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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
6.3.1.12
669439
Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium
J. Biol. Chem.
281
11586-11594
2006
Enterococcus faecium
16510449
6.3.1.12
669171
Biosynthesis of the peptidoglycan of bacterial cell walls. XXII. Activation of D-aspartic acid for incorporation into peptidoglycan
J. Biol. Chem.
247
5095-5102
1972
Enterococcus faecalis
4262567
6.3.1.12
669171
Biosynthesis of the peptidoglycan of bacterial cell walls. XXII. Activation of D-aspartic acid for incorporation into peptidoglycan
J. Biol. Chem.
247
5095-5102
1972
Lacticaseibacillus casei
4262567
6.3.1.12
727421
Discovery of the first inhibitors of bacterial enzyme D-aspartate ligase from Enterococcus faecium (Aslfm)
Eur. J. Med. Chem.
67
208-220
2013
Enterococcus faecium
23867605
6.3.1.12
727421
Discovery of the first inhibitors of bacterial enzyme D-aspartate ligase from Enterococcus faecium (Aslfm)
Eur. J. Med. Chem.
67
208-220
2013
Enterococcus faecium D359
23867605
6.3.1.12
669172
Further studies of the D-aspartic acid-activating enzyme of Streptococcus faecalis and its attachment to the membrane
J. Biol. Chem.
247
5289-5296
1972
Enterococcus faecalis
4626717
6.3.1.12
670324
Identification of an essential gene responsible for D-Asp incorporation in the Lactococcus lactis peptidoglycan crossbridge
Mol. Microbiol.
62
1713-1724
2006
Lactococcus lactis
17083466
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