Literature summary for 1.3.98.1 extracted from

Inaoka, D.; Sakamoto, K.; Shimizu, H.; Shiba, T.; Kurisu, G.; Nara, T.; Aoki, T.; Kita, K.; Harada, S.
Structures of Trypanosoma cruzi dihydroorotate dehydrogenase complexed with substrates and products: Atomic resolution insights into mechanisms of dihydroorotate oxidation and fumarate reduction (2008), Biochemistry, 47, 10881-10891.

Crystallization (Commentary)

Crystallization (Comment)	Organism
in ligand-free form and in complexes with inhibitor oxonate, physiological substrates and products of the first and second half-reactions. Ligands bind to the same active site of enzyme, consistent with one-site ping-pong Bi-Bi mechanism. The binding of ligands does not cause any significant structural changes, and both reduced and oxidized FMN cofactors are in planar conformation. Resiude C130 is well located for abstracting a proton from dihydroorotate C5 and transferring it to outside water molecules. The bound fumarate is in a twisted conformation, which induces partial charge separation. The thermodynamically favorable reduction of fumarate with reduced FMN seems to proceed in the way that its C2 accepts a proton from C130 and C3 a hydride or a hydride equivalent from reduced FMN N5	Trypanosoma cruzi

Crystallization (Comment)

Organism

in ligand-free form and in complexes with inhibitor oxonate, physiological substrates and products of the first and second half-reactions. Ligands bind to the same active site of enzyme, consistent with one-site ping-pong Bi-Bi mechanism. The binding of ligands does not cause any significant structural changes, and both reduced and oxidized FMN cofactors are in planar conformation. Resiude C130 is well located for abstracting a proton from dihydroorotate C5 and transferring it to outside water molecules. The bound fumarate is in a twisted conformation, which induces partial charge separation. The thermodynamically favorable reduction of fumarate with reduced FMN seems to proceed in the way that its C2 accepts a proton from C130 and C3 a hydride or a hydride equivalent from reduced FMN N5

Trypanosoma cruzi

Inhibitors

Inhibitors	Comment	Organism	Structure
oxonate	crystallization data	Trypanosoma cruzi

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma cruzi	Q4D3W2	-	-

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Release 2023.1 (January 2023)