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ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + 2 D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + Ala + Ala
?
-
a possible cellular role of VanA is to synthesize a modified cell-wall component, with D-Ala-D-Met or D-Ala-Phe instead of D-Ala-D-Ala, which is subsequently not recognized by vancomycin
-
-
?
ATP + D-Ala + 2-aminopentanoate
ADP + phosphate + D-Ala-2-aminopentanoate
-
-
-
-
?
ATP + D-Ala + D-2-aminopentanoate
ADP + phosphate + D-Ala-D-2-aminopentanoate
-
-
-
-
?
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
ATP + D-Ala + D-Met
ADP + phosphate + D-Ala-D-Met
-
-
-
-
?
ATP + D-Ala + D-norleucine
ADP + phosphate + D-Ala-D-norleucine
-
-
-
-
?
ATP + D-Ala + D-Phe
ADP + phosphate + D-Ala-D-Phe
-
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
ATP + D-alanine + D-serine
ADP + D-alanyl-D-serine + D-alanyl-D-alanine + D-seryl-D-serine
-
-
-
-
?
ATP + D-serine
ADP + phosphate + D-alanyl-D-serine
-
-
-
?
D-cysteine + ATP
ADP + D-cysteinyl-D-cysteine
-
-
-
-
?
D-serine + ATP
ADP + D-serinyl-D-serine
-
-
-
-
?
D-threonine + ATP
ADP + D-threonyl-D-threonine
-
-
-
-
?
dipeptides + ATP
?
-
-
-
-
?
glycine + glycine + ATP
ADP + Gly-Gly + phosphate
-
-
-
-
?
additional information
?
-
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
Y216, S150, and E15 form a hydrogen-bonding triad that orients an omega-loop to close over the active site and also to orient substrate D-Ala1 (the first molecule of substrate that is activated by the enzyme protein). The bifunctional enzyme also catalyzes the formation of D-alanyl-D-lactate (D-alanine-(R)-lactate ligase)
-
-
?
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
?
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
?
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
?
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
?
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
?
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
?
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
?
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
?
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
-
r
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
additional information
?
-
DDl is an essential enzyme in bacterial cell wall biosynthesis
-
-
?
additional information
?
-
-
the enzyme is also capable of synthesizing fluorinated dipeptides
-
-
?
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(2Z)-N-(2-chloro-6-methylphenyl)-2-ethynyl-3-hydroxybut-2-enamide
-
(E)-N,N'-bis(2-chloroethyl)diazene-1,2-dicarboxamide
-
(E)-N,N'-bis(pyridin-3-ylmethyl)diazene-1,2-dicarboxamide
-
(E)-N-(2-chloroethyl)-N'-(4-isopropylphenyl)diazene-1,2-dicarboxamide
-
(E)-N-(2-chloroethyl)-N'-(pyridin-2-ylmethyl)diazene-1,2-dicarboxamide
-
(E)-N-(2-chloroethyl)-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
-
(E)-N-(3-chlorophenyl)-N'-(pyridin-3-ylmethyl)diazene-1,2-dicarboxamide
-
(E)-N-(3-chlorophenyl)-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
-
(E)-N-(4-fluorophenyl)-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
-
(E)-N-(4-sec-butylphenyl)-N'-(2-chloroethyl)diazene-1,2-dicarboxamide
-
(E)-N-cyclohexyl-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
-
(E)-N-phenyl-N'-(pyridin-2-ylmethyl)diazene-1,2-dicarboxamide
-
(E)-N-phenyl-N'-(pyridin-3-ylmethyl)diazene-1,2-dicarboxamide
-
(E)-N-phenyl-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
-
(E)-N-[4-(butan-2-yl)phenyl]-N'-(2-chloroethyl)diazene-1,2-dicarboxamide
-
D-Ala-D-2-hydroxybutanoate phosphonate
-
D-Ala-D-Ala phosphinate
-
leflunomide
an antirheumatic drug
LFM-A12
an analog of the Leflunomide metabolite A771726
LFM-A13
Brutons's tyrosine kinase inhibitor, an analog of the Leflunomide metabolite A771726
LY294002
slight inhibition
N-(2,5-dibromophenyl)-2-oxopropanamide
-
phospho-D-cycloserine
DCSP, inhibition of D-Ala:D-Ala ligase through a phosphorylated form of the antibiotic D-cycloserine, DCS, bimodal mechanism of action of the inhibitor. The compound also inhibits the phosphatase activity of EcDdlB, formation of phospho-D-cycloserine by EcDdlB in solution a positional isotope exchange (PIX) reaction, a phosphatase activity of EcDdlB is detected as a side-reaction alongside the positional isotope exchange (PIX) reaction. DCS is the specific acceptor of the ATP gamma-P group during the phosphate transfer reaction by the enzyme, and DCS inhibits EcDdlB phosphatase activity
piceatannol
slight inhibition
tyrphostin 47
competitive versus ATP
tyrphostin 51
mixed-type inhibition
Wortmannin
slight inhibition
[3-chloro-2,2-dimethyl-N-4(trimethylfluoro)phenyl]propanamide
-
1,4-dimethyl-9H-carbazole
-
-
1,4-dimethyl-9H-carbazole-3-carbaldehyde
-
-
1-(2-amino-6-phenylpyrido[2,3-d]pyrimidin-7-yl)-3-tert-butylurea
-
-
1-(3-chloro-8-methoxy-11H-indolo[3,2-c]quinolin-9-yl)-N,N-dimethylmethanamine
-
-
1-tert-butyl-3-[6-(2,6-dichlorophenyl)-2-[[3-(morpholin-4-yl)propyl]amino]pyrido[2,3-d]pyrimidin-7-yl]urea
-
-
1-tert-butyl-3-[6-(3,5-dimethoxyphenyl)-2-[[3-(dimethylamino)propyl]amino]pyrido[2,3-d]pyrimidin-7-yl]urea
-
-
1-tert-butyl-3-[6-(3,5-dimethoxyphenyl)-2-[[3-(morpholin-4-yl)propyl]amino]pyrido[2,3-d]pyrimidin-7-yl]urea
-
-
1-[2-amino-6-(1,3-benzodioxol-5-yl)pyrido[2,3-d]pyrimidin-7-yl]-3-tert-butylurea
-
-
1-[2-amino-6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidin-7-yl]-3-tert-butylurea
-
-
1-[2-amino-6-(2-bromo-6-fluorophenyl)pyrido[2,3-d]pyrimidin-7-yl]-3-tert-butylurea
-
-
1-[2-amino-6-(3,5-dimethoxyphenyl)pyrido[2,3-d]pyrimidin-7-yl]-3-tert-butylurea
-
-
1-[2-amino-6-[3,5-bis(trifluoromethyl)phenyl]pyrido[2,3-d]pyrimidin-7-yl]-3-tert-butylurea
-
-
1-[4-[(6-chloro-2-methoxyacridin-9-yl)amino]phenyl]-3-(dimethylamino)propan-1-ol
-
-
1-[[(4-fluorophenyl)sulfonyl]amino]-3-(morpholin-4-yl)propan-2-yl dihydrogen phosphate
-
0.5 mM, 77% inhibition
1-[[(4-methoxyphenyl)sulfonyl]amino]-3-(morpholin-4-yl)propan-2-yl dihydrogen phosphate
-
0.5 mM, 83% inhibition
2,2-diethoxy-N-[(6-methoxy-1,4-dimethyl-9H-carbazol-3-yl)methyl]ethanamine
-
-
2,2-diethoxy-N-[(7-fluoro-1,4-dimethyl-9H-carbazol-3-yl)methyl]ethanamine
-
-
2,2-diethoxy-N-[(8-ethyl-1,4-dimethyl-9H-carbazol-3-yl)methyl]ethanamine
-
-
2,5,11-trimethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
-
-
2-[(1-[[2-amino-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-7-yl]amino]ethenyl)amino]propan-2-ol
-
-
2-[(1-[[2-amino-6-(2,6-difluorophenyl)pyrido[2,3-d]pyrimidin-7-yl]amino]ethenyl)amino]propan-2-ol
-
-
2-[(1-[[2-amino-6-(3,5-dichlorophenyl)pyrido[2,3-d]pyrimidin-7-yl]amino]ethenyl)amino]propan-2-ol
-
-
2-[(1-[[2-amino-6-(3,5-difluorophenyl)pyrido[2,3-d]pyrimidin-7-yl]amino]ethenyl)amino]propan-2-ol
-
-
3-(9-methoxy-5,11-dimethyl-6H-pyrido[4,3-b]carbazol-6-yl)propan-1-amine
-
-
3-[(1,6-dichloro-4-methoxyacridin-9-yl)amino]-2-[(diethylamino)methyl]phenol
-
-
3-[(6-chloro-2-methoxyacridin-9-yl)amino]-2-(pyrrolidin-1-ylmethyl)phenol
-
-
3-[(6-chloro-2-methoxyacridin-9-yl)amino]-2-[(4-methylpiperazin-1-yl)methyl]phenol
-
-
3-[(6-chloro-2-methoxyacridin-9-yl)amino]-2-[(diethylamino)methyl]-6-(prop-2-en-1-yl)phenol
-
-
3-[(6-chloro-2-methoxyacridin-9-yl)amino]-2-[(diethylamino)methyl]phenol
-
-
5,11-Dimethyl-6H-pyrido[4,3-b]carbazole
-
-
5,6,11-trimethyl-6H-pyrido[4,3-b]carbazole
-
-
6-(1,3-benzodioxol-5-yl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-(2,6-dichlorophenyl)-N2-[3-(dimethylamino)propyl]pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-(2,6-dichlorophenyl)-N2-[3-(morpholin-4-yl)propyl]pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-(2,6-difluorophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-(2-chloro-6-fluorophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-(3,5-dichlorophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-(3,5-difluorophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-(3,5-dimethoxyphenyl)-N2-[3-(morpholin-4-yl)propyl]pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-(3,5-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-bromo-1,4-dimethyl-9H-carbazole
-
-
6-bromo-1,4-dimethyl-9H-carbazole-3-carbaldehyde
-
-
6-chloro-2-methoxy-N-(6-methoxyquinolin-8-yl)acridin-9-amine
-
-
6-methoxy-1,4-dimethyl-9H-carbazole
-
-
6-methoxy-1,4-dimethyl-9H-carbazole-3-carbaldehyde
-
-
6-phenylpyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-[3,5-bis(trifluoromethyl)phenyl]pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
7-ethyl-5,11-dimethyl-6H-pyrido[4,3-b]carbazole
-
-
7-fluoro-1,4-dimethyl-9H-carbazole
-
-
7-fluoro-1,4-dimethyl-9H-carbazole-3-carbaldehyde
-
-
8-ethyl-1,4-dimethyl-9H-carbazole
-
-
8-ethyl-1,4-dimethyl-9H-carbazole-3-carbaldehyde
-
-
8-fluoro-2,5,11-trimethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
-
-
8-fluoro-5,11-dimethyl-6H-pyrido[4,3-b]carbazole
-
-
8-fluoro-5,6,11-trimethyl-6H-pyrido[4,3-b]carbazole
-
-
9-bromo-2,5,11-trimethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
-
-
9-bromo-2,5,6,11-tetramethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
-
-
9-bromo-5,11-dimethyl-6H-pyrido[4,3-b]carbazole
-
-
9-bromo-5,6,11-trimethyl-6H-pyrido[4,3-b]carbazole
-
-
9-methoxy-2,5,11-trimethyl-6H-pyrido[4,3-b]carbazol-2-ium acetate
-
-
9-methoxy-2,5,11-trimethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
-
-
9-methoxy-2,5,6,11-tetramethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
-
-
9-methoxy-5,11-dimethyl-6H-pyrido[4,3-b]carbazole
-
-
9-methoxy-5,6,11-trimethyl-6H-pyrido[4,3-b]carbazole
-
-
Aminoalkylphosphinate
-
-
-
apigenin
-
4',5,7-trihydroxyflavone, inhibition mechanism, competitive with respect to the substrate ATP and non-competitive to the substrate D-Ala
N-[(1,4-dimethyl-9H-carbazol-3-yl)methyl]-2,2-diethoxyethanamine
-
-
N-[(3-chloro-8-methoxy-11H-indolo[3,2-c]quinolin-9-yl)methyl]-N-ethylethanamine
-
-
N-[(6-bromo-1,4-dimethyl-9H-carbazol-3-yl)methyl]-2,2-diethoxyethanamine
-
-
Phosphonate dipeptide analogs
-
weak inhibition of ligase B from E. coli and Van A from Enterococcus faecium
-
quercetin
-
i.e. 3,3',4',5,7-pentahydroxyflavone, inhibition mechanism, competitive with respect to the substrate ATP and non-competitive to the substrate D-Ala
[1(S)-Aminoethyl][(2RS)2-carboxy-1-octyl]phosphinic acid
-
classical slow-binding
D-cycloserine
-
D-cycloserine
competitive inhibitor
Phosphinates
-
-
-
Phosphinates
-
weak inhibition of ligase B of E. coli and Van A from Enterococcus faecium, strong inhibition of ligase A from E. coli
-
additional information
antibiotic inhibitor design, bisubstrate inhibitors that block the ATP and D-Ala binding sites exhibit enhanced selectivity and potency profiles by preferentially inhibiting DDl over kinases, overview
-
additional information
-
6-arylpyrido[2,3-d]pyrimidines as novel ATP-competitive inhibitors of the bacterial enzyme, ligand docking and modeling, overview
-
additional information
-
evaluation of ellipticines and 9-acridinylamines as enzyme inhibitors. Ellipticines with a quaternary methylpyridinium moiety are the most potent among all studied compounds, with MIC values as low as 2 mg/l in strains with intact efflux mechanisms. The compounds cause membrane damage. Inhibitor MIC values, overview
-
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33
2-aminopentanoate
-
reaction with D-Ala + ATP
15
D-norleucine
-
reaction with D-Ala + ATP
6
D-Phe
-
reaction with D-Ala + ATP
additional information
additional information
-
0.003
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule) , wild-type enzyme, pH 7.5
0.004
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule), wild-type enzyme, pH 9.2
0.11
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule), wild-type enzyme, pH 6.0
0.51
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule), mutant enzyme E15Q, pH 7.5
0.51
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule), mutant enzyme E15Q, pH 9.2
0.85
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule), mutant enzyme S150A, pH 7.5
1.1
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), wild-type enzyme, pH 9.2
2
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), wild-type enzyme, pH 7.5
4.8
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule), mutant enzyme Y216F, pH 9.2
6.2
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule), mutant enzyme S150A, pH 6.0
8
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), wild-type enzyme, pH 6.0
11
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule), mutant enzyme E15Q, pH 6.0
16
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule), mutant enzyme Y216F, pH 7.5
44
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule) , mutant enzyme S150A, pH 9.2
65
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), mutant enzyme E15Q, pH 9.2
74
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), mutant enzyme E15Q, pH 7.5
80
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), mutant enzyme S150A, pH 7.5
82
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), mutant enzyme E15Q, pH 6.0
140
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), mutant enzyme S150A, pH 6.0
150
D-alanine
37°C, KM-value for D-alanine1 (the first molecule of substrate that is activated by the enzyme molecule) , mutant enzyme Y216F, pH 6.0
450
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), mutant enzyme Y216F, pH 6.0
630
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), mutant enzyme Y216F, pH 7.5
1100
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), mutant enzyme S150A, pH 9.2
1200
D-alanine
37°C, KM-value for D-alanine2 (the second molecule of substrate that is activated by the enzyme molecule), mutant enzyme Y216F, pH 9.2
0.008
ATP
-
mutant enzyme Y216K
0.033
ATP
-
mutant enzyme Y216F
0.049
ATP
-
wild-type enzyme
0.055
ATP
-
mutant enzyme E15Q
0.161
ATP
-
mutant enzyme H63Q
0.179
ATP
-
mutant enzyme S150A
2.4
ATP
-
mutant enzyme K144A
2.5
ATP
-
mutant enzyme K144T
0.0012
D-Ala
-
N-terminal Ala, wild-type enzyme
0.0033
D-Ala
-
N-terminal Ala, ligase B
0.0057
D-Ala
-
C-terminal Ala, ligase A
0.26
D-Ala
-
N-terminal Ala, mutant enzyme Y216F
0.43
D-Ala
-
N-terminal Ala, mutant enzyme E15Q, mutant enzyme Y216K
0.49
D-Ala
-
N-terminal Ala, mutant enzyme L282R
0.55
D-Ala
-
D-Ala, C-terminal, ligase A
0.55
D-Ala
-
N-terminal Ala, mutant enzyme H63Q
0.76
D-Ala
-
N-terminal Ala, mutant enzyme S150A
1.05
D-Ala
-
C-terminal Ala, mutant enzyme D257N
1.13
D-Ala
-
C-terminal Ala, wild-type enzyme
1.2
D-Ala
-
C-terminal Ala, ligase B
5.4
D-Ala
-
reaction with D-Met + ATP
6.4
D-Ala
-
reaction with D-Phe + ATP
20.9
D-Ala
-
C-terminal Ala, mutant enzyme L282R
22.8
D-Ala
-
C-terminal Ala, mutant enzyme K144A, reaction with 5 mM ATP
22.9
D-Ala
-
C-terminal Ala, mutant enzyme K144A, reaction with 15 mM ATP
25.7
D-Ala
-
C-terminal Ala, mutant enzyme Y216F
43.7
D-Ala
-
C-terminal Ala, mutant enzyme E15Q
57.5
D-Ala
-
C-terminal Ala, mutant enzyme H63Q
60.4
D-Ala
-
C-terminal Ala, mutant enzyme S150A
70.3
D-Ala
-
C-terminal Ala, mutant enzyme K144T, reaction with 5 mM ATP
86
D-Ala
-
C-terminal Ala, mutant enzyme K144T, reaction with 15 mM ATP
additional information
additional information
steady-state kinetics of ATP hydrolysis
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic analysis
-
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1.4
D-alanine
37°C, mutant enzyme S150A, kcat/Km(D-alanine2), pH 6.0. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
2.4
D-alanine
37°C, mutant enzyme E15Q, kcat/Km(D-alanine2), pH 6.0. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
3
D-alanine
37°C, mutant enzyme Y216F, kcat/Km(D-alanine2), pH 6.0. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
11
D-alanine
37°C, mutant enzyme E15Q, kcat/Km(D-alanine2), pH 7.5. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
12
D-alanine
37°C, mutant enzyme S150A, kcat/Km(D-alanine2), pH 7.5. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
17
D-alanine
37°C, mutant enzyme E15Q, kcat/Km(D-alanine2), pH 9.2. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
26
D-alanine
37°C, mutant enzyme S150A, kcat/Km(D-alanine2), pH 9.2. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
39
D-alanine
37°C, mutant enzyme Y216F, kcat/Km(D-alanine2), pH 7.5. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
89
D-alanine
37°C, wild-type enzyme, kcat/Km(D-alanine2), pH 6.0. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
260
D-alanine
37°C, mutant enzyme Y216F, kcat/Km(D-alanine2), pH 9.2. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
440
D-alanine
37°C, wild-type enzyme, kcat/Km(D-alanine2), pH 7.5. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
1500
D-alanine
37°C, wild-type enzyme, kcat/Km(D-alanine2), pH 9.2. D-Alanine2 is the second molecule of substrate that is activated by the enzyme molecule
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0.133
(E)-N,N'-bis(2-chloroethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.123
(E)-N,N'-bis(pyridin-3-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.049
(E)-N-(2-chloroethyl)-N'-(4-isopropylphenyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.119
(E)-N-(2-chloroethyl)-N'-(pyridin-2-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.236
(E)-N-(2-chloroethyl)-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.015
(E)-N-(3-chlorophenyl)-N'-(pyridin-3-ylmethyl)diazene-1,2-dicarboxamide
0.033
(E)-N-(3-chlorophenyl)-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
0.073
(E)-N-(4-fluorophenyl)-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.025
(E)-N-(4-sec-butylphenyl)-N'-(2-chloroethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.121
(E)-N-cyclohexyl-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.111
(E)-N-phenyl-N'-(pyridin-2-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.036
(E)-N-phenyl-N'-(pyridin-3-ylmethyl)diazene-1,2-dicarboxamide
0.106
(E)-N-phenyl-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.025
(E)-N-[4-(butan-2-yl)phenyl]-N'-(2-chloroethyl)diazene-1,2-dicarboxamide
Escherichia coli
pH 8.0, 37°C
0.135
1-[4-[(6-chloro-2-methoxyacridin-9-yl)amino]phenyl]-3-(dimethylamino)propan-1-ol
Escherichia coli
-
pH 8.0, 37°C
0.046
2,5,11-trimethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
Escherichia coli
-
pH 8.0, 37°C
0.07
3-(9-methoxy-5,11-dimethyl-6H-pyrido[4,3-b]carbazol-6-yl)propan-1-amine
Escherichia coli
-
pH 8.0, 37°C
0.119
3-[(1,6-dichloro-4-methoxyacridin-9-yl)amino]-2-[(diethylamino)methyl]phenol
Escherichia coli
-
pH 8.0, 37°C
0.102
3-[(6-chloro-2-methoxyacridin-9-yl)amino]-2-(pyrrolidin-1-ylmethyl)phenol
Escherichia coli
-
pH 8.0, 37°C
0.162
3-[(6-chloro-2-methoxyacridin-9-yl)amino]-2-[(4-methylpiperazin-1-yl)methyl]phenol
Escherichia coli
-
pH 8.0, 37°C
0.161
3-[(6-chloro-2-methoxyacridin-9-yl)amino]-2-[(diethylamino)methyl]-6-(prop-2-en-1-yl)phenol
Escherichia coli
-
pH 8.0, 37°C
0.32
3-[(6-chloro-2-methoxyacridin-9-yl)amino]-2-[(diethylamino)methyl]phenol
Escherichia coli
-
pH 8.0, 37°C
0.192
5,11-Dimethyl-6H-pyrido[4,3-b]carbazole
Escherichia coli
-
pH 8.0, 37°C
0.032 - 0.09
6-chloro-2-methoxy-N-(6-methoxyquinolin-8-yl)acridin-9-amine
0.125
7-ethyl-5,11-dimethyl-6H-pyrido[4,3-b]carbazole
Escherichia coli
-
pH 8.0, 37°C
0.064
8-fluoro-2,5,11-trimethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
Escherichia coli
-
pH 8.0, 37°C
0.103
8-fluoro-5,11-dimethyl-6H-pyrido[4,3-b]carbazole
Escherichia coli
-
pH 8.0, 37°C
0.09
8-fluoro-5,6,11-trimethyl-6H-pyrido[4,3-b]carbazole
Escherichia coli
-
pH 8.0, 37°C
0.023
9-bromo-2,5,11-trimethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
Escherichia coli
-
pH 8.0, 37°C
0.036
9-bromo-2,5,6,11-tetramethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
Escherichia coli
-
pH 8.0, 37°C
0.086
9-bromo-5,11-dimethyl-6H-pyrido[4,3-b]carbazole
Escherichia coli
-
pH 8.0, 37°C
0.297
9-bromo-5,6,11-trimethyl-6H-pyrido[4,3-b]carbazole
Escherichia coli
-
pH 8.0, 37°C
0.089
9-methoxy-2,5,11-trimethyl-6H-pyrido[4,3-b]carbazol-2-ium acetate
Escherichia coli
-
pH 8.0, 37°C
0.065
9-methoxy-2,5,11-trimethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
Escherichia coli
-
pH 8.0, 37°C
0.043
9-methoxy-2,5,6,11-tetramethyl-6H-pyrido[4,3-b]carbazol-2-ium iodide
Escherichia coli
-
pH 8.0, 37°C
0.06
9-methoxy-5,11-dimethyl-6H-pyrido[4,3-b]carbazole
Escherichia coli
-
pH 8.0, 37°C
0.184
9-methoxy-5,6,11-trimethyl-6H-pyrido[4,3-b]carbazole
Escherichia coli
-
pH 8.0, 37°C
0.163
apigenin
Escherichia coli
-
pH 7.4, 25°C
0.33 - 0.623
N-[(3-chloro-8-methoxy-11H-indolo[3,2-c]quinolin-9-yl)methyl]-N-ethylethanamine
0.0199
quercetin
Escherichia coli
-
pH 7.4, 25°C
0.015
(E)-N-(3-chlorophenyl)-N'-(pyridin-3-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.015
(E)-N-(3-chlorophenyl)-N'-(pyridin-3-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
pH 8.0, 37°C
0.033
(E)-N-(3-chlorophenyl)-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.033
(E)-N-(3-chlorophenyl)-N'-(pyridin-4-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
pH 8.0, 37°C
0.036
(E)-N-phenyl-N'-(pyridin-3-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
-
0.036
(E)-N-phenyl-N'-(pyridin-3-ylmethyl)diazene-1,2-dicarboxamide
Escherichia coli
pH 8.0, 37°C
0.032
6-chloro-2-methoxy-N-(6-methoxyquinolin-8-yl)acridin-9-amine
Escherichia coli
-
pH 8.0, 37°C
0.09
6-chloro-2-methoxy-N-(6-methoxyquinolin-8-yl)acridin-9-amine
Escherichia coli
-
pH 8.0, 37°C
0.33
N-[(3-chloro-8-methoxy-11H-indolo[3,2-c]quinolin-9-yl)methyl]-N-ethylethanamine
Escherichia coli
-
pH 8.0, 37°C
0.623
N-[(3-chloro-8-methoxy-11H-indolo[3,2-c]quinolin-9-yl)methyl]-N-ethylethanamine
Escherichia coli
-
pH 8.0, 37°C
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Shi, Y.; Walsh, C.T.
Active site mapping of Escherichia coli D-Ala-D-Ala ligase by structure-based mutagenesis
Biochemistry
34
2768-2776
1995
Escherichia coli
brenda
Lugtenberg, E.J.J.; van Schijndel-van Dam, A.
Temperature-sensitive mutant of Escherichia coli K-12 with an impaired D-alanine:D-alanine ligase
J. Bacteriol.
113
96-104
1973
Escherichia coli
brenda
Bugg, T.D.H.; Dutka-Malen, S.; Athur, M.; Courvalin, P.; Walsh, C.T.
Identification of vancomycin resistance protein VanA as a D-alanine:D-alanine ligase of altered substrate specificity
Biochemistry
30
2017-2021
1991
Escherichia coli, Escherichia coli JM105
brenda
Lugtenberg, E.J.J.
Studies on Escherichia coli enzymes involved in the synthesis of uridine diphosphate-N-acetyl-muramyl-pentapeptide
J. Bacteriol.
110
26-34
1972
Escherichia coli
brenda
Zawadzke, L.E.; Bugg, T.D.H.; Walsh, C.T.
Existence of two D-alanine:D-alanine ligases in Escherichia coli: cloning and sequencing of the ddlA gene and purification and characterization of the DdlA and DdlB enzymes
Biochemistry
30
1673-1682
1991
Escherichia coli
brenda
Fan, C.; Park, I.S.; Walsh, C.T.; Knox, J.R.
D-Alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant
Biochemistry
36
2531-2538
1997
Escherichia coli (P07862), Escherichia coli
brenda
Duncan, K.; van Heijenoort, J.; Walsh, C.T.
Purification and characterization of the D-alanyl-D-alanine-adding enzyme from Escherichia coli
Biochemistry
29
2379-2386
1990
Escherichia coli
brenda
Ellsworth, B.A.; Tom, N.J.; Bartlett, P.A.
Synthesis and evaluation of inhibitors of bacterial D-alanine:D-alanine ligases
Chem. Biol.
3
37-44
1996
Escherichia coli, Enterococcus faecium
brenda
Al-Bar, O.A.M.; OConnor, C.D.; Giles, I.G.; Akhtar, M.
D-Alanine:D-alanine ligase of Escherichia coli. Expression, purification and inhibitory studies on the cloned enzyme
Biochem. J.
282
747-752
1992
Escherichia coli
brenda
Fan, C.; Moews, P.C.; Walsh, C.T.; Knox, J.R.
Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution
Science
266
439-443
1994
Escherichia coli
brenda
Healy, V.L.; Park, I.S.; Walsh, C.T.
Active-site mutants of the VanC2 D-alanyl-D-serine ligase, characteristic of one vancomycin-resistant bacterial phenotype, revert towards wild-type D-alanyl-D-alanine ligases
Chem. Biol.
5
197-207
1998
Escherichia coli
brenda
Sato, M.; Kirimura, K.; Kino, K.
D-Amino acid dipeptide production utilizing D-alanine-D-alanine ligases with novel substrate specificity
J. Biosci. Bioeng.
99
623-628
2005
Escherichia coli, Oceanobacillus iheyensis, Synechocystis sp. PCC 6803, Thermotoga maritima, Oceanobacillus iheyensis JCM 11309
brenda
Kovac, A.; Majce, V.; Lenarsic, R.; Bombek, S.; Bostock, J.M.; Chopra, I.; Polanc, S.; Gobec, S.
Diazenedicarboxamides as inhibitors of D-alanine-D-alanine ligase (Ddl)
Bioorg. Med. Chem. Lett.
17
2047-2054
2007
Escherichia coli (P07862), Escherichia coli
brenda
Triola, G.; Wetzel, S.; Ellinger, B.; Koch, M.; Huebel, K.; Rauh, D.; Waldmann, H.
ATP competitive inhibitors of D-alanine-D-alanine ligase based on protein kinase inhibitor scaffolds
Bioorg. Med. Chem.
17
1079-1087
2008
Escherichia coli (P07862)
brenda
Wu, D.; Kong, Y.; Han, C.; Chen, J.; Hu, L.; Jiang, H.; Shen, X.
D-Alanine:D-alanine ligase as a new target for the flavonoids quercetin and apigenin
Int. J. Antimicrob. Agents
32
421-426
2008
Escherichia coli, Helicobacter pylori
brenda
Batson, S.; Rea, D.; Fueloep, V.; Roper, D.I.
Crystallization and preliminary X-ray analysis of a D-alanyl-D-alanine ligase (EcDdlB) from Escherichia coli
Acta Crystallogr. Sect. F
66
405-408
2010
Escherichia coli
brenda
Sova, M.; Cadez, G.; Turk, S.; Majce, V.; Polanc, S.; Batson, S.; Lloyd, A.J.; Roper, D.I.; Fishwick, C.W.; Gobec, S.
Design and synthesis of new hydroxyethylamines as inhibitors of D-alanyl-D-lactate ligase (VanA) and D-alanyl-D-alanine ligase (DdlB)
Bioorg. Med. Chem. Lett.
19
1376-1379
2009
Enterococcus faecium, Escherichia coli
brenda
Park, I.-S.; Lin, C.-H.; Walsh, C.T.
Gain of D-alanyl-D-lactate or D-lactyl-D-alanine synthetase activities in three active-site mutants of the Escherichia coli D-alanyl-D-alanine ligase B
Biochemistry
35
10464-10471
1996
Escherichia coli (P07862), Escherichia coli
brenda
Vehar, B.; Hrast, M.; Kovac, A.; Konc, J.; Mariner, K.; Chopra, I.; O'Neill, A.; Janezic, D.; Gobec, S.
Ellipticines and 9-acridinylamines as inhibitors of D-alanine:D-alanine ligase
Bioorg. Med. Chem.
19
5137-5146
2011
Escherichia coli
brenda
Skedelj, V.; Arsovska, E.; Tomasic, T.; Kroflic, A.; Hodnik, V.; Hrast, M.; Bester-Rogac, M.; Anderluh, G.; Gobec, S.; Bostock, J.; Chopra, I.; O'Neill, A.J.; Randall, C.; Zega, A.
6-Arylpyrido[2,3-d]pyrimidines as novel ATP-competitive inhibitors of bacterial D-alanine:D-alanine ligase
PLoS ONE
7
e39922
2012
Escherichia coli
brenda
Batson, S.; de Chiara, C.; Majce, V.; Lloyd, A.J.; Gobec, S.; Rea, D.; Fueloep, V.; Thoroughgood, C.W.; Simmons, K.J.; Dowson, C.G.; Fishwick, C.W.G.; de Carvalho, L.P.S.; Roper, D.I.
Inhibition of D-Ala D-Ala ligase through a phosphorylated form of the antibiotic D-cycloserine
Nat. Commun.
8
1939
2017
Escherichia coli (P07862)
brenda