Literature summary for 3.5.2.3 extracted from

Ahuja, A.; Purcarea, C.; Ebert, R.; Sadecki, S.; Guy, H.I.; Evans, D.R.
Aquifex aeolicus dihydroorotase: association with aspartate transcarbamoylase switches on catalytic activity (2004), J. Biol. Chem., 279, 53136-53144.

Search for more literature for 3.5.2.3

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Aquifex aeolicus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
3.03	-	dihydroorotate	-	Aquifex aeolicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	one mol per mol of protein	Aquifex aeolicus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
49000	-	1 * 49000, SDS-PAGE	Aquifex aeolicus
53000	-	gel filtration	Aquifex aeolicus
386000	-	gel filtration, enzyme-aspartate transcarbamoylase complex	Aquifex aeolicus

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
His-tagged recombinant protein	Aquifex aeolicus

Reaction

Reaction	Comment	Organism	Reaction ID
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate	complex formation of enzyme with aspartate transcarbamoylase drives reaction in the biosynthetic direction	Aquifex aeolicus	a

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
monomer	1 * 49000, SDS-PAGE	Aquifex aeolicus
More	recombinant protein lacks catalytic activity, activity is acquired by forming a complex with aspartate transcarbamoylase, complex may be a heterohexamer or dodecamer	Aquifex aeolicus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
99	-	enzyme complex with aspartate transcarbamoylase, both activities are stable	Aquifex aeolicus

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Release 2023.1 (January 2023)