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The taxonomic range for the selected organisms is: Streptomyces sp.
The enzyme appears in selected viruses and cellular organisms
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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
-
?
benzoyl-D-Ala-thioglycolate + H2O
?
-
-
?
benzoyl-Gly-thioglycolate + H2O
?
-
-
?
benzoyl-Gly-thiolactate + H2O
?
-
-
?
hippuryl-mercaptoacetic acid
hippuric acid + mercaptoacetate
-
-
-
-
?
L-Lys-D-Ala-D-Ala + H2O
L-Lys-D-Ala + D-Ala
-
-
-
-
?
N-alpha-acetyl-L-Lys-D-Ala-thiolactate + H2O
?
-
-
?
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
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-thiolactate + H2O
?
-
-
?
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha-Acetyl-L-Lys-D-Ala + D-Ala
-
-
?
phenylacetyl-D-Ala-thioglycolate + H2O
?
-
-
?
phenylacetyl-D-Ala-thiolactate + H2O
?
-
-
?
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
X-D-Ala-D-Ala + H2O
?
-
-
-
-
?
additional information
?
-
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
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-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
-
-
-
?
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
?
-
-
influence of substrate conformation
-
-
?
additional information
?
-
-
requirement for D-Ala in P1 position
-
-
?
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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
1.3 - 1.5
benzoyl-D-Ala-thioglycolate
0.8 - 3
benzoyl-Gly-thioglycolate
0.22 - 1
benzoyl-Gly-thiolactate
0.12
hippuryl-mercaptoacetic acid
-
crystal and solution
0.4
N-alpha-acetyl-L-Lys-D-Ala-thiolactate
pH 7.2, 37°C, wild-type enzyme
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
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
5 - 20
X-D-Ala-D-Ala
-
value depending on X
1.3
benzoyl-D-Ala-thioglycolate
pH 7.2, 37°C, mutant enzyme C98A
1.5
benzoyl-D-Ala-thioglycolate
pH 7.2, 37°C, wild-type enzyme
0.8
benzoyl-Gly-thioglycolate
pH 7.2, 37°C, mutant enzyme C98A
3
benzoyl-Gly-thioglycolate
above, pH 7.2, 37°C, wild-type enzyme
0.22
benzoyl-Gly-thiolactate
pH 7.2, 37°C, wild-type enzyme
0.3
benzoyl-Gly-thiolactate
pH 7.2, 37°C, mutant enzyme C98A
1
benzoyl-Gly-thiolactate
pH 7.2, 37°C, mutant enzyme K38H
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, 37°C, mutant enzyme C98A
6.2
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
pH 7.2, 37°C, wild-type enzyme
14
Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala
-
-
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
9.4
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala
pH 7.2, 37°C, wild-type enzyme
30
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala
pH 7.2, 37°C, mutant enzyme C98A
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
1.2
phenylacetyl-D-Ala-thiolactate
pH 7.2, 37°C, mutant enzyme C98A
1.2
phenylacetyl-D-Ala-thiolactate
pH 7.2, 37°C, wild-type enzyme
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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
0.11 - 0.3
benzoyl-D-Ala-thioglycolate
0.024 - 0.08
benzoyl-Gly-thioglycolate
0.006 - 0.08
benzoyl-Gly-thiolactate
17.5 - 350
diacetyl-L-Lys-D-Ala-D-Ala
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
0.11
benzoyl-D-Ala-thioglycolate
pH 7.2, 37°C, wild-type enzyme
0.3
benzoyl-D-Ala-thioglycolate
pH 7.2, 37°C, mutant enzyme C98A
0.024
benzoyl-Gly-thioglycolate
above, pH 7.2, 37°C, wild-type enzyme
0.08
benzoyl-Gly-thioglycolate
pH 7.2, 37°C, mutant enzyme C98A
0.006
benzoyl-Gly-thiolactate
pH 7.2, 37°C, mutant enzyme K38H
0.017
benzoyl-Gly-thiolactate
pH 7.2, 37°C, wild-type enzyme
0.08
benzoyl-Gly-thiolactate
pH 7.2, 37°C, mutant enzyme C98A
17.5
diacetyl-L-Lys-D-Ala-D-Ala
-
Streptomyces sp. R39
55
diacetyl-L-Lys-D-Ala-D-Ala
-
Streptomyces sp. R61
267
diacetyl-L-Lys-D-Ala-D-Ala
-
54000 MW enzyme
350
diacetyl-L-Lys-D-Ala-D-Ala
-
40000 MW 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
0.43
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
0.45
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala
pH 7.2, 37°C, wild-type enzyme
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
0.6
phenylacetyl-D-Ala-thiolactate
pH 7.2, 37°C, wild-type enzyme
2.2
phenylacetyl-D-Ala-thiolactate
pH 7.2, 37°C, mutant enzyme C98A
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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
brenda
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.
brenda
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.
brenda
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.
brenda
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.
brenda
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.
brenda
Frere, J.M.; Joris, B.
Penicillin-sensitive enzymes in peptidoglycan biosynthesis
CRC Crit. Rev. Microbiol.
11
299-396
1985
Actinomadura sp., Streptomyces sp.
brenda
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.
brenda
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.
-
brenda
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.
brenda
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
brenda
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.
brenda
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.
brenda
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.
brenda
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.
brenda
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.
brenda
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.
brenda
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
brenda
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
brenda
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.
brenda
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
brenda
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)
brenda
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.
brenda
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.
brenda
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.
brenda
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)
brenda
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.
brenda
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.
brenda
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)
brenda
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)
brenda
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.
brenda
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.
brenda
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
brenda
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)
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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)
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