Literature summary for 3.5.2.3 extracted from

Prange, T.; Girard, E.; Fourme, R.; Dhaussy, A.C.; Edwards, B.; Vaishnav, A.; Patel, C.; Guy-Evans, H.; Herve, G.; Evans, D.R.
Pressure-induced activation of latent dihydroorotase from Aquifex aeolicus as revealed by high pressure protein crystallography (2019), FEBS J., 286, 1204-1213 .

Search for more literature for 3.5.2.3

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	pressure-induced activation of dihydroorotase, overview	Aquifex aeolicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure analysis of the zinc environment at ambient pressure, at 600 bar, and at 1200 bar	Aquifex aeolicus

Protein Variants

Protein Variants	Comment	Organism
C181G	site-directed mutagenesis, the mutant does not restore the activity of DHOase that has been isolated from aspartate transcarbamylase (ATCase, EC 2.1.3.2)	Aquifex aeolicus
D179V	site-directed mutagenesis, the mutant partially restores the activity of DHOase that has been isolated from aspartate transcarbamylase (ATCase, EC 2.1.3.2)	Aquifex aeolicus
D183G	site-directed mutagenesis, the mutant partially restores the activity of DHOase that has been isolated from aspartate transcarbamylase (ATCase, EC 2.1.3.2)	Aquifex aeolicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	DHOase is a zinc-dependent metalloenzyme, analysis of the catalytic zinc environment, structure, overview. Cys181 is observed bonded to the zinc atom of the catalytic site, with residues 181-187 visible and tethered by the interaction of loop A with other regions of the protein. On one end, the 1200 bar zinc coordination is like in the monoclinic-ap form with the Cys181 recruited again by the zinc atom, instead of the water molecule; the Cys-181 sulfur atom rotates and becomes more and more closely connected to the zinc when pressure increases	Aquifex aeolicus

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	O66990	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
DHOase	-	Aquifex aeolicus

General Information

General Information	Comment	Organism
malfunction	the replacement of the zinc ligand Cys181 with glycine does not restore the latent catalytic activity suggesting that it plays a minor role in stabilizing loop A	Aquifex aeolicus
metabolism	dihydroorotase (DHOase) catalyses the third reaction of the de novo pyrimidine biosynthetic pathway, the reversible condensation of carbamylaspartate into dihydroorotate	Aquifex aeolicus
additional information	in the hyperthermophilic bacterium Aquifex aeolicus, aspartate transcarbamylase (ATCase, EC 2.1.3.2) and dihydroorotase (DHOase) are noncovalently associated. Upon dissociation, ATCase keeps its activity entirely while DHOase is totally inactivated. High pressure fully restores the activity of this isolated DHOase. Under high-hydrostatic pressure, at 600 bar, and to a greater extent at 1200 bar, the orthorhombic form of DHOase displays a structure, which includes the Cys-181 bridge of the C2-ap form and some additional residues of the missing loops that become ordered and visible in the electron density	Aquifex aeolicus

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Release 2023.1 (January 2023)