Transient-State Analysis of Porcine Dihydropyrimidine Dehydrogenase Reveals Reductive Activation by NADPH.


Journal

Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623

Informations de publication

Date de publication:
07 07 2020
Historique:
pubmed: 10 6 2020
medline: 24 2 2021
entrez: 10 6 2020
Statut: ppublish

Résumé

Dihydropyrimidine dehydrogenase (DPD) catalyzes the initial step in the catabolism of the pyrimidines uracil and thymine. Crystal structures have revealed an elaborate subunit architecture consisting of two flavin cofactors, apparently linked by four Fe

Identifiants

pubmed: 32516529
doi: 10.1021/acs.biochem.0c00223
doi:

Substances chimiques

Pyrimidines 0
NADP 53-59-8
Flavin Mononucleotide 7N464URE7E
Dihydrouracil Dehydrogenase (NADP) EC 1.3.1.2
pyrimidine K8CXK5Q32L

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2419-2431

Auteurs

Brett A Beaupre (BA)

Department of Chemistry and Biochemistry, Loyola University Chicago, 1068 West Sheridan Road, Chicago, Illinois 60660, United States.

Dariush C Forouzesh (DC)

Department of Chemistry and Biochemistry, Loyola University Chicago, 1068 West Sheridan Road, Chicago, Illinois 60660, United States.

Graham R Moran (GR)

Department of Chemistry and Biochemistry, Loyola University Chicago, 1068 West Sheridan Road, Chicago, Illinois 60660, United States.

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Classifications MeSH