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Literature summary 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 .
    View publication on PubMed

Activating Compound

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

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.5.2.3 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
3.5.2.3 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
3.5.2.3 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

EC Number Metals/Ions Comment Organism Structure
3.5.2.3 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)

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

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.3 Aquifex aeolicus O66990
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.5.2.3 DHOase
-
 Aquifex aeolicus

General Information

EC Number General Information Comment Organism
3.5.2.3 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
3.5.2.3 metabolism dihydroorotase (DHOase) catalyses the third reaction of the de novo pyrimidine biosynthetic pathway, the reversible condensation of carbamylaspartate into dihydroorotate Aquifex aeolicus
3.5.2.3 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