Literature summary for 4.1.1.23 extracted from

Takashima, Y.; Mizohata, E.; Krungkrai, S.R.; Fukunishi, Y.; Kinoshita, T.; Sakata, T.; Matsumura, H.; Krungkrai, J.; Horii, T.; Inoue, T.
The in silico screening and X-ray structure analysis of the inhibitor complex of Plasmodium falciparum orotidine 5-monophosphate decarboxylase (2012), J. Biochem., 152, 133-138.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with inhibitor 4-(2-hydroxy-4-methoxyphenyl)-4-oxobutanoic acid, to 2.1 A resolution. The inhibitor molecule occupies a part of the active site that overlaps with the phosphate-binding region in the OMP- or UMP-bound complexes. The carboxyl group of the inhibitor causes a dramatic movement of the L1 and L2 loops that play a role in the recognition of the substrate and product molecules	Plasmodium falciparum

Inhibitors

Inhibitors	Comment	Organism	Structure
4-(2-hydroxy-4-methoxyphenyl)-4-oxobutanoic acid	the inhibitor molecule occupies a part of the active site that overlaps with the phosphate-binding region in the OMP- or UMP-bound complexes. The carboxyl group of the inhibitor causes a dramatic movement of the L1 and L2 loops that play a role in the recognition of the substrate and product molecules	Plasmodium falciparum

Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum	Q8T6J6	-	-

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Release 2023.1 (January 2023)