Literature summary for 3.5.2.3 extracted from

Zhang, P.; Martin, P.D.; Purcarea, C.; Vaishnav, A.; Brunzelle, J.S.; Fernando, R.; Guy-Evans, H.I.; Evans, D.R.; Edwards, B.F.
Dihydroorotase from the hyperthermophile Aquifex aeolicus is activated by stoichiometric association with aspartate transcarbamoylase and forms a one-pot reactor for pyrimidine biosynthesis (2009), Biochemistry, 48, 766-778.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli strain BL21	Aquifex aeolicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
complex of aspartate transcarbamoylase and dihydroorotase	Aquifex aeolicus

Protein Variants

Protein Variants	Comment	Organism
additional information	in noncovalent association with aspartate transcarbamoylase, possible model for mammalian polypeptide chain CPSase/ATCase/DHOase during pyrimidine biosynthesis	Aquifex aeolicus

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	O66990	in noncovalent association with aspartate transcarbamoylase, possible model for the mammalian polypeptide chain CPSase/ATCase/DHOase during pyrimidine biosynthesis	-

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
hexamer	noncovalent association with aspartate transcarbamoylase	Aquifex aeolicus

Synonyms

Synonyms	Comment	Organism
dihydroorotase	-	Aquifex aeolicus

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Release 2023.1 (January 2023)