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Literature summary for 6.3.2.9 extracted from

  • Kristan, K.; Kotnik, M.; Oblak, M.; Urleb, U.
    New high-throughput fluorimetric assay for discovering inhibitors of UDP-N-acetylmuramyl-L-alanine: D-glutamate (MurD) ligase (2009), J. Biomol. Screen., 14, 412-418.
    View publication on PubMed
Search for more literature for 6.3.2.9

Application

Application Comment Organism
analysis assay for monitoring enzyme activity based on the accumulation of adenosine 5'-diphosphate, a product of the reaction catalyzed by MurD ligase, by conversion to a fluorescent signal via a coupled enzyme system, with counterscreen assay to eliminate false positive results Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
3-([[(5-amino-1,3,4-thiadiazol-2-yl)sulfanyl]acetyl]amino)-4-methylbenzoic acid
-
 Escherichia coli
beta,gamma-methyleneadenosine 5'-triphosphate nonhydrolyzable ATP analogue Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0073
-
 UDP-N-acetylmuramate-L-alanine 37°C Escherichia coli
0.067
-
 D-glutamate 37°C Escherichia coli
0.106
-
 ATP 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramate-L-alanine + D-glutamate
-
 Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
 ?

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.105
-
 37°C Escherichia coli 3-([[(5-amino-1,3,4-thiadiazol-2-yl)sulfanyl]acetyl]amino)-4-methylbenzoic acid
0.177
-
 37°C Escherichia coli beta,gamma-methyleneadenosine 5'-triphosphate