Literature summary for 1.3.98.1 extracted from

Cordeiro, A.T.; Feliciano, P.R.; Pinheiro, M.P.; Nonato, M.C.
Crystal structure of dihydroorotate dehydrogenase from Leishmania major (2012), Biochimie, 94, 1739-1748.

Search for more literature for 1.3.98.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Leishmania major

Crystallization (Commentary)

Crystallization (Comment)	Organism
apo-enzyme and in complex with orotate and with fumarate, to 2.0 A, 2.5 A and 1.9 A resolution, respectively. Both orotate and fumarate bind to the same active site and exploit similar interactions, consistent with a ping-pong mechanism. Rearrangements in the conformation of the catalytic loop have direct influence on the dimeric interface	Leishmania major

Organism

Organism	UniProt	Comment	Textmining
Leishmania major	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-dihydroorotate + fumarate	-	Leishmania major	orotate + succinate	-	?

Cofactor

Cofactor	Comment	Organism	Structure
FMN	two molecules per dimer in the asymmetric crystal unit	Leishmania major

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Release 2023.1 (January 2023)