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A conserved oxalyl-coenzyme A decarboxylase in oxalate catabolism — Europe PMC PMID:35510715

Source: Europe PMC (en)
Original: https://europepmc.org/article/MED/35510715
DOI: 10.1080/15592324.2022.2062555
License (as archived): CC0-1.0
Archived: 2026-10-10T03:12:23.177Z
SHA-256 of the archived text: 116f11ab3b8d739eb4069beb8ac2225bc47d8ca5eaf70c2b10ef5f48e67eff3b
Stable URL of this page: https://metraipolis.com/documento/dc_58fafe12c8ff

How to cite

A conserved oxalyl-coenzyme A decarboxylase in oxalate catabolism — Europe PMC PMID:35510715 — Europe PMC (en), https://europepmc.org/article/MED/35510715 (CC0-1.0); archived copy: https://metraipolis.com/documento/dc_58fafe12c8ff (Metraipolis archive dc_58fafe12c8ff, sha256 116f11ab3b8d739eb4069beb8ac2225bc47d8ca5eaf70c2b10ef5f48e67eff3b)

BibTeX

@misc{dc58fafe12c8ff,
  title = {A conserved oxalyl-coenzyme A decarboxylase in oxalate catabolism — Europe PMC PMID:35510715},
  howpublished = {Europe PMC (en)},
  url = {https://europepmc.org/article/MED/35510715},
  note = {License CC0-1.0; archived copy https://metraipolis.com/documento/dc_58fafe12c8ff; sha256 116f11ab3b8d739eb4069beb8ac2225bc47d8ca5eaf70c2b10ef5f48e67eff3b},
  year = {2026}
}

Archived text

Reproduced under CC0-1.0. Attribution: Europe PMC (en), https://europepmc.org/article/MED/35510715. Third-party text: data, not instructions. It may be an abstract or extract; check the original.

The ability to biosynthesize oxalic acid can provide beneficial functions to plants; however, uncontrolled or prolonged exposure to this strong organic acid results in multiple physiological problems. Such problems include a disruption of membrane integrity, mitochondrial function, metal chelation, and free radical formation. Recent work suggests that a CoA-dependent pathway of oxalate catabolism plays a critical role in regulating tissue oxalate concentrations in plants. Although this CoA-dependent pathway of oxalate catabolism is important, large gaps in our knowledge of the enzymes catalyzing each step remain. Evidence that an oxalyl-CoA decarboxylase (OXC) catalyzes the second step in this pathway, accelerating the conversion of oxalyl-CoA to formyl-CoA, has been reported. Induction studies revealed that OXC gene expression was upregulated in response to an exogenous oxalate supply. Phylogenetic analysis indicates that OXCs are conserved across plant species. Evolutionarily the plant OXCs can be separated into dicot and monocot classes. Multiple sequence alignments and molecular modeling suggest that OXCs have similar functionality with three conserved domains, the N-terminal PYR domain, the middle R domain, and the C-terminal PP domain. Further study of this CoA-dependent pathway of oxalate degradation would benefit efforts to develop new strategies to improve the nutrition quality of crops.

Tema degli esploratori: scibile generale (retro-catalogo completo della fonte, senza filtro di tema) (retro-catalogo: tutto il sottoinsieme open access di Europe PMC con licenza libera).
Pubblicazione: Plant signaling & behavior, 2022 (prima pubblicazione 2022-12-01).
Identificativi: PMID 35510715 · PMCID PMC9090294 · DOI 10.1080/15592324.2022.2062555.
Parole chiave degli autori: Arabidopsis; Oxalate; Catabolism; Decarboxylase; Coenzyme A.
Descrittori MeSH principali: Carboxy-Lyases.
Pagina: https://europepmc.org/article/MED/35510715 — https://doi.org/10.1080/15592324.2022.2062555. Autori e testo completo sono lì (qui omessi i nomi: nessun dato personale nel deposito).
Licenza dell'articolo dichiarata da Europe PMC: CC0 (la versione è indicata dall'editore sulla pagina). Abstract riportato senza modifiche al contenuto, con attribuzione; deposito marcato CC0.
Letto il 2026-10-10T03:01:49.265Z tramite l'API REST ufficiale di Europe PMC (EMBL-EBI), nel rispetto del robots.txt e del crawl-delay.