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ATP + 2 D-Ala
ADP + phosphate + D-Ala-D-Ala
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
ATP + beta-Ala
ADP + phosphate + ?
at 60°C activity is 1.3% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Ala + 2-aminopentanoate
ADP + phosphate + D-Ala-2-aminopentanoate
-
-
-
-
?
ATP + D-Ala + 2-hydroxybutanoate
ADP + phosphate + D-Ala-D-2-hydroxybutanoate
-
-
-
?
ATP + D-Ala + 2-hydroxypentanoate
ADP + phosphate + D-Ala-D-2-hydroxypentanoate
-
-
-
?
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-lactate
ADP + phosphate + D-Ala-D-lactate
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-Ala + NH3
ADP + phosphate + D-AlaNH2
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-Arg
ADP + phosphate + D-Arg-D-Arg
at 60°C activity is 0.43% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Asn
ADP + phosphate + D-Asn-D-Asn
at 60°C activity is 0.22% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Asp
ADP + phosphate + D-Asp-D-Asp
at 60°C activity is 0.051% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Cys
ADP + phosphate + D-Cys-D-Cys
at 60°C activity is 29% of the activity with D-Ala
-
-
?
ATP + D-Gln
ADP + phosphate + D-Gln-D-Gln
at 60°C activity is 0.56% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Glu
ADP + phosphate + D-Glu-D-Glu
at 60°C activity is 0.012% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-His
ADP + phosphate + D-His-D-His
at 60°C activity is 0.49% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Ile
ADP + phosphate + D-Ile-D-Ile
at 60°C activity is 0.36% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Leu
ADP + phosphate + D-Leu-D-Leu
at 60°C activity is 0.31% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Lys
ADP + phosphate + D-Lys-D-Lys
at 60°C activity is 0.6% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Met
ADP + phosphate + D-Met-D-Met
at 60°C activity is 0.34% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Phe
ADP + phosphate + D-Phe-D-Phe
at 60°C activity is 0.31% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Pro
ADP + phosphate + D-Pro-D-Pro
at 60°C activity is 0.29% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Ser
ADP + phosphate + D-Ser-D-Ser
at 60°C activity is 16% of the activity with D-Ala
-
-
?
ATP + D-serine
ADP + phosphate + D-alanyl-D-serine
-
-
-
?
ATP + D-Thr
ADP + phosphate + D-Thr-D-Thr
at 60°C activity is 2.2% of the activity with D-Ala
-
-
?
ATP + D-Trp
ADP + phosphate + D-Trp-D-Trp
at 60°C activity is 0.1% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + D-Val
ADP + phosphate + D-Val-D-Val
at 60°C activity is 0.43% of the activity with D-Ala, no activity at 37°C
-
-
?
ATP + Gly
ADP + phosphate + Gly-Gly
at 60°C activity is 3.6% of the activity with D-Ala
-
-
?
beta-alanine + beta-alanine + ATP
beta-alanyl-beta-alanine + ADP + phosphate
-
1.3% of the activity with D-serine
-
?
D-alanine + D-alanine + ATP
D-alanyl-D-alanine + ADP + phosphate
-
-
-
?
D-cysteine + ATP
ADP + D-cysteinyl-D-cysteine
D-cysteine + D-cysteine + ATP
D-cysteinyl-D-cysteine + ADP + phosphate
-
29% of the activity with D-serine
-
?
D-serine + ATP
ADP + D-serinyl-D-serine
D-serine + D-serine + ATP
D-seryl-D-serine + ADP + phosphate
-
16% of the activity with D-serine
-
?
D-threonine + ATP
ADP + D-threonyl-D-threonine
D-threonine + D-threonine + ATP
D-threonyl-D-threonine + ADP + phosphate
-
2.2% of the activity with D-serine
-
?
glycine + D-alanine + ATP
glycyl-D-alanine + ADP + phosphate
-
3.6% of the activity with D-serine
-
?
glycine + glycine + ATP
ADP + Gly-Gly + phosphate
additional information
?
-
ATP + 2 D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
-
?
ATP + 2 D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
-
?
ATP + 2 D-Ala
ADP + phosphate + D-Ala-D-Ala
-
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
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 + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
DdlA catalyzes the dimerization of two D-alanine molecules and typically couples ATP hydrolysis to provide a thermodynamic driving force and exhibits a cleavage of ATP to ADP and phosphate. D-Alanine is completely converted into D-alanyl-D-alanine, so no remaining D-alanine is detected
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
DdlA catalyzes the dimerization of two D-alanine molecules and typically couples ATP hydrolysis to provide a thermodynamic driving force and exhibits a cleavage of ATP to ADP and phosphate. D-Alanine is completely converted into D-alanyl-D-alanine, so no remaining D-alanine is detected
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + 2 D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + Ala + Ala
?
-
the finding that the reactions of EC 6.3.2.4 and EC 6.3.2.10 are reversible may represent a functional regulatory mechanism which determines the level of the lysine-containing UDPMurNAc-pentapeptide depending on the intracellular ATP/ADP ratio
-
-
?
ATP + Ala + Ala
?
-
second step in the biosynthesis of bacterial peptidoglycan
-
-
?
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 + Ala + Ala
?
-
enzyme involved in peptidoglycan precursor synthesis during sporulation
-
-
?
ATP + Ala + Ala
?
-
enzyme involved in peptidoglycan precursor synthesis during sporulation
-
-
?
ATP + Ala + Ala
?
-
one step in peptidoglycan synthesis: the formation of D-Ala-D-Ala, the terminal dipeptide of the UDP-N-acetylmuramylpentapeptide
-
-
?
ATP + Ala + Ala
?
-
second enzyme in the three enzyme D-alanine branch of peptidoglycan biosynthesis
-
-
?
ATP + Ala + Ala
?
-
the finding that the reactions of EC 6.3.2.4 and EC 6.3.2.10 are reversible may represent a functional regulatory mechanism which determines the level of the lysine-containing UDPMurNAc-pentapeptide depending on the intracellular ATP/ADP ratio
-
-
?
ATP + Ala + Ala
?
-
one step in peptidoglycan synthesis: the formation of D-Ala-D-Ala, the terminal dipeptide of the UDP-N-acetylmuramylpentapeptide
-
-
?
ATP + D-Ala + D-2-aminopentanoate
ADP + phosphate + D-Ala-D-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-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-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
-
-
-
?
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-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
-
-
-
?
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-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-lactate
ADP + phosphate + D-Ala-D-lactate
-
-
-
?
ATP + D-Ala + D-lactate
ADP + phosphate + D-Ala-D-lactate
-
enzyme uses both D-Ala and D-lactate as a substrate
-
-
?
ATP + D-Ala + D-lactate
ADP + phosphate + D-Ala-D-lactate
-
-
?
ATP + D-Ala + D-lactate
ADP + phosphate + D-Ala-D-lactate
-
-
depsipeptide D-Ala-D-lactate is responsible for the intrinsic resistance of Leuconostoc mesenteroides to vancomycin
-
?
ATP + D-Ala + D-lactate
ADP + phosphate + D-Ala-D-lactate
-
D-lactate is not a substrate for wild-type, but for mutants S137A/Y207F, S137F/Y207F, S137T/Y207F, S137G/Y207F, Y207F
-
-
?
ATP + D-Ala + D-lactate
ADP + phosphate + D-Ala-D-lactate
-
D-lactate is not a substrate for wild-type, but for mutants S137A/Y207F, S137F/Y207F, S137T/Y207F, S137G/Y207F, Y207F
-
-
?
ATP + D-Ala + D-Met
ADP + phosphate + D-Ala-D-Met
-
-
-
-
?
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-norleucine
ADP + phosphate + D-Ala-D-norleucine
-
-
-
-
?
ATP + D-Ala + D-Phe
ADP + phosphate + D-Ala-D-Phe
-
-
-
-
?
ATP + D-Ala + D-Phe
ADP + phosphate + D-Ala-D-Phe
-
-
-
-
?
ATP + D-Ala + NH3
ADP + phosphate + D-AlaNH2
the D-AlaNH2 production of enzyme S293X mutants is optimized, the S293E variant, which is selected as the best enzyme for D-AlaNH2 production, exhibits an optimal activity at pH 9.0 and 40°C for D-AlaNH2 production. The S293E variant catalyzes the synthesis of 9.3 and 35.7 mM of D-AlaNH2 from 10 and 50 mM D-Ala and 3 M NH4Cl with conversion yields of 93% and 71.4%, respectively. The S293E variant exhibits higher reaction specificity to D-AlaNH2 production compared with the S293D variant and the other variants
-
-
?
ATP + D-Ala + NH3
ADP + phosphate + D-AlaNH2
the D-AlaNH2 production of enzyme S293X mutants is optimized, the S293E variant, which is selected as the best enzyme for D-AlaNH2 production, exhibits an optimal activity at pH 9.0 and 40°C for D-AlaNH2 production. The S293E variant catalyzes the synthesis of 9.3 and 35.7 mM of D-AlaNH2 from 10 and 50 mM D-Ala and 3 M NH4Cl with conversion yields of 93% and 71.4%, respectively. The S293E variant exhibits higher reaction specificity to D-AlaNH2 production compared with the S293D variant and the other variants
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
essential enzyme
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
the enzyme shows relatively weak binding affinity and poor catalytic activity against the substrate D-Ala in vitro, active site structure, overview
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
D-alanine:D-alanine ligase is an essential enzyme in bacterial cell wall biosynthesis and an important target for developing new antibiotics
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
-
-
-
-
?
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-alanine + D-serine
ADP + D-alanyl-D-serine + D-alanyl-D-alanine + D-seryl-D-serine
-
-
-
-
?
ATP + D-alanine + D-serine
ADP + D-alanyl-D-serine + D-alanyl-D-alanine + D-seryl-D-serine
-
-
-
-
?
D-cycloserine
?
-
-
-
-
?
D-cycloserine
?
-
-
-
-
?
D-cycloserine
?
-
-
-
-
?
D-cysteine + ATP
ADP + D-cysteinyl-D-cysteine
-
-
-
-
?
D-cysteine + ATP
ADP + D-cysteinyl-D-cysteine
-
-
-
-
?
D-cysteine + ATP
ADP + D-cysteinyl-D-cysteine
-
-
-
-
?
D-serine + ATP
ADP + D-serinyl-D-serine
-
-
-
-
?
D-serine + ATP
ADP + D-serinyl-D-serine
-
-
-
-
?
D-serine + ATP
ADP + D-serinyl-D-serine
-
-
-
-
?
D-threonine + ATP
ADP + D-threonyl-D-threonine
-
-
-
-
?
D-threonine + ATP
ADP + D-threonyl-D-threonine
-
-
-
-
?
D-threonine + ATP
ADP + D-threonyl-D-threonine
-
-
-
-
?
dipeptides + ATP
?
-
-
-
-
?
dipeptides + ATP
?
-
-
-
-
?
dipeptides + ATP
?
-
-
-
-
?
dipeptides + ATP
?
-
-
-
-
?
dipeptides + ATP
?
-
-
-
-
?
glycine + glycine + ATP
ADP + Gly-Gly + phosphate
-
-
-
-
?
glycine + glycine + ATP
ADP + Gly-Gly + phosphate
-
-
-
-
?
glycine + glycine + ATP
ADP + Gly-Gly + phosphate
-
-
-
-
?
additional information
?
-
-
the enzyme is also capable of synthesizing fluorinated dipeptides
-
-
?
additional information
?
-
DDl is an essential enzyme in bacterial cell wall biosynthesis
-
-
?
additional information
?
-
no activity with D-Ser, Gly, and D-lactate
-
-
?
additional information
?
-
-
no activity with D-Ser, Gly, and D-lactate
-
-
?
additional information
?
-
putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
substrate specificity expands at high temperature. At 37°C, enzyme shows reactivity only for D-alanine, D-serine, D-threonine, D-cysteine and glycine. At 60°C, substrates additionally include D-lysine, D-glutamine, D-histidine, D-arginine, D-valine, D-isoleucine, D-methionine, D-leucine, D-phenylalanine, D-proline, and D-asparagine, all below 1% of the activity with D-alanine
-
-
?
additional information
?
-
substrate specificity expands at high temperature. At 37°C, enzyme shows reactivity only for D-alanine, D-serine, D-threonine, D-cysteine and glycine. At 60°C, substrates additionally include D-lysine, D-glutamine, D-histidine, D-arginine, D-valine, D-isoleucine, D-methionine, D-leucine, D-phenylalanine, D-proline, and D-asparagine, all below 1% of the activity with D-alanine
-
-
?
additional information
?
-
substrate-binding mechanism of enzyme YpDDL involving conformational changes of the loops, overview. Two D-alanine-binding sites are located next to each other between the N-terminal domain and the C-terminal domain, and an ATP-binding site exists between the central and the C-terminal domains
-
-
?
additional information
?
-
-
substrate-binding mechanism of enzyme YpDDL involving conformational changes of the loops, overview. Two D-alanine-binding sites are located next to each other between the N-terminal domain and the C-terminal domain, and an ATP-binding site exists between the central and the C-terminal domains
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(1-aminoethyl)boronic acid
-
time-dependent, slow binding
(1E,3Z)-N-(2-carbamimidamidoethyl)-4-(pyridin-3-yl)buta-1,3-diene-1-sulfonamide
-
(2-aminoethyl)phosphonic acid
-
(2E)-3-amino-2-[(E)-(3-hydroxy-4-oxocyclohexa-2,5-dien-1-ylidene)methyl]-3-sulfanylprop-2-enenitrile
-
(2R)-2-aminopropanoyl hydrogen (2-hydroxybutanoyl)phosphonate
-
(2R)-2-[[(1-aminoethyl)(hydroxy)phosphoryl]methyl]nonanoic acid
-
(2S)-2-amino-4-[(3S)-3-hydroxy-2-oxoazetidin-3-yl]butanoic acid
-
(2Z)-2-cyano-3-hydroxy-N-(2,4,6-trimethylphenyl)but-2-enamide
-
(2Z)-2-cyano-3-hydroxy-N-[2-methyl-3,6-bis(trifluoromethyl)phenyl]but-2-enamide
-
(2Z)-2-cyano-3-hydroxy-N-[4-(trifluoromethoxy)phenyl]but-2-enamide
-
(2Z)-2-cyano-N-(2,5-dibromophenyl)-3-hydroxybut-2-enamide
-
(2Z)-2-cyano-N-(2,6-dimethylphenyl)-3-hydroxybut-2-enamide
-
(2Z)-N-(2-chloro-6-methylphenyl)-2-cyano-3-hydroxybut-2-enamide
-
(2Z)-N-(2-chloro-6-methylphenyl)-2-ethynyl-3-hydroxybut-2-enamide
(3-Amino-2-oxoalkyl)phosphonic acids
-
e.g. (3(R)-amino-2-oxobutyl)phosphonic acid and the corresponding aza analogue
(3Z)-4-cyano-5-(3,6-dibromo-2-methylanilino)-3-hydroxy-5-oxopent-3-enoic acid
-
(4R)-4-amino-1,2-oxazolidin-3-one
-
(E)-2-[[(chloromethyl)amino]acetyl]-N-[(pyridin-2-yl)methyl]diazene-1-carboxamide
-
(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
-
(E)-N1,N2-bis(2-chloroethyl)diazene-1,2-dicarboxamide
-
(E)-N1,N2-bis[(pyridin-3-yl)methyl]diazene-1,2-dicarboxamide
-
(E)-N1-(2-chloroethyl)-N2-(4-methylphenyl)diazene-1,2-dicarboxamide
-
(E)-N1-(2-chloroethyl)-N2-[(pyridin-4-yl)methyl]diazene-1,2-dicarboxamide
-
(E)-N1-(3-chlorophenyl)-N2-[(pyridin-3-yl)methyl]diazene-1,2-dicarboxamide
-
(E)-N1-(3-chlorophenyl)-N2-[(pyridin-4-yl)methyl]diazene-1,2-dicarboxamide
-
(E)-N1-(4-fluorophenyl)-N2-[(pyridin-4-yl)methyl]diazene-1,2-dicarboxamide
-
(E)-N1-cyclohexyl-N2-[(pyridin-2-yl)methyl]diazene-1,2-dicarboxamide
-
(E)-N1-cyclohexyl-N2-[(pyridin-4-yl)methyl]diazene-1,2-dicarboxamide
-
(E)-N1-phenyl-N2-[(pyridin-3-yl)methyl]diazene-1,2-dicarboxamide
-
(E)-N1-phenyl-N2-[(pyridin-4-yl)methyl]diazene-1,2-dicarboxamide
-
(E)-N1-[4-(butan-2-yl)phenyl]-N2-(2-chloroethyl)diazene-1,2-dicarboxamide
-
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-[(4-fluorocyclohexane-1-sulfonyl)amino]-3-(morpholin-4-yl)propan-2-yl dihydrogen phosphate
-
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
1-[[(4-fluorophenyl)sulfonyl]amino]-3-(morpholin-4-yl)propan-2-yl phenyl hydrogen phosphate
-
0.5 mM, 65% inhibition
1-[[(4-methoxyphenyl)sulfonyl]amino]-3-(morpholin-4-yl)propan-2-yl dihydrogen phosphate
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-(3,4-dihydroxyphenyl)-3,5,7-trihydroxy-4H-1-benzopyran-4-one
-
2-(3-methylmorpholin-4-yl)-8-phenyl-2,3-dihydro-4H-1-benzopyran-4-one
-
2-([(1R)-1-aminoethyl](hydroxy)phosphoryl]methyl)octanoic acid
-
2-amino-4-(3,4,5-trihydroxyphenyl)but-1-ene-1,1,3-tricarbonitrile
-
2-aminoethylphosphonate
-
weak
2-cyano-3-hydroxy-N-[2-methyl-4-(trifluoromethyl)phenyl]butanamide
-
2-hydroxy-N-(2,4,6-trimethylphenyl)benzamide
-
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
-
-
2-[[(1-aminoethyl)(hydroxy)phosphoryl]methyl]nonanoic acid
-
2-[[6-(benzylamino)-9-methyl-9H-purin-2-yl]amino]ethan-1-ol
-
3-(9-methoxy-5,11-dimethyl-6H-pyrido[4,3-b]carbazol-6-yl)propan-1-amine
-
-
3-chloro-2,2-dimethyl-N-[4(trifluoromethyl)phenyl]propanamide
the inhibitor binds to a hydrophobic pocket at the interface of the first and the third domain. This inhibitor-binding pocket is adjacent to the first D-alanine substrate site but does not overlap with any substrate sites
3-chloro-2,2-dimethyl-N-[4-(trifluoromethyl)cyclohexyl]propanamide
-
3-chloro-2,2-dimethyl-N-[4-(trifluoromethyl)phenyl]propanamide
-
binding structure, overview
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
-
-
3-[[(1S)-1-aminoethyl](hydroxy)phosphoryl]-2-methylpropanoic acid
-
4-chloro-3,3-dimethyl-N-[4-(trifluoromethyl)phenyl]butanamide
-
4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]benzene-1,2-diol
-
5,11-Dimethyl-6H-pyrido[4,3-b]carbazole
-
-
5,6,11-trimethyl-6H-pyrido[4,3-b]carbazole
-
-
5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-1-benzopyran-4-one
-
5-methyl-N-[4-(trifluoromethyl)phenyl]-1,2-oxazole-4-carboxamide
-
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-(3,5-dimethylphenyl)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
-
-
alpha-Aminophosphonamidic acid
-
time-dependent inhibition in presence of ATP
Aminoalkylphosphinate
-
-
-
D-(1-Aminoethyl)phosphinic acid
-
competitive
D-(1-Aminoethyl)phosphonic acid
D-3-[(1-Aminoethyl)phosphinyl]-2-heptylpropionic acid
-
potent active site directed inhibitor, competitive with D-Ala, time-dependent inhibition in the presence of ATP
D-Ala-D-2-hydroxybutanoate phosphonate
-
D-Ala-D-Ala phosphinate
-
EDTA
10 mM, complete inhibition
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
methylphosphinophosphate
-
strong inhibition
-
N-(2,5-dibromophenyl)-2-oxopropanamide
N-(2,6-dimethylphenyl)-2-hydroxybenzamide
-
N-(2-amino-6-phenylpyrido[2,3-d]pyrimidin-7-yl)-N'-tert-butylurea
-
N-(3,6-dibromo-2-methylphenyl)-2-hydroxybenzamide
-
N-tert-butyl-N'-[6-(2,6-dichlorophenyl)-2-[[3-(morpholin-4-yl)propyl]amino]pyrido[2,3-d]pyrimidin-7-yl]urea
-
N-tert-butyl-N'-[6-(3,5-dimethoxyphenyl)-2-[[3-(morpholin-4-yl)propyl]amino]pyrido[2,3-d]pyrimidin-7-yl]urea
-
N-[(1,4-dimethyl-9H-carbazol-3-yl)methyl]-2,2-diethoxyethanamine
-
-
N-[(2S)-1-[(dihydroxyphosphanyl)oxy]-1-oxopropan-2-yl]-D-alaninamide
-
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
-
-
N-[2-amino-6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidin-7-yl]-N'-tert-butylurea
-
N-[2-amino-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-7-yl]-N'-tert-butylurea
-
N-[2-amino-6-(2,6-difluorophenyl)pyrido[2,3-d]pyrimidin-7-yl]-N'-tert-butylurea
-
N-[2-amino-6-(2-chloro-6-fluorophenyl)pyrido[2,3-d]pyrimidin-7-yl]-N'-tert-butylurea
-
N-[2-amino-6-(3,5-dichlorophenyl)pyrido[2,3-d]pyrimidin-7-yl]-N'-tert-butylurea
-
N-[2-amino-6-(3,5-difluorophenyl)pyrido[2,3-d]pyrimidin-7-yl]-N'-tert-butylurea
-
N-[2-amino-6-(3,5-dimethoxyphenyl)pyrido[2,3-d]pyrimidin-7-yl]-N'-tert-butylurea
-
N-[2-amino-6-[3,5-bis(trifluoromethyl)phenyl]pyrido[2,3-d]pyrimidin-7-yl]-N'-tert-butylurea
-
N2-(3-aminopropyl)-6-(3,5-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
P-(aminomethyl)phosphonamidic acid
-
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
Phosphonate dipeptide analogs
-
phosphorylated D-ala-D-alpha-hydroxybutyrate phosphonate
-
binding structure, overview
piceatannol
slight inhibition
Tabtoxinine
-
no inhibition by the lactam analogues
tyrphostin 47
competitive versus ATP
tyrphostin 51
mixed-type inhibition
Vancomycin
the antibiotic is primarily used against methicillin-resistant Staphylococcus, it recognizes the terminal D-Ala-D-Ala moiety of the peptide chain of peptidoglycan and inhibits the cross-linking of cell-wall peptidoglycan precursors, eventually causing bacterial cell lysis
Wortmannin
slight inhibition
[(1R)-1-aminoethyl]phosphinic acid
-
[(1R)-1-aminoethyl]phosphonic acid
-
[1(S)-Aminoethyl][(2RS)2-carboxy-1-octyl]phosphinic acid
-
classical slow-binding
[1(S)-aminoethyl][2-carboxy-2(R)-methyl-1-ethyl]phosphinic acid
-
ATP-dependent, slow-binding, enzyme-inhibitor half-life is 17 days at 37°C, mechanism of inactivation involves phosphorylation of the enzyme-bound inhibitor by ATP to form a phosphoryl-phosphinate adduct
[3-chloro-2,2-dimethyl-N-4(trimethylfluoro)phenyl]propanamide
-
(2Z)-N-(2-chloro-6-methylphenyl)-2-ethynyl-3-hydroxybut-2-enamide
-
(2Z)-N-(2-chloro-6-methylphenyl)-2-ethynyl-3-hydroxybut-2-enamide
-
1-[[(4-fluorophenyl)sulfonyl]amino]-3-(morpholin-4-yl)propan-2-yl dihydrogen phosphate
-
0.5 mM, 75% inhibition
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
1-[[(4-methoxyphenyl)sulfonyl]amino]-3-(morpholin-4-yl)propan-2-yl dihydrogen phosphate
-
0.5 mM, 83% inhibition
6-(2,6-dibromophenyl)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-(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)-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-dichlorophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
6-(2,6-difluorophenyl)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-(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-dichlorophenyl)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)-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-(3,5-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
6-phenylpyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-phenylpyrido[2,3-d]pyrimidine-2,7-diamine
-
6-[3,5-bis(trifluoromethyl)phenyl]pyrido[2,3-d]pyrimidine-2,7-diamine
-
-
6-[3,5-bis(trifluoromethyl)phenyl]pyrido[2,3-d]pyrimidine-2,7-diamine
-
apigenin
-
4',5,7-trihydroxyflavone, inhibition mechanism, competitive with respect to the substrate ATP and non-competitive to the substrate D-Ala
apigenin
-
4',5,7-trihydroxyflavone, inhibition mechanism, competitive with respect to the substrate ATP and non-competitive to the substrate D-Ala
D-(1-Aminoethyl)phosphonic acid
-
DL-
D-(1-Aminoethyl)phosphonic acid
-
DL-
D-(1-Aminoethyl)phosphonic acid
-
time-dependent inhibition in presence of ATP
D-alanyl-D-alanine
-
D-cycloserine
-
-
D-cycloserine
-
weak inhibition
D-cycloserine
competitive inhibitor
D-cycloserine
-
0.2 mg/ml, approx. 60% inhibition, 0.8 mg/ml, approx. 95% inhibition
D-cycloserine
preferential and weak inhibition at the second, lower-affinity binding site. D-cycloserine binding is tighter at higher ATP concentrations
D-cycloserine
-
a slow-onset inhibitor specifically to the Mycobacterium tuberculosis enzyme orthologue, inhibition mechanism, overview. D-Cycloserine binds exclusively to the C-terminal D-alanine binding site, even in the absence of bound D-alanine at the N-terminal binding site
D-cycloserine
-
interferes with the formation of peptidoglycan biosynthesis by competitive inhibition of alanine racemase and D-alanine-D-alanine ligase, the latter is the primary lethal target, inhibition mechanism and physiological effects, NMR metabolomic study, overview. D-Alanine is able to effectively compete with the inhibitor for uptake
D-cycloserine
a competitive inhibitor
D-cycloserine
0.2 mg/ml, approx. 50% inhibition, 0.8 mg/ml, approx. 80% inhibition
dipeptides
-
-
N-(2,5-dibromophenyl)-2-oxopropanamide
-
N-(2,5-dibromophenyl)-2-oxopropanamide
-
Phosphinates
-
weak inhibition of ligase B of E. coli and Van A from Enterococcus faecium, strong inhibition of ligase A from E. coli
-
Phosphinates
-
weak inhibition of ligase B of E. coli and Van A from Enterococcus faecium, strong inhibition of ligase A from E. coli
-
Phosphonate dipeptide analogs
-
weak inhibition of ligase B from E. coli and Van A from Enterococcus faecium
-
Phosphonate dipeptide analogs
-
weak inhibition of ligase B from E. coli and Van A from Enterococcus faecium
-
quercetin
-
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
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
additional information
-
proposed inhibitor binding site structure, overview
-
additional information
-
large reduction in binding affinity of the VanA mutant enzyme for all the phosphorus-containing analogs has significant implications for the design of inhibitors specific for this enzyme
-
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
-
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
-
additional information
-
6-arylpyrido[2,3-d]pyrimidines as novel ATP-competitive inhibitors of the bacterial enzyme, ligand docking and modeling, overview
-
additional information
inhibitor docking and molecular structure modeling, overview
-
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33
2-aminopentanoate
-
reaction with D-Ala + ATP
8.3
2-hydroxypentanoate
-
-
15
D-norleucine
-
reaction with D-Ala + ATP
6
D-Phe
-
reaction with D-Ala + ATP
additional information
additional information
-
0.00087
ATP
pH 8.0, 30°C
0.008
ATP
-
mutant enzyme Y216K
0.033
ATP
-
mutant enzyme Y216F
0.049
ATP
-
wild-type enzyme
0.0503
ATP
pH 8.0, 37°C, recombinant His-tagged enzyme
0.055
ATP
-
mutant enzyme E15Q
0.161
ATP
-
mutant enzyme H63Q
0.179
ATP
-
mutant enzyme S150A
1.7
ATP
-
pH 7.8, 45°C, first D-Ala
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
-
D-Ala, N-terminal Ala, + D-Ala, VanB
1.2
D-Ala
-
C-terminal Ala, ligase B
3.4
D-Ala
-
N-terminal Ala
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
34
D-Ala
-
C-terminal Ala, reaction with D-Ala + ATP, VanB
38
D-Ala
-
C-terminal Ala
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
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
0.008
D-alanine
-
pH 7.8, 45°C, first D-Ala
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
1.011
D-alanine
pH 8.0, 37°C, recombinant His-tagged enzyme
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
1.49
D-alanine
pH 9.0, 30°C
1.89
D-alanine
pH 8.0, 30°C
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
2.7
D-alanine
-
pH 7.8, 45°C, second D-Ala
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
7.35
D-alanine
pH 9.0, 40°C, mutant S293E
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
8.86
D-alanine
pH 9.0, 40°C, mutant S293D
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
1530
NH3
pH 9.0, 40°C, mutant S293D
1580
NH3
pH 9.0, 40°C, mutant S293E
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic analysis
-
additional information
additional information
-
kinetic analysis
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
steady-state kinetics
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics
-
additional information
additional information
steady-state kinetics of ATP hydrolysis
-
additional information
additional information
-
steady-state kinetics of the Michaelis-Menten equation with a single binding site
-
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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
0.37
D-cycloserine
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.33 - 0.623
N-[(3-chloro-8-methoxy-11H-indolo[3,2-c]quinolin-9-yl)methyl]-N-ethylethanamine
0.0199 - 0.0485
quercetin
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
0.1327
apigenin
Helicobacter pylori
-
pH 7.4, 25°C
0.163
apigenin
Escherichia coli
-
pH 7.4, 25°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
0.0199
quercetin
Escherichia coli
-
pH 7.4, 25°C
0.0485
quercetin
Helicobacter pylori
-
pH 7.4, 25°C
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E15Q
mutant enzyme with negligible depsipeptide synthetase activity. The mutant uniquely activates D-Lac as the electrophilic rather than the nucleophilic partner for condensation with D-Ala to make a regioisomeric D-Lac-D-Ala, an amide rather than an ester product
L282R
-
11fold decrease in kcat for D-alanine, 18fold increase in Km for D-alanine, 23fold decrease in Km for D-serine, 9fold drop in kcat for D-serine
S150A
mutant has gained depsipeptide (D-Ala-D-Lac, D-Ala-D-hydroxybutyrate) ligase activity with dipeptide/depsipeptide partition ratios that mimic the pH behavior of VanA (D-alanine(R)-lactate ligase)
Y216F
mutant has gained depsipeptide (D-Ala-D-Lac, D-Ala-D-hydroxybutyrate) ligase activity with dipeptide/depsipeptide partition ratios that mimic the pH behavior of VanA (D-alanine(R)-lactate ligase)
I16V
site-directed mutagenesis of an active site mutant, mutant kinetics compared to the wild-type structure
L241F
site-directed mutagenesis of an active site mutant, mutant kinetics compared to the wild-type structure
L241Y
site-directed mutagenesis of an active site mutant, mutant kinetics compared to the wild-type structure
L308T
site-directed mutagenesis of an active site mutant, mutant kinetics compared to the wild-type structure
Y311S
site-directed mutagenesis of an active site mutant, mutant kinetics compared to the wild-type structure
F261Y
-
mutation of the Omega loop, inactive mutant
S137A/Y207F
-
higher D-alanyl-D-lactate and lower D-alanyl-D-alanine synthase activity than mutant Y207F. Broad substrate specificity toward D-amino acids, accepts D-lactate and D,L-isoleucine as substrate
S137F/Y207F
-
about 20% of wild-type activity. Accepts D-lactate as substrate
S137G/Y207F
-
about 200% of wild-type activity. Accepts D-lactate as substrate
S137T/Y207F
-
about 40% of wild-type activity. Does not accept D-lactate as substrate
Y201F
-
increase in activity compared to wild-type, mutant is not able to synthesize D-alanyl-D-lactate
Y207F
-
mutant is able to synthesize D-alanyl-D-lactate
S137A/Y207F
-
higher D-alanyl-D-lactate and lower D-alanyl-D-alanine synthase activity than mutant Y207F. Broad substrate specificity toward D-amino acids, accepts D-lactate and D,L-isoleucine as substrate
-
S137F/Y207F
-
about 20% of wild-type activity. Accepts D-lactate as substrate
-
S137T/Y207F
-
about 40% of wild-type activity. Does not accept D-lactate as substrate
-
Y201F
-
increase in activity compared to wild-type, mutant is not able to synthesize D-alanyl-D-lactate
-
Y207F
-
mutant is able to synthesize D-alanyl-D-lactate
-
S293A
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293C
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293D
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with high production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293E
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with high production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293F
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293G
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293H
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293I
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with high production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293K
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293L
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293M
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with high production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293N
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293P
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme, it catalyzes the synthesis of both D-AlaNH2 and D-Ala-dDAla
S293Q
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293R
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme, it catalyzes the synthesis of both D-AlaNH2 and D-Ala-D-Ala
S293S
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293T
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293V
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with high production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293W
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293Y
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
S293A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
-
S293C
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
-
S293E
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme with high production of D-AlaNH2 from D-Ala and NH3 in contrast to the wild-type enzyme
-
S293P
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type enzyme, it catalyzes the synthesis of both D-AlaNH2 and D-Ala-dDAla
-
additional information
-
9 clinical isolates that show high resistance to vancomycin have mutations in the Ddl gene, lack of growth of these mutants in the absence of vancomycin is most probably due to a complete loss of Ddl activity
additional information
-
insertion in the middle of the ddl gene is responsible for inactivation of D-alanine-D-alanine ligase in strain BM4416
additional information
-
insertion in the middle of the ddl gene is responsible for inactivation of D-alanine-D-alanine ligase in strain BM4416
-
additional information
-
mutant enzymes at K144, K215, and E270 in the ATP binding site, at E15, S150, H63, and R255 in the first D-Ala subsite, and at Y216, S281, L282, and D257 in the second D-Ala subsite. Mutant enzymes E270Q, K215A, R255A, and D257N retain very low or no detectable activity. Mutants enzyme Y216F shows substantial retention of activity
additional information
homology structure modeling analyses of wild-type enzyme and mutants S293D and S293E
additional information
-
homology structure modeling analyses of wild-type enzyme and mutants S293D and S293E
additional information
-
homology structure modeling analyses of wild-type enzyme and mutants S293D and S293E
-
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Oppenheim, B.; Patchornik, A.
Formation of D-alanyl-D-alanine and D-alanine from UDPMurNAc-L-Ala-D-isoGlu-L-Lys-D-Ala-D-Ala by extracts of Staphylococcus aureus and Streptococcus faecalis
FEBS Lett.
48
172-175
1974
Enterococcus faecalis, Staphylococcus aureus
brenda
Linnett, P.E.; Tipper, D.J.
Cell wall polymers of Bacillus sphaericus: activities of enzymes involved in peptidoglycan precursor synthesis during sporulation
J. Bacteriol.
120
342-354
1974
Lysinibacillus sphaericus, Lysinibacillus sphaericus 9602
brenda
Duncan, K.; Walsh, C.T.
ATP-dependent inactivation and slow binding inhibition of Salmonella typhimurium D-alanine:D-alanine ligase (ADP) by (aminoalkyl)phosphinate and aminophosphonate analogues of D-alanine
Biochemistry
27
3709-3714
1988
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Daub, E.; Zawadzke, L.E.; Botstein, D.; Walsh, C.T.
Isolation, cloning, and sequencing of the Salmonella typhimurium ddlA gene with purification and characterization of its product, D-alanine:D-alanine ligase (ADP forming)
Biochemistry
27
3701-3708
1988
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Vicario, P.P.; Green, B.G.; Katzen, H.M.
A single assay for simultaneously testing effectors of alanine racemase and/or D-alanine:D-alanine ligase
J. Antibiot.
15
209-216
1987
Enterococcus faecalis, Enterococcus faecalis R / ATCC 8043
brenda
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
Buxton, R.S.; Ward, J.B.
Heat-sensitive lysis mutants of Bacillus subtilis 168 blocked at three different stages of peptidoglycan synthesis
J. Gen. Microbiol.
120
283-293
1980
Bacillus subtilis, Bacillus subtilis 168
brenda
Lacoste, A.M.; Poulsen, M.; Cassaigne, A.; Neuzil, E.
Inhibition of D-alanyl-D-alanine ligase in different bacterial species by amino phosphonic acids
Curr. Microbiol.
2
113-117
1979
Staphylococcus aureus, Pseudomonas aeruginosa
-
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
Pandhi, P.N.; Panos, C.
Biosynthesis of D-alanyl-D-alanine from L-alanine by extracts of a stabilized L-form fro Streptococcus pyogenes
J. Gen. Microbiol.
71
487-494
1972
Streptococcus pyogenes
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
McDermott, A.E.; Creuzet, F.; Griffin, R.G.
Rotational resonance determination of the structure of an enzyme-inhibitor complex: phosphorylation of an (aminoalkyl)phosphinate inhibitor of D-alanyl-D-alanine ligase by ATP
Biochemistry
29
5767-5775
1990
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Knox, J.R.; Liu, H.; Walsh, C.T.; Zawadzke, L.E.
D-Alanine-D-alanine ligase (ADP) from Salmonella typhimurium. Overproduction, purification, crystallization and preliminary X-ray analysis
J. Mol. Biol.
205
461-463
1989
Salmonella enterica subsp. enterica serovar Typhimurium
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
Chakravarty, P.K.; Greenlee, W.J.; Parsons, W.H.; Patchett, A.A.; Combs, P.; Roth, A.; Busch, R.D.; Mellin, T.N.
(3-Amino-2-oxoalkyl)phosphonic acids and their analogues as novel inhibitors of D-alanine:D-alanine ligase
J. Med. Chem.
32
1886-1890
1989
Enterococcus faecalis
brenda
Greenlee, W.J.; Springer, J.P.; Patchett, A.A.
Synthesis of an analogue of tabtoxinine as a potential inhibitor of the D-alanine:D-alanine ligase (ADP forming)
J. Med. Chem.
32
165-170
1989
Enterococcus faecalis
brenda
Lacoste, A.M.; Chollet-Gravey, A.M.; Quang, L.V.; Quang, Y.V.; le Goffic, F.
Time-dependent inhibition of Streptococcus faecalis D-alanine:D-alanine ligase by alpha-aminophosphonamidic acids
Eur. J. Med. Chem.
26
255-260
1991
Enterococcus faecalis
-
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
Park, I.S.; Walsh, C.T.
D-Alanyl-D-lactate and D-alanyl-D-alanine synthesis by D-alanyl-D-alanine ligase from vancomycin-resistant Leuconostoc mesenteroides. Effects of a phenylalanine 261 to tyrosine mutation
J. Biol. Chem.
272
9210-9214
1997
Leuconostoc mesenteroides (P71454), Leuconostoc mesenteroides
brenda
Meziane-Cherif, D.; Badet-Denisot, M.A.; Evers, S.; Courvalin, P.; Badet, B.
Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583
FEBS Lett.
354
140-142
1994
Bacteria, Enterococcus faecalis
brenda
Duncan, K.; Faraci, W.S.; Matteson, D.S.; Walsh, C.T.
(1-Aminoethyl)boronic acid: a novel inhibitor for Bacillus stearothermophilus alanine racemase and Salmonella typhimurium D-alanine:D-alanine ligase (ADP-forming)
Biochemistry
28
3541-3549
1989
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Perichon, B.; Casadewall, B.; Reynolds, P.; Courvalin, P.
Glycopeptide-resistant Enterococcus faecium BM4416 is a VanD-type strain with an impaired D-alanine:D-alanine ligase
Antimicrob. Agents Chemother.
44
1346-1348
2000
Enterococcus faecium, Enterococcus faecium BM4416
brenda
Feng, Z.; Barletta, R.G.
Roles of Mycobacterium smegmatis D-alanine:D-alanine ligase and D-alanine racemase in the mechanisms of action of and resistance to the peptidoglycan inhibitor D-cycloserine
Antimicrob. Agents Chemother.
47
283-291
2003
Mycobacterium tuberculosis, Mycolicibacterium smegmatis (Q9ZGN0), Mycolicibacterium smegmatis
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
Prevost, M.; Van Belle, D.; Tulkens, P.M.; Courvalin, P.; Van Bambeke, F.
Modeling of Enterococcus faecalis D-alanine:D-alanine ligase: structure-based study of the active site in the wild-type enzyme and in glycopeptide-dependent mutants
J. Mol. Microbiol. Biotechnol.
2
321-330
2000
Enterococcus faecalis
brenda
Gholizadeh, Y.; Prevost, M.; Van Bambeke, F.; Casadewall, B.; Tulkens, P.M.; Courvalin, P.
Sequencing of the ddl gene and modeling of the mutated D-alanine:D-alanine ligase in glycopeptide-dependent strains of Enterococcus faecium
Protein Sci.
10
836-844
2001
Enterococcus faecium
brenda
Noda, M.; Kawahara, Y.; Ichikawa, A.; Matoba, Y.; Matsuo, H.; Lee, D.G.; Kumagai, T.; Sugiyama, M.
Self-protection mechanism in D-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase and D-alanyl-D-alanine ligase, which are target enzymes of D-cycloserine
J. Biol. Chem.
279
46143-46152
2004
Streptomyces lavendulae, Streptomyces lavendulae ATCC 25233
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
McCoy, A.J.; Maurelli, A.T.
Characterization of Chlamydia MurC-Ddl, a fusion protein exhibiting D-alanyl-D-alanine ligase activity involved in peptidoglycan synthesis and D-cycloserine sensitivity
Mol. Microbiol.
57
41-52
2005
Chlamydia trachomatis
brenda
Lu, Y.; Sheng, Y.; Li, L.; Tang, D.; Liu, X.; Zhao, X.; Liang, Y.; Su, X.
Crystallization and preliminary crystallographic analysis of D-alanine-D-alanine ligase from Streptococcus mutans
Acta Crystallogr. Sect. F
63
807-808
2007
Streptococcus mutans
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
Sato, M.; Kirimura, K.; Kino, K.
Substrate specificity of thermostable D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589
Biosci. Biotechnol. Biochem.
70
2790-2792
2006
Thermotoga maritima, Thermotoga maritima (P46805)
brenda
Sato, M.; Masuda, Y.; Kirimura, K.; Kino, K.
Thermostable ATP regeneration system using polyphosphate kinase from Thermosynechococcus elongatus BP-1 for D-amino acid dipeptide synthesis
J. Biosci. Bioeng.
103
179-184
2007
Thermosynechococcus vestitus
brenda
Liu, S.; Chang, J.S.; Herberg, J.T.; Horng, M.M.; Tomich, P.K.; Lin, A.H.; Marotti, K.R.
Allosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by crystallographic studies
Proc. Natl. Acad. Sci. USA
103
15178-15183
2006
Staphylococcus aureus (Q5HEB7), Staphylococcus aureus
brenda
Lee, J.H.; Na, Y.; Song, H.; Kim, D.; Park, B.; Rho, S.; Im, Y.J.; Kim, M.; Kang, G.B.; Lee, D.; Eom, S.H.
Crystal structure of the apo form of D-alanine: D-alanine ligase from Thermus caldophilus: A basis for the substrate-induced conformation changes
Proteins Struct. Funct. Bioinform.
64
1078-1082
2006
Thermus caldophilus
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
Wu, D.; Zhang, L.; Kong, Y.; Du, J.; Chen, S.; Chen, J.; Ding, J.; Jiang, H.; Shen, X.
Enzymatic characterization and crystal structure analysis of the D-alanine-D-alanine ligase from Helicobacter pylori
Proteins
72
1148-1160
2008
Helicobacter pylori (Q2N4T5), Helicobacter pylori
brenda
Kitamura, Y.; Ebihara, A.; Agari, Y.; Shinkai, A.; Hirotsu, K.; Kuramitsu, S.
Structure of D-alanine-D-alanine ligase from Thermus thermophilus HB8: cumulative conformational change and enzyme-ligand interactions
Acta Crystallogr. Sect. D
65
1098-1106
2009
Thermus thermophilus HB8 (Q5SHZ3), Thermus thermophilus HB8
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
Escherichia coli, Enterococcus faecium
brenda
Jofre, E.; Fischer, S.; Principe, A.; Castro, M.; Ferrari, W.; Lagares, A.; Mori, G.
Mutation in a D-alanine-D-alanine ligase of Azospirillum brasilense Cd results in an overproduction of exopolysaccharides and a decreased tolerance to saline stress
FEMS Microbiol. Lett.
290
236-246
2009
Azospirillum brasilense
brenda
Neuhaus, F.C.
Role of Arg301 in substrate orientation and catalysis in subsite 2 of D-alanine:D-alanine (D-lactate) ligase from Leuconostoc mesenteroides: A molecular docking study
J. Mol. Graph. Model.
28
728-734
2010
Leuconostoc mesenteroides
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
Bruning, J.B.; Murillo, A.C.; Chacon, O.; Barletta, R.G.; Sacchettini, J.C.
Structure of the Mycobacterium tuberculosis D-alanine:D-alanine ligase, a target of the antituberculosis drug D-cycloserine
Antimicrob. Agents Chemother.
55
291-301
2011
Mycobacterium tuberculosis (P9WP31), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WP31)
brenda
Nakagawa, T.; Satake, R.; Sato, M.; Kino, K.
Structure-based modification of D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589 for depsipeptide synthesis
Biosci. Biotechnol. Biochem.
75
700-704
2011
Thermotoga maritima, Thermotoga maritima ATCC 43589
brenda
Doan, T.T.; Kim, J.K.; Ngo, H.P.; Tran, H.T.; Cha, S.S.; Min Chung, K.; Huynh, K.H.; Ahn, Y.J.; Kang, L.W.
Crystal structures of D-alanine-D-alanine ligase from Xanthomonas oryzae pv. oryzae alone and in complex with nucleotides
Arch. Biochem. Biophys.
545C
92-99
2014
Xanthomonas oryzae (Q5H614)
brenda
Prosser, G.A.; de Carvalho, L.P.
Reinterpreting the mechanism of inhibition of Mycobacterium tuberculosis D-alanine:D-alanine ligase by D-cycloserine
Biochemistry
52
7145-7149
2013
Mycobacterium tuberculosis
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
Neuhaus, F.C.
Role of the omega loop in specificity determination in subsite 2 of the D-alanine:D-alanine (D-lactate) ligase from Leuconostoc mesenteroides: a molecular docking study
J. Mol. Graph. Model.
30
31-37
2011
Leuconostoc mesenteroides
brenda
Halouska, S.; Fenton, R.; Zinniel, D.; Marshall, D.; Barletta, R.; Powers, R.
Metabolomics analysis identifies D-alanine-D-alanine ligase as the primary lethal target of D-cycloserine in mycobacteria
J. Proteome Res.
13
1065-1076
2014
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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
Tran, H.T.; Hong, M.K.; Ngo, H.P.; Huynh, K.H.; Ahn, Y.J.; Wang, Z.; Kang, L.W.
Structure of D-alanine-D-alanine ligase from Yersinia pestis nucleotide phosphate recognition by the serine loop
Acta Crystallogr. Sect. D
72
12-21
2016
Yersinia pestis (Q8ZIE7), Yersinia pestis
brenda
Takenaka, T.; Ito, T.; Miyahara, I.; Hemmi, H.; Yoshimura, T.
A new member of MocR/GabR-type PLP-binding regulator of D-alanyl-D-alanine ligase in Brevibacillus brevis
FEBS J.
282
4201-4217
2015
Brevibacillus brevis (C0ZB62), Brevibacillus brevis 47 / JCM 6285 / NBRC 100599 (C0ZB62)
brenda
Asker, M.; Shady, H.; Soliman, M.; Gadalla, M.; Abd el-Nasser, S.
Cloning and expression of a D-alanine-D-alanine ligase gene from Bacillus megaterium in Escherichia coli
Int. J. Pharm. Sci. Rev. Res.
25
183-187
2014
Priestia megaterium (A0A1Q8TTZ0), Priestia megaterium (D5D9X4), Priestia megaterium (D5DWS5), Priestia megaterium DSM 319 (D5D9X4), Priestia megaterium WSH-002 (A0A1Q8TTZ0), Priestia megaterium ATCC 12872 / QM B1551 (D5DWS5)
-
brenda
Miki, Y.; Okazaki, S.; Asano, Y.
Engineering an ATP-dependent D-Ala D-Ala ligase for synthesizing amino acid amides from amino acids
J. Ind. Microbiol. Biotechnol.
44
667-675
2017
Thermus thermophilus (Q5SHZ3), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SHZ3)
brenda
Huynh, K.H.; Hong, M.K.; Lee, C.; Tran, H.T.; Lee, S.H.; Ahn, Y.J.; Cha, S.S.; Kang, L.W.
The crystal structure of the D-alanine-D-alanine ligase from Acinetobacter baumannii suggests a flexible conformational change in the central domain before nucleotide binding
J. Microbiol.
53
776-782
2015
Acinetobacter baumannii
brenda
Azam, S.; Abbasi, S.; Akhtar, A.; Mirza, M.
Comparative modeling and molecular docking studies of D-alanine D-alanine ligase a target of antibacterial drugs
Med. Chem. Res.
23
4108-4137
2014
Streptococcus sanguinis (A3CLS3), Streptococcus sanguinis SK36 (A3CLS3)
-
brenda
Yang, S.; Xu, Y.; Wang, Y.; Ren, F.; Li, S.; Ding, W.; Ma, Y.; Zhang, W.
The biological properties and potential interacting proteins of D-alanyl-D-alanine ligase a from Mycobacterium tuberculosis
Molecules
23
324-338
2018
Mycobacterium tuberculosis (P9WP31), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WP31)
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