Multiple substrate recognition by yeast diadenosine and diphosphoinositol polyphosphate phosphohydrolase through phosphate clamping-Reference-Cited by-同舟云学术

Multiple substrate recognition by yeast diadenosine and diphosphoinositol polyphosphate phosphohydrolase through phosphate clamping

Published:2021-04-23 Issue:17 Volume:7 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Márquez-Moñino María Ángeles¹^ORCID,Ortega-García Raquel¹,Shipton Megan L.²^ORCID,Franco-Echevarría Elsa¹^ORCID,Riley Andrew M.²^ORCID,Sanz-Aparicio Julia¹,Potter Barry V. L.²^ORCID,González Beatriz¹^ORCID

Affiliation:

1. Department of Crystallography and Structural Biology, Institute of Physical-Chemistry Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.

2. Drug Discovery and Medicinal Chemistry, Department of Pharmacology, University of Oxford Mansfield Road, Oxford OX1 3QT, UK.

Abstract

A NUDIX enzyme joins inositide and polyphosphate metabolisms through multisubstrate binding ability.

Funder

Wellcome

Ministerio de Ciencia e Innovación

Wellcome Trust Centre for Mitochondrial Research

Ministerio de Ciencia, Innovación y Universidades

Ministerio de Economía, Industria y Competitividad, Gobierno de España

Ministerio de Economía y Competitividad

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference51 articles.

1. Back in the water: the return of the inositol phosphates

2. Inositol Pyrophosphates: Signaling Molecules with Pleiotropic Actions in Mammals

3. Diphosphoinositol Polyphosphates: Metabolic Messengers?

4. Metabolism and Functions of Inositol Pyrophosphates: Insights Gained from the Application of Synthetic Analogues

5. Messengers for morphogenesis: inositol polyphosphate signaling and yeast pseudohyphal growth

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