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Article

The Asp1 pyrophosphatase from S. pombe hosts a [2Fe-2S]2+ cluster in vivo.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Feb 2021

Rosenbach Hannah, Walla Eva, Cutsail George E, Birrell James A, Pascual-Ortiz Marina, DeBeer Serena, Fleig Ursula, Span Ingrid

Abstract excerpt

The Schizosaccharomyces pombe Asp1 protein is a bifunctional kinase/pyrophosphatase that belongs to the highly conserved eukaryotic diphosphoinositol pentakisphosphate kinase PPIP5K/Vip1 family. The N-terminal Asp1 kinase domain generates specific high-energy inositol pyrophosphate (IPP) molecules, which are hydrolyzed by the C-terminal Asp1 pyrophosphatase domain (Asp1365-920). Thus, Asp1 activities regulate the...

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PMID: 33544225
DOI: 10.1007/s00775-020-01840-w
PMCID: PMC8038993

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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