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Pregled bibliografske jedinice broj: 395302

Crystal structure of bovine 3-hydroxyanthranilate 3, 4-dioxygenase

Đilović, Ivica; Gliubich, Francesca; Malpeli, Giorgio; Zanotti, Giuseppe; Matković-Čalogović, Dubravka
Crystal structure of bovine 3-hydroxyanthranilate 3, 4-dioxygenase // Biopolymers, 91 (2009), 12 Special Issue; 1189-1195 doi:10.1002/bip.21167 (međunarodna recenzija, članak, znanstveni)

Crystal structure of bovine 3-hydroxyanthranilate 3, 4-dioxygenase

Đilović, Ivica ; Gliubich, Francesca ; Malpeli, Giorgio ; Zanotti, Giuseppe ; Matković-Čalogović, Dubravka

Biopolymers (0006-3525) 91 (2009), 12 Special Issue; 1189-1195

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Quinolinic acid; Dioxygenase; 3-hydroxyanthranilate; 3HAO; Cupin fold

3-Hydroxyanthranilate 3, 4-dioxygenase, the enzyme that catalyzes the conversion of 3- hydroxyanthranilate to quinolinic acid, has been extracted and purified from bovine kidney, crystallized and its structure determined at 2.5 Å ; ; ; resolution. The enzyme, which crystallizes in the triclinic P1 space group, is a monomer, characterized by the so-called cupin fold. The monomer of the bovine enzyme mimics the dimer present in lower species, such as bacteria and yeast, since it is composed of two domains: one of them is equivalent to one monomer, whilst the second domain corresponds to only a portion of it. The active site consists of an iron ion coordinated by two histidine residues, one glutamate and an external ligand, which has been interpreted as a solvent molecule. It is contained in the N-terminal domain, whilst the function of the C-terminal domain is possibly structural. The catalytic mechanism very likely has been conserved through all species, since the positions of all residues considered relevant for the reaction are present from bacteria to humans.

Izvorni jezik

Znanstvena područja


Projekt / tema
119-1193079-1084 - Strukturno istraživanje bioloških makromolekula metodom rentgenske difrakcije (Dubravka Matković-Čalogović, )

Prirodoslovno-matematički fakultet, Zagreb

Časopis indeksira:

  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus