Arginine-178 is an essential residue for ITPA function.


Journal

Archives of biochemistry and biophysics
ISSN: 1096-0384
Titre abrégé: Arch Biochem Biophys
Pays: United States
ID NLM: 0372430

Informations de publication

Date de publication:
08 2023
Historique:
received: 20 06 2023
revised: 18 07 2023
accepted: 22 07 2023
pmc-release: 01 08 2024
medline: 7 8 2023
pubmed: 29 7 2023
entrez: 28 7 2023
Statut: ppublish

Résumé

The inosine triphosphate pyrophosphatase (ITPA) enzyme plays a critical cellular role by removing noncanonical nucleoside triphosphates from nucleotide pools. One of the first pathological ITPA mutants identified is R178C (rs746930990), which causes a fatal infantile encephalopathy, termed developmental and epileptic encephalopathy 35 (DEE 35). The accumulation of noncanonical nucleotides such as inosine triphosphate (ITP), is suspected to affect RNA and/or interfere with normal nucleotide function, leading to development of DEE 35. Molecular dynamics simulations have shown that the very rare R178C mutation does not significantly perturb the overall structure of the protein, but results in a high level of structural flexibility and disrupts active-site hydrogen bond networks, while preliminary biochemical data indicate that ITP hydrolyzing activity is significantly reduced for the R178C mutant. Here we report Michaelis-Menten enzyme kinetics data for the R178C ITPA mutant and three other position 178 ITPA mutants. These data confirm that position 178 is essential for ITPA activity and even conservative mutation at this site (R178K) results in significantly reduced enzyme activity. Our data support that disruption of the active-site hydrogen bond network is a major cause of diminished ITP hydrolyzing activity for the R178C mutation. These results suggest an avenue for developing therapies to address DEE 35.

Identifiants

pubmed: 37506994
pii: S0003-9861(23)00199-6
doi: 10.1016/j.abb.2023.109700
pmc: PMC10530447
mid: NIHMS1921446
pii:
doi:

Substances chimiques

Inosine 5A614L51CT
Pyrophosphatases EC 3.6.1.-
Inosine Triphosphate 132-06-9
Arginine 94ZLA3W45F
Nucleotides 0

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

109700

Subventions

Organisme : NIGMS NIH HHS
ID : R15 GM112121
Pays : United States

Informations de copyright

Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.

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Auteurs

Nicholas E Burgis (NE)

Department of Chemistry, Biochemistry & Physics, Eastern Washington University, Cheney, WA, 99004, USA. Electronic address: nburgis@ewu.edu.

Caitlin April (C)

Department of Chemistry, Biochemistry & Physics, Eastern Washington University, Cheney, WA, 99004, USA.

Kandise VanWormer (K)

Department of Chemistry, Biochemistry & Physics, Eastern Washington University, Cheney, WA, 99004, USA.

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Classifications MeSH