Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.16.4 - serine-type D-Ala-D-Ala carboxypeptidase and Organism(s) Streptomyces sp. and UniProt Accession P39042

for references in articles please use BRENDA:EC3.4.16.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Streptomyces sp.
UNIPROT: P39042 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Streptomyces sp.
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
Synonyms
transpeptidase, penicillin-binding protein, pbp2x, pbp1a, pbp1b, penicillin binding proteins, pbp 2, pbp 3, pbp 5, dd-peptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DD-transpeptidase/penicillin-binding protein
-
carboxypeptidase I
-
-
-
-
CPase
-
-
-
-
D-alanine carboxypeptidase
-
-
-
-
D-alanine carboxypeptidase I
-
-
-
-
D-alanyl 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-cleaving peptidase
-
-
-
-
D-alanyl-D-alanine-cleaving-peptidase
-
-
-
-
DD-Carboxypeptidase
-
-
-
-
DD-peptidase
DD-transpeptidase
PBP-5*
-
-
-
-
PBP-6B
-
-
-
-
PBP5
-
-
-
-
penicillin binding protein 5
-
-
-
-
penicillin-binding protein
-
-
serine type D-alanyl-D-alanine carboxypeptidase/transpeptidase
-
transpeptidase
-
-
VanX
-
-
-
-
VanY
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
CAS REGISTRY NUMBER
COMMENTARY hide
9077-67-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
?
N-alpha-acetyl-L-Lys-D-Ala-thiolactate + H2O
?
show the reaction diagram
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate + H2O
?
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
-
-
?
phenylacetyl-D-Ala-thioglycolate + H2O
?
show the reaction diagram
-
-
?
phenylacetyl-D-Ala-thiolactate + H2O
?
show the reaction diagram
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-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
-
-
-
?
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
-
?
hippuryl-mercaptoacetic acid
hippuric acid + mercaptoacetate
show the reaction diagram
-
-
-
-
?
L-Lys-D-Ala-D-Ala + H2O
L-Lys-D-Ala + 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
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-lactate + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-lactate
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-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
-
-
-
-
?
X-D-Ala-D-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
additional information
?
-
the enzyme is responsible for the final peptidoglycan cross-linking step in bacterial cell wall biosynthesis
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2,3)-alpha-methylene benzylpenicillin
-
modeling of enzyme-inhibitor complex
2-Methylpenem
-
-
2-Phenylpenem
-
-
7-(phenoxyacetamido)-3-desacetoxycephalosporamic acid
-
-
benzylpenicillin
-
-
beta-lactam
-
-
beta-lactams
-
cephalosporin
-
-
cephalothin
-
-
Delta2-(and Delta3)-Deacetoxy-7-phenylacetamidocephalosporanates
-
-
-
depsipeptides
-
-
-
nocardicin A
-
-
Oxyimino-DELTA3-cephalosporins
-
syn- and anti-isomers
-
Penicillanate
-
-
penicillin
-
kinetic model of interaction
penicillin G
-
-
phenyl glycyl-L-alpha-aminopimelyl-epsilon-(D-2-aminoethyl)phosphonate
-
sulfazecine
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 1.5
benzoyl-D-Ala-thioglycolate
0.8 - 3
benzoyl-Gly-thioglycolate
0.22 - 1
benzoyl-Gly-thiolactate
0.4
N-alpha-acetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37°C, wild-type enzyme
0.35 - 6.2
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
2 - 3
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate
9.4 - 30
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala
0.6
Nalpha-acetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37°C, mutant enzyme C98A
2.4 - 3
phenylacetyl-D-Ala-thioglycolate
1.2
phenylacetyl-D-Ala-thiolactate
0.36
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-hydroxyglycinate
pH 7.5, 25°C
0.45
3-carboxyphenyl (2R)-N-(phenylacetyl)-2-methoxyglycinate
pH 7.5, 25°C
0.12
hippuryl-mercaptoacetic acid
-
crystal and solution
12
Nalpha, Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
lysozyme releasable enzyme
0.1 - 14
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
5 - 20
X-D-Ala-D-Ala
-
value depending on X
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 0.3
benzoyl-D-Ala-thioglycolate
0.024 - 0.08
benzoyl-Gly-thioglycolate
0.006 - 0.08
benzoyl-Gly-thiolactate
0.1 - 0.8
N-alpha-acetyl-L-Lys-D-Ala-thiolactate
0.2 - 0.3
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
0.43 - 1.1
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-thiolactate
0.13 - 0.45
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala
0.015 - 6.08
phenylacetyl-D-Ala-thioglycolate
0.6 - 2.2
phenylacetyl-D-Ala-thiolactate
6.9
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
17.5 - 350
diacetyl-L-Lys-D-Ala-D-Ala
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
hydrolysis, value increased by high ionic strength
8
-
transpeptidation, Streptomyces sp. R61
9.5
-
transpeptidation, Streptomyces sp. R39
additional information
-
ratio of hydrolysis/transpeptidation depending on pH
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
mutant enzyme S96A is produced in cytoplasm of Escherichia coli
Manually annotated by BRENDA team
mutant enzymes K38H, C98A and C98N are produced in culture medium of Streptomyces lividans
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
gel filtration
53000
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. Mutant enzymes S96A, K38H, C98A and C98N are produced in culture medium of Streptomyces lividans
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. Benzylpenicillin’s 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, 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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C98A
half-life at 72°C increases to 13 min, compared to 10 min for the wild-type enzyme. Half-life at 60°C 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 72°C decreases to 6 min, compared to 10 min for the wild-type enzyme. Half-life at 60°C 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 72°C 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 72°C decreases to 8 min, compared to 10 min for the wild-type enzyme. Half-life at 60°C 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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
50
-
10 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
bacterial DD-peptidases are still an enticing target for antibacterial agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Frere, J.M.; Moreno, R.; Ghuysen, J.M.; Perkins, H.R.; Dierickx, L.; Delcambe, L.
Molecular weight, amino acid composition and physicochemical properties of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39
Biochem. J.
143
233-240
1974
Streptomyces sp., Streptomyces sp. R39
Manually annotated by BRENDA team
Duez, C.; Piron-Fraipont, C.; Joris, B.; Dusart, J.; Urdea, M.S; Martial, J.A.; Frere, J.M.; Ghuysen, J.M.
Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene [published erratum appears in Eur J Biochem 1994 Sep 15;224(3):1079
Eur. J. Biochem.
162
509-518
1987
Streptomyces sp.
Manually annotated by BRENDA team
Kelly, J.A.; Knox, J.R.; Zhao, H.; Frere, J.M.; Ghuysen, J.M.
Crystallographic mapping of beta-lactams bound to a D-alanyl-D-alanine peptidase target enzyme
J. Mol. Biol.
209
281-295
1989
Streptomyces sp.
Manually annotated by BRENDA team
Leyh-Bouille, M.; Nguyen-Disteche, M.; Pirlot, S.; Veithen, A.; Bourguignon, C.; Ghuysen, J.M.
Streptomyces K15 DD-peptidase-catalysed reactions with suicide beta-lactam carbonyl donors [published erratum appears in Biochem J 1986 Jun 15;236(3):following 933
Biochem. J.
235
177-182
1986
Streptomyces sp.
Manually annotated by BRENDA team
Laurent, G.; Durant, F.; Frere, J.M.; Klein, D.; Ghuysen, J.M.
Des-, syn- and anti-oxyimino-delta 3-cephalosporins. Intrinsic reactivity and reaction with RTEM-2 serine beta-lactamase and D-alanyl-D-alanine-cleaving serine and Zn2+-containing peptidases
Biochem. J.
218
933-937
1984
Actinomadura sp., Streptomyces sp.
Manually annotated by BRENDA team
Georgopapadakou, N.H.; Liu, F.Y.; Ryono, D.E.; Neubeck, R.; Gordon, E.M.; Pluscec, J.
Streptomyces R61 DD-carboxypeptidase: hydrolysis of X-D-alanyl-D-alanine peptides measured by a fluorometric assay
Anal. Biochem.
137
125-128
1984
Streptomyces sp.
Manually annotated by BRENDA team
Frere, J.M.; Joris, B.
Penicillin-sensitive enzymes in peptidoglycan biosynthesis
CRC Crit. Rev. Microbiol.
11
299-396
1985
Actinomadura sp., Streptomyces sp.
Manually annotated by BRENDA team
Ghuysen, J.M.; Frere, J.M.; Leyh-Bouille, M.; Nguyen-Disteche, M.; Coyette, J.; Dusart, J.; Charlier, P.; Dive, G.; Lamotte-Brasseur, J.
Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics
Scand. J. Infect. Dis.
42
17-37
1984
Actinomadura sp., Streptomyces sp.
Manually annotated by BRENDA team
Frere, J.M.; Klein, D.; Kelly, J.A.; Ghuysen, J.M.
Interaction between monobactams and model D-alanyl-D-alanine-cleaving peptidases
FEMS Microbiol. Lett.
21
213-217
1984
Actinomadura sp., Streptomyces sp.
-
Manually annotated by BRENDA team
Joris, B.; Jacques, P.; Frere, J.M.; Ghuysen, J.M.; VanBeeumen, J.
Primary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid sequence data
Eur. J. Biochem.
162
519-524
1987
Streptomyces sp.
Manually annotated by BRENDA team
Frere, J.M.; Kelly, J.A.; Klein, D.; Ghuysen, J.M.
delta 2- and delta 3-Cephalosporins, penicillinate and 6-unsubstituted penems. Intrinsic reactivity and interaction with beta-lactamases and D-alanyl-D-alanine-cleaving serine peptidases
Biochem. J.
203
223-234
1982
Streptomyces sp., Streptomyces sp. R39
Manually annotated by BRENDA team
DeCoen, J.L.; Lamotte-Brasseur, J.; Ghuysen, J.M.; Frere, J.M.; Perkins, H.R.
Conformational analysis of peptide substrates and inhibitors of the Zn2+ G and serine R61 D-alanyl-D-alanine peptidases
Eur. J. Biochem.
121
221-232
1981
Streptomyces sp.
Manually annotated by BRENDA team
Leyh-Bouille, M.; Nguyen-Disteche, M.; Ghuysen, J.M.
On the DD-carboxypeptidase enzyme system of Streptomyces strain K15
Eur. J. Biochem.
115
579-584
1981
Streptomyces sp.
Manually annotated by BRENDA team
Varetto, L.; Frere, J.M.; Nguyen-Disteche, M.; Ghuysen, J.M.; Houssier, C.
The pH dependence of the active-site serine DD-peptidase of Streptomyces R61
Eur. J. Biochem.
162
525-531
1987
Streptomyces sp.
Manually annotated by BRENDA team
Murphy, B.P.; Pratt, R.F.
Evidence for an oxyanion hole in serine beta-lactamases and DD-peptidases
Biochem. J.
256
669-672
1988
Streptomyces sp.
Manually annotated by BRENDA team
Kelly, J.A.; Knox, J.R.; Moews, P.C.; Hite, G.J.; Bartolone, J.B.; Zhao, H.; Joris, B.; Frere, J.M.; Ghuysen, J.M.
2.8-A Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 and complexes with beta-lactams
J. Biol. Chem.
260
6449-6458
1985
Streptomyces sp.
Manually annotated by BRENDA team
Frere, J.M.; Duez, C.; Ghuysen, J.M.
Occurrence of a serine residue in the penicillin-binding site of the exocellular DD-carboxy-peptidase-transpeptidase from Streptomyces R61
FEBS Lett.
70
257-260
1976
Streptomyces sp.
Manually annotated by BRENDA team
Van der Linden, M.P.G.; Mottl, H.; Keck, W.
Cytoplasmic high-level expression of a soluble, enzymatically active form of the Escherichia coli penicillin-binding protein 5 and purification by dye chromatography
Eur. J. Biochem.
204
197-202
1992
Streptomyces sp., Escherichia coli, Streptomyces sp. R39
Manually annotated by BRENDA team
Perkins, H.R.; Nieto, M.; Frere, J.M.; Leyh-Bouille, M.; Ghuysen, J.M.
Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors
Biochem. J.
131
707-718
1973
Streptomyces sp., Streptomyces sp. R39, Streptomyces sp. K11
Manually annotated by BRENDA team
Leyh-Bouille, M.; Coyette, J.; Ghuysen, J.M.; Idczak, J.; Perkins, H.R.; Nieto, M.
Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61
Biochemistry
10
2163-2170
1971
Streptomyces sp.
Manually annotated by BRENDA team
Kimura, Y.; Takashima, Y.; Tokumasu, Y.; Sato, M.
Molecular cloning, sequence analysis, and characterization of a penicillin-resistant DD-carboxypeptidase of Myxococcus xanthus
J. Bacteriol.
181
4696-4699
1999
Streptomyces sp., Myxococcus xanthus
Manually annotated by BRENDA team
Fonze, E.; Vermeire, M.; Nguyen-Disteche, M.; Brasseur, R.; Charlier, P.
The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15
J. Biol. Chem.
274
21853-21860
1999
Streptomyces sp. (P39042)
Manually annotated by BRENDA team
Palomeque-Messia, P.; Quittre, V.; Leyh-Bouille, M.; Nguyen-Disteche, M.; Gershater, C.J.L.; Dacey, I.K.; Dusart, J.; van Beeumen, J.; Ghuysen, J.M.
Secretion by overexpression and purification of the water-soluble Streptomyces K15 DD-transpeptidase/penicillin-binding protein
Biochem. J.
288
87-91
1992
Streptomyces sp.
Manually annotated by BRENDA team
Eng, G.Y.; Maxwell, R.J.
Effect of immobilization on the penicillin binding and reactivity properties of DD-peptidase from Streptomyces R61
J. Mol. Recognit.
9
706-714
1996
Streptomyces sp.
Manually annotated by BRENDA team
Cabaret, D.; Liu, J.; Wakselman, M.; Pratt, R.F.; Xu, Y.
Functionalized depsipeptides, substrates and inhibitors of beta-lactamases and DD-peptidases
Bioorg. Med. Chem. Lett.
2
757-771
1994
Streptomyces sp.
Manually annotated by BRENDA team
Kelly, J.A.; Kuzin, A.P.
The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 A resolution
J. Mol. Biol.
254
223-236
1995
Streptomyces sp. (P15555)
Manually annotated by BRENDA team
Kelly, J.A.; Waley, S.G.; Adam, M.; Frere, J.M.
Crystalline enzyme kinetics: activity of the Streptomyces R61 D-alanyl-D-alanine peptidase
Biochim. Biophys. Acta
1119
256-260
1992
Streptomyces sp.
Manually annotated by BRENDA team
Erpicum, T.; Granier, B.; Delcour, M.; Lenzini, V.M.; Nguyen-Disteche, M.; Dusart, J.; Frere, J.M.
Enzyme production by genetically engineered Streptomyces strains: Influence of culture conditions
Biotechnol. Bioeng.
35
719-726
1990
Streptomyces sp.
Manually annotated by BRENDA team
Silvaggi, N.R.; Anderson, J.W.; Brinsmade, S.R.; Pratt, R.F.; Kelly, J.A.
The crystal structure of phosphonate-inhibited D-Ala-D-Ala peptidase reveals an analogue of a tetrahedral transition state
Biochemistry
42
1199-1208
2003
Streptomyces sp. (P15555)
Manually annotated by BRENDA team
Rhazi, N.; Charlier, P.; Dehareng, D.; Engher, D.; Vermeire, M.; Frere, J.M.; Nguyen-Disteche, M.; Fonze, E.
Catalytic mechanism of the Streptomyces K15 DD-transpeptidase/penicillin-binding protein probed by site-directed mutagenesis and structural analysis
Biochemistry
42
2895-2906
2003
Streptomyces sp. (P39042)
Manually annotated by BRENDA team
Lee, W.; McDonough, M.A.; Kotra, L.P.; Li, Z.H.; Silvaggi, N.R.; Takeda, Y.; Kelly, J.A.; Mobashery, S.
A 1.2-.ANG. snapshot of the final step of bacterial cell wall biosynthesis
Proc. Natl. Acad. Sci. USA
98
1427-1431
2001
Streptomyces sp. (P15555), Streptomyces sp.
Manually annotated by BRENDA team
Diaz, N.; Sordo, T.L.; Suarez, D.
Insights into the base catalysis exerted by the DD-transpeptidase from Streptomyces K15: A molecular dynamics study
Biochemistry
44
3225 - 3240
2005
Streptomyces sp.
Manually annotated by BRENDA team
Pratt, R.F.
Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins)
Cell. Mol. Life Sci.
65
2138-2155
2008
Bacillus subtilis, Caulobacter vibrioides, Streptomyces sp., Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Staphylococcus aureus, Neisseria gonorrhoeae, Streptomyces sp. R61, Streptomyces sp. K15
Manually annotated by BRENDA team
Hargis, J.; Vankayala, S.; White, J.; Woodcock, H.
Identification and characterization of noncovalent interactions that drive binding and specificity in DD-peptidases and beta-lactamases
J. Chem. Theory Comput.
10
855-864
2014
Streptomyces sp. (P15555)
Manually annotated by BRENDA team
Pelto, R.B.; Pratt, R.F.
Kinetics and stereochemistry of hydrolysis of an N-(phenylacetyl)-alpha-hydroxyglycine ester catalyzed by serine beta-lactamases and DD-peptidases
Org. Biomol. Chem.
10
7356-7362
2012
Streptomyces sp. (P15555), Actinomadura sp. (P39045)
Manually annotated by BRENDA team