Binding of l-kynurenine to X. campestris tryptophan 2,3-dioxygenase.
J Inorg Biochem
; 225: 111604, 2021 12.
Article
en En
| MEDLINE
| ID: mdl-34571402
ABSTRACT
The kynurenine pathway is the major route of tryptophan metabolism. The first step of this pathway is catalysed by one of two heme-dependent dioxygenase enzymes - tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) - leading initially to the formation of N-formylkynurenine (NFK). In this paper, we present a crystal structure of a bacterial TDO from X. campestris in complex with l-kynurenine, the hydrolysed product of NFK. l-kynurenine is bound at the active site in a similar location to the substrate (l-Trp). Hydrogen bonding interactions with Arg117 and the heme 7-propionate anchor the l-kynurenine molecule into the pocket. A mechanism for the hydrolysis of NFK in the active site is presented.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Triptófano Oxigenasa
/
Quinurenina
Idioma:
En
Revista:
J Inorg Biochem
Año:
2021
Tipo del documento:
Article
País de afiliación:
Reino Unido