Literature summary for 3.5.2.3 extracted from

Lee, M.; Chan, C.W.; Mitchell Guss, J.; Christopherson, R.I.; Maher, M.J.
Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits (2005), J. Mol. Biol., 348, 523-533.

Search for more literature for 3.5.2.3

Crystallization (Commentary)

Crystallization (Comment)	Organism
in the presence of enantiomerically pure L-dihydroorotate, refined at 1.9 Angstrom resolution	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	active sites contain Zn atoms coordinated by His and Asp residues	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	O04904	-	-
Escherichia coli	P05020	-	-
Helicobacter pylori	P56465	-	-
Homo sapiens	P27708	-	-
Mesocricetus auratus	P08955	-	-
Plasmodium falciparum	Q8IKA9	-	-
Saccharomyces cerevisiae	P20051	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-carbamoyl-L-aspartate	-	Escherichia coli	L-dihydroorotate + H2O	-	r

Subunits

Subunits	Comment	Organism
homodimer	crystallization data, asymmetry between active sites, with N-carbamyl-L-aspartate bound to one site and dihydroorotate bound to the other	Escherichia coli

Synonyms

Synonyms	Comment	Organism
DHOase	-	Saccharomyces cerevisiae
DHOase	-	Homo sapiens
DHOase	-	Mesocricetus auratus
DHOase	-	Arabidopsis thaliana
DHOase	-	Escherichia coli
DHOase	-	Plasmodium falciparum
DHOase	-	Helicobacter pylori

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Release 2023.1 (January 2023)