Literature summary for 1.13.11.47 extracted from

Pietra, F.
Binding pockets and permeation channels for dioxygen through cofactorless 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase in association with its natural substrate, 3-hydroxy-2-methylquinolin-4(1H)-one. A perspective from molecular dynamics simulations (2014), Chem. Biodivers., 11, 861-871 .

Search for more literature for 1.13.11.47

Crystallization (Commentary)

Crystallization (Comment)	Organism
random-acceleration molecular dynamics study. Gates for expulsion of O2 from the protein, which can also be taken as gates for O2 uptake, are found throughout almost the whole external surface of the protein, alongside a variety of binding pockets for O2 . The most exploited gates and binding pockets do not correspond to the single gate and binding pocket proposed from the examination of the static model from X-ray diffraction analysis	Paenarthrobacter nitroguajacolicus

Crystallization (Comment)

Organism

random-acceleration molecular dynamics study. Gates for expulsion of O2 from the protein, which can also be taken as gates for O2 uptake, are found throughout almost the whole external surface of the protein, alongside a variety of binding pockets for O2 . The most exploited gates and binding pockets do not correspond to the single gate and binding pocket proposed from the examination of the static model from X-ray diffraction analysis

Paenarthrobacter nitroguajacolicus

Organism

Organism	UniProt	Comment	Textmining
Paenarthrobacter nitroguajacolicus	O31266	cf. EC 1.13.11.47	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)