Literature summary for 2.5.1.54 extracted from

Pratap, S.; Dev, A.; Kumar, V.; Yadav, R.; Narwal, M.; Tomar, S.; Kumar, P.
Structure of chorismate mutase-like domain of DAHPS from Bacillus subtilis complexed with novel inhibitor reveals conformational plasticity of active site (2017), Sci. Rep., 7, 6364 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of N-terminal domain AroQ in complex with citrate and chlorogenic acid at 1.9 A and 1.8 A resolution, respectively. Helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. Chlorogenic acid binds with a higher affinity than chorismate	Bacillus subtilis

Crystallization (Comment)

Organism

structure of N-terminal domain AroQ in complex with citrate and chlorogenic acid at 1.9 A and 1.8 A resolution, respectively. Helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. Chlorogenic acid binds with a higher affinity than chorismate

Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P39912	bifunctional enzyme, catalyzes reactions of EC 2.5.1.54 and EC 5.4.99.5	-
Bacillus subtilis 168	P39912	bifunctional enzyme, catalyzes reactions of EC 2.5.1.54 and EC 5.4.99.5	-

Synonyms

Synonyms	Comment	Organism
AroA	-	Bacillus subtilis

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Release 2023.1 (January 2023)