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Literature summary for 6.3.2.4 extracted from

  • 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 (2011), Antimicrob. Agents Chemother., 55, 291-301.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
t 2.1 A resoluion. Ddl is a dimer and consists of three discrete domains. The ligand binding cavity is at the intersection of all three domains and conjoined by several loop regions. The nucleotide and D-alanine binding pockets are flexible, requiring significant structural rearrangement of the bordering regions for entry and binding of both ATP and D-Ala molecules. D-cycloserine interacts with Ddl in a manner similar to that observed for D-Ala. Each ligand binds to two binding sites that have significant differences in affinity, with the first binding site exhibiting high affinity Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
D-cycloserine preferential and weak inhibition at the second, lower-affinity binding site. D-cycloserine binding is tighter at higher ATP concentrations Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WP31
-
-
Mycobacterium tuberculosis H37Rv P9WP31
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-Ala + D-Ala
-
Mycobacterium tuberculosis ADP + phosphate + D-Ala-D-Ala
-
?
ATP + D-Ala + D-Ala
-
Mycobacterium tuberculosis H37Rv ADP + phosphate + D-Ala-D-Ala
-
?

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.37
-
pH not specified in the publication, temperature not specified in the publication Mycobacterium tuberculosis D-cycloserine