Deciphering CAD: Structure and function of a mega-enzymatic pyrimidine factory in health and disease.

aspartate transcarbamoylase carbamoyl phosphate synthetase de novo pyrimidine biosynthesis dihydroorotase multienzymatic protein nucleotide metabolism rare diseases

Journal

Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750

Informations de publication

Date de publication:
10 2021
Historique:
revised: 12 07 2021
received: 01 07 2021
accepted: 13 07 2021
pubmed: 22 7 2021
medline: 25 12 2021
entrez: 21 7 2021
Statut: ppublish

Résumé

CAD is a 1.5 MDa particle formed by hexameric association of a 250 kDa protein divided into different enzymatic domains, each catalyzing one of the initial reactions for de novo biosynthesis of pyrimidine nucleotides: glutaminase-dependent Carbamoyl phosphate synthetase, Aspartate transcarbamoylase, and Dihydroorotase. The pathway for de novo pyrimidine synthesis is essential for cell proliferation and is conserved in all living organisms, but the covalent linkage of the first enzymatic activities into a multienzymatic CAD particle is unique to animals. In other organisms, these enzymatic activities are encoded as monofunctional proteins for which there is abundant structural and biochemical information. However, the knowledge about CAD is scarce and fragmented. Understanding CAD requires not only to determine the three-dimensional structures and define the catalytic and regulatory mechanisms of the different enzymatic domains, but also to comprehend how these domains entangle and work in a coordinated and regulated manner. This review summarizes significant progress over the past 10 years toward the characterization of CAD's architecture, function, regulatory mechanisms, and cellular compartmentalization, as well as the recent finding of a new and rare neurometabolic disorder caused by defects in CAD activities.

Identifiants

pubmed: 34288185
doi: 10.1002/pro.4158
pmc: PMC8442968
doi:

Substances chimiques

CAD trifunctional enzyme 0
Aspartate Carbamoyltransferase EC 2.1.3.2
Dihydroorotase EC 3.5.2.3
Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) EC 6.3.5.5

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

1995-2008

Informations de copyright

© 2021 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.

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Auteurs

Francisco Del Caño-Ochoa (F)

Instituto de Biomedicina de Valencia (IBV-CSIC), Valencia, Spain.
Group 739, Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER) - Instituto de Salud Carlos III, Valencia, Spain.

Santiago Ramón-Maiques (S)

Instituto de Biomedicina de Valencia (IBV-CSIC), Valencia, Spain.
Group 739, Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER) - Instituto de Salud Carlos III, Valencia, Spain.

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Classifications MeSH