A single evolutionarily divergent mutation determines the different FAD‐binding affinities of human and rat NQO1 due to site‐specific phosphorylation-Reference-Cited by-同舟云学术

A single evolutionarily divergent mutation determines the different FAD‐binding affinities of human and rat NQO1 due to site‐specific phosphorylation

Published:2021-12-09 Issue:1 Volume:596 Page:29-41
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Letters

Author:

Pacheco‐Garcia Juan Luis¹^ORCID,Loginov Dmitry²^ORCID,Rizzuti Bruno³⁴^ORCID,Vankova Pavla⁵⁶^ORCID,Neira Jose L.⁴⁷^ORCID,Kavan Daniel²^ORCID,Mesa‐Torres Noel¹^ORCID,Guzzi Rita³⁸^ORCID,Man Petr²^ORCID,Pey Angel L.⁹^ORCID

Affiliation:

1. Departamento de Química Física Facultad de Ciencias Universidad de Granada Spain

2. Institute of Microbiology of the Czech Academy of Sciences BioCeV Praha Czech Republic

3. CNR‐NANOTEC SS Rende (CS) Department of Physics University of Calabria Rende Italy

4. Instituto de Biocomputación y Física de los Sistemas Complejos (BIFI) Zaragoza Spain

5. Institute of Biotechnology of the Czech Academy of Sciences BioCeV Vestec Czech Republic

6. Department of Biochemistry Faculty of Science Charles University Prague Czech Republic

7. Instituto de Biología Molecular y Celular Universidad Miguel Hernández Elche Spain

8. Molecular Biophysics Laboratory Department of Physics University of Calabria Rende Italy

9. Departamento de Química Física Unidad de Excelencia de Química aplicada a Biomedicina y Medioambiente e Instituto de Biotecnología Facultad de Ciencias Universidad de Granada Spain

Funder

Horizon 2020

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.14238

Reference46 articles.

1. The human flavoproteome

2. Recognition of enzymes lacking bound cofactor by protein quality control

3. Phosphorylation compromises FAD binding and intracellular stability of wild-type and cancer-associated NQO1: Insights into flavo-proteome stability

4. A Mutually Inhibitory Feedback Loop between the 20S Proteasome and Its Regulator, NQO1

5. FAD-dependent regulation of transcription, translation, post-translational processing, and post-processing stability of various mitochondrial acyl-CoA dehydrogenases and of electron transfer flavoprotein and the site of holoenzyme formation.

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1. Phenotypic Modulation of Cancer-Associated Antioxidant NQO1 Activity by Post-Translational Modifications and the Natural Diversity of the Human Genome;Antioxidants;2023-02-04

2. Different phenotypic outcome due to site-specific phosphorylation in the cancer-associated NQO1 enzyme studied by phosphomimetic mutations;Archives of Biochemistry and Biophysics;2022-10