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
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

105610

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

Auteurs

Brett A Beaupre (BA)

Department of Chemistry and Biochemistry, Loyola University Chicago, Flanner Hall, 1068 W Sheridan Rd, Chicago, IL, 60660, USA.

Joseph V Roman (JV)

Department of Chemistry and Biochemistry, Loyola University Chicago, Flanner Hall, 1068 W Sheridan Rd, Chicago, IL, 60660, USA.

Graham R Moran (GR)

Department of Chemistry and Biochemistry, Loyola University Chicago, Flanner Hall, 1068 W Sheridan Rd, Chicago, IL, 60660, USA. Electronic address: gmoran3@luc.edu.

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Classifications MeSH