An improved method for the expression and purification of porcine dihydropyrimidine dehydrogenase.
Journal
Protein expression and purification
ISSN: 1096-0279
Titre abrégé: Protein Expr Purif
Pays: United States
ID NLM: 9101496
Informations de publication
Date de publication:
07 2020
07 2020
Historique:
received:
25
09
2019
revised:
19
12
2019
accepted:
18
02
2020
pubmed:
24
2
2020
medline:
16
1
2021
entrez:
24
2
2020
Statut:
ppublish
Résumé
Dihydropyrimidine dehydrogenase (DPD) catalyzes the reduction of uracil and thymine bases with electrons derived from NADPH. The mammalian DPD enzyme is a functional homodimer and has an elaborate cofactor arrangement. Two flavin cofactors (FAD and FMN) reside in two active site cavities that are separated by around 60 Å. The flavins are apparently bridged by four Fe
Identifiants
pubmed: 32088324
pii: S1046-5928(19)30524-8
doi: 10.1016/j.pep.2020.105610
pii:
doi:
Substances chimiques
Recombinant Fusion Proteins
0
Dihydrouracil Dehydrogenase (NADP)
EC 1.3.1.2
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
105610Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.