Literature summary for 4.2.99.21 extracted from

Kerbarh, O.; Chirgadze, D.Y.; Blundell, T.L.; Abell, C.
Crystal structures of Yersinia enterocolitica salicylate synthase and its complex with the reaction products salicylate and pyruvate (2006), J. Mol. Biol., 357, 524-534.

Search for more literature for 4.2.99.21

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of Irp9 and of its complex with the reaction products salicylate and pyruvate at 1.85 A and 2.1 A resolution, respectively. Irp9 has a complex alpha/beta fold. The crystal structure of Irp9 contains one molecule each of phosphate and acetate derived from the crystallization buffer. The enzyme is still catalytically active in the crystal. Both structures contain Mg2+ in the active site. There is no evidence of an allosteric tryptophan binding site	Yersinia enterocolitica

Crystallization (Comment)

Organism

crystal structure of Irp9 and of its complex with the reaction products salicylate and pyruvate at 1.85 A and 2.1 A resolution, respectively. Irp9 has a complex alpha/beta fold. The crystal structure of Irp9 contains one molecule each of phosphate and acetate derived from the crystallization buffer. The enzyme is still catalytically active in the crystal. Both structures contain Mg2+ in the active site. There is no evidence of an allosteric tryptophan binding site

Yersinia enterocolitica

Protein Variants

Protein Variants	Comment	Organism
E240A	complete loss of activity	Yersinia enterocolitica
H321M	complete loss of activity	Yersinia enterocolitica
Y372F	about 20% residual activity	Yersinia enterocolitica
Y372W	strong decrease in activity	Yersinia enterocolitica

Organism

Organism	UniProt	Comment	Textmining
Yersinia enterocolitica	Q9X9I8	-	-

Synonyms

Synonyms	Comment	Organism
Irp9	-	Yersinia enterocolitica

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Release 2023.1 (January 2023)