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Coordination of the ferrous ion in the structure of bovine 3-hydroxyanthranilic 3, 4-dioxygenase (CROSBI ID 548396)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa

Đilović, Ivica ; Matković-Čalogović, Dubravka ; Zanotti, Giuseppe Coordination of the ferrous ion in the structure of bovine 3-hydroxyanthranilic 3, 4-dioxygenase // Seventeenth Slovenian Croatian Crystallographic Meeting / Pevec, Andrej ; Leban, Ivan (ur.). Ljubljana: Fakulteta za kemijo in kemijsko tehnologijo Univerze v Ljubljani, 2008. str. 26-26

Podaci o odgovornosti

Đilović, Ivica ; Matković-Čalogović, Dubravka ; Zanotti, Giuseppe

engleski

Coordination of the ferrous ion in the structure of bovine 3-hydroxyanthranilic 3, 4-dioxygenase

Bovine 3-hydroxyanthranilic 3, 4-dioxygenase (3HAO) is a monomeric cytosolic protein made of 286 residues with a molecular mass of 32542 Da. It catalyzes the synthesis of quinolinic acid from hydroxyanthranilic acid in the kynurenine pathway for the tryptophan catabolism. More specific, it catalyzes the final aromatic ring opening, utilizing non-heme Fe2+ to include both oxygen atoms into product. This pathway is of special interest because quinolinate activates the N-methyl-D-aspartate receptors, which are implicated in several neurological disorders (stroke, epilepsy, Huntington's desease etc.) The structure was determined by the molecular replacement method using a model from the protein data bank (PDB ID: 2QNK1). The overall molecular structure is closely related to those found in various homologues2, 3. The secondary structure is mainly consisted of β strands. Residues His47, His91 and Glu53 are coordinated to the ferrous ion forming part of the active site. The octahedral environment is completed by two water molecules. Oxygen binding site is situated between the Fe2+ ion and Arg 43 residue (plays important role in O− O bond cleavage). Other neighbouring residues form a hydrophobic substrate-binding pocket.

X-ray; molecular structure; ferrous ion coordination; 3-hydroxyanthranilic 3; 4-dioxygenase

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Podaci o prilogu

26-26.

2008.

objavljeno

Podaci o matičnoj publikaciji

Seventeenth Slovenian Croatian Crystallographic Meeting

Pevec, Andrej ; Leban, Ivan

Ljubljana: Fakulteta za kemijo in kemijsko tehnologijo Univerze v Ljubljani

Podaci o skupu

Seventeenth Slovenian-Croatian Crystallographic Meeting

predavanje

18.06.2008-22.06.2008

Ptuj, Slovenija

Povezanost rada

Kemija