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Literature summary for 2.1.3.2 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.
    View publication on PubMedView publication on EuropePMC

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
noncovalent hexamer of dihydroorotase and ATCase, to 2.3 A resolution. The structure has citrate, bound to the active sites of both enzymes.Six DHO and six ATC chains form a hollow dodecamer, in which the 12 active sites face an internal reaction chamber that is approximately 60 A in diameter and connected to the cytosol by narrow tunnels. The entrances and the interior of the chamber are both electropositive, which suggests that the architecture of this nanoreactor modifies the kinetics of the bisynthase, not only by steric channeling but also by preferential escape of the product, dihydroorotase Aquifex aeolicus

Protein Variants

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

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus O66726
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Aquifex aeolicus O66726 in noncovalent association with dihydroorotase, possible model for the mammalian polypeptide chain CPSase/ATCase/DHOase during pyrimidine biosynthesis
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Subunits

Subunits Comment Organism
hexamer noncovalent association with dihydroorotase Aquifex aeolicus

Synonyms

Synonyms Comment Organism
aspartate transcarbamoylase
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Aquifex aeolicus