
brenda
-
enzyme preferentially accumulates in the cell wall fractions obtained by the step of spheroplast preparation
-
brenda
mutant enzymes K38H, C98A and C98N are produced in culture medium of Streptomyces lividans
-
brenda
-
membrane-bound, the active site is present on the outside surface of the membrane
brenda
-
membrane-bound, the active site is present on the outside surface of the membrane
-
brenda
-
localized in the outer leaflet of the cytosolic membrane
brenda
protein harbors two protein domains separated by a putative hydrophobic transmembrane region
brenda
-
protein harbors two protein domains separated by a putative hydrophobic transmembrane region
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
loss of penicillin-binding protein 5 enhances beta-lactam susceptibility, the observed susceptibilities for ampicillin, piperacillin, amoxicillin, penicillin G, cefadroxil and cefalexin are enhanced by 4fold and for cefalothin and cefaclor the susceptibilities are at least 8fold higher in the mutants
physiological function
physiological function
-
the beta-lactam-sensitive D,D-carboxypeptidase activity of Pbp4 controls the L,D and D,D transpeptidation pathways in Corynebacterium jeikeium
physiological function
-
the DD-carboxypeptidase activity of PBP 5 is responsible for maintaining cell shape
physiological function
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 choleraeâs 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
physiological function
-
D,D-CPases PBP5, PBP6a, and PBP6b change dimer conformation between resting and active states. The isoforms are not redundant but that their balanced activity is required for robust peptidoglycan synthesis
physiological function
in a gene disruption mutant, the spores are affected in their resistance to heat and acid and show a dramatic increase in swelling during germination. The mycelium of the mutant is more sensitive to glycopeptide antibiotics vancomycin and teicoplanin. Both the DD-CPase domain and the hydrophobic transmembrane region are essential for complementing the wild type phenotypes in the mutant. In a model for the biological mechanism, DD-CPase releases D-Ala from peptidoglycan precursors, thereby reducing the substrate pool for peptidoglycan crosslinking (transpeptidation)
physiological function
-
in an isoform DacC deletion mutant, the extracellular activities and fluorescence value of recombinant amylase, green fluorescent protein, and alpha-galactosidase are increased by 82.3, 29.1, and 37.7%, respectively, compared with that of control cells. The outer membrane permeability and intracellular soluble peptidoglycan accumulation of the deletion mutant are also enhanced. In the poles of the deletion mutant, local transparent bulges are found
physiological function
-
overexpression of D,D-carboxypeptidase DacA or DacB promotes the accumulation of intracellular soluble peptidoglycan, alters cell morphology (shape and size) and leads to the formation of transparent globular structures in Escherichia coli cells. Extracellular production of recombinant green fluorescent protein is increased by 1.7- and 2.3fold upon overexpression of DacA and DacB, respectively. Extracellular production of recombinant amylase and apha-galactosidase is increased by 4.5- and 2.8fold, respectively, upon overexpression of DacA, and by 11.9- and 2.5fold, respectively, upon overexpression of DacB. Overexpression of DacA or DacB enhances both the outer and inner membrane permeability of Escherichia coli
physiological function
-
peptide uptake transporters BclA and DD-CPase1 act independently in the morphological differentiation of bacteroids induced by Nodule-specific Cysteine-Rich peptides NCR. The nitrogenase activity of plants infected with a DD-CPase1 mutant is strongly reduced, in large part because the mutant induces much less nodules than the wild type. A BclA/DD-CPAse1 double exhibits a similar symbiotic phenotype as the DD-CPase1 single mutant
physiological function
-
peptide uptake transporters BclA and DD-CPase1 act independently in the morphological differentiation of bacteroids induced by Nodule-specific Cysteine-Rich peptides NCR. The nitrogenase activity of plants infected with a DD-CPase1 mutant is strongly reduced, in large part because the mutant induces much less nodules than the wild type. A BclA/DD-CPAse1 double exhibits a similar symbiotic phenotype as the DD-CPase1 single mutant
-
physiological function
-
in a gene disruption mutant, the spores are affected in their resistance to heat and acid and show a dramatic increase in swelling during germination. The mycelium of the mutant is more sensitive to glycopeptide antibiotics vancomycin and teicoplanin. Both the DD-CPase domain and the hydrophobic transmembrane region are essential for complementing the wild type phenotypes in the mutant. In a model for the biological mechanism, DD-CPase releases D-Ala from peptidoglycan precursors, thereby reducing the substrate pool for peptidoglycan crosslinking (transpeptidation)
-
physiological function
-
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 choleraeâs 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
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM