Literature summary for 4.2.99.21 extracted from

Zaitseva, J.; Lu, J.; Olechoski, K.L.; Lamb, A.L.
Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa (2006), J. Biol. Chem., 281, 33441-33449.

Search for more literature for 4.2.99.21

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment)	Organism
apo-structure, to 2.35 A resolution, has one dimer per asymmetric unit with nitrate bound in an open active site. The loop between the first and second helices is disordered, providing a gateway for substrate entry and product exit. The pyruvate-bound structure, to 1.95 A resolution, has two dimers per asymmetric unit. One has two open active sites like the apo structure, and the other has two closed active sites with the loop between the first and second helices ordered for catalysis	Pseudomonas aeruginosa

Crystallization (Comment)

Organism

apo-structure, to 2.35 A resolution, has one dimer per asymmetric unit with nitrate bound in an open active site. The loop between the first and second helices is disordered, providing a gateway for substrate entry and product exit. The pyruvate-bound structure, to 1.95 A resolution, has two dimers per asymmetric unit. One has two open active sites like the apo structure, and the other has two closed active sites with the loop between the first and second helices ordered for catalysis

Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	-	-

Subunits

Subunits	Comment	Organism
More	enzyme is an intertwined dimer of three helices with connecting loops, and amino acids from each monomer participate in each of two active sites, crystallization data	Pseudomonas aeruginosa

Synonyms

Synonyms	Comment	Organism
PchB	-	Pseudomonas aeruginosa

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)