Cited by 154Metabolism and Genetic DisordersAmino Acid Enzymes and MetabolismNeurological diseases and metabolism

The human gene SLC25A17 encodes a peroxisomal transporter of coenzyme A, FAD and NAD+

Agrimi, Gennaro, Russo, Annamaria, Scarcia, Pasquale, Palmieri, Ferdinando·2012·Biochemical Journal

Abstract

The essential cofactors CoA, FAD and NAD+ are synthesized outside the peroxisomes and therefore must be transported into the peroxisomal matrix where they are required for important processes. In the present study we have functionally identified and characterized SLC25A17 (solute carrier family 25 member 17), which is the only member of the mitochondrial carrier family that has previously been shown to be localized in the peroxisomal membrane. Recombinant and purified SLC25A17 was reconstituted into liposomes. Its transport properties and kinetic parameters demonstrate that SLC25A17 is a transporter of CoA, FAD, FMN and AMP, and to a lesser extent of NAD+, PAP (adenosine 3′,5′-diphosphate) and ADP. SLC25A17 functioned almost exclusively by a counter-exchange mechanism, was saturable and was inhibited by pyridoxal 5′-phosphate and other mitochondrial carrier inhibitors. It was expressed to various degrees in all of the human tissues examined. Its main function is probably to transport free CoA, FAD and NAD+ into peroxisomes in exchange for intraperoxisomally generated PAP, FMN and AMP. The present paper is the first report describing the identification and characterization of a transporter for multiple free cofactors in peroxisomes.

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Crossref · 10.1042/bj20111420

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  • SLC25A17 localizes in peroxisomes, where NAD+ participates in beta-oxidation as in mitochondria.

    “Furthermore, some NAD+ transporters (SLC25A17) localize in peroxisomes, where NAD+ participates in b-oxidation like in mitochondria (Agrimi et al., 2012).”

    From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Agrimi et al., 2012

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Authors
Agrimi, G., Russo, A., Scarcia, P., & Palmieri, F.
Affiliations
  • University of Bari Aldo Moro (IT)
  • Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IT)
Corresponding author
  • Agrimi, Gennaro
  • Russo, Annamaria
  • Scarcia, Pasquale
  • Palmieri, Ferdinando
Venue
Biochemical Journal
Published
2012-03-14
Volume
443
Issue
1
Pages
241-247
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W2152510156
Cited by
154
References
49
Citations by year
2026: 3 · 2025: 11 · 2024: 24 · 2023: 10 · 2022: 10 · 2021: 11 · 2020: 18 · 2019: 12 · 2018: 15 · 2017: 5 · 2016: 4 · 2015: 8 · 2014: 8 · 2013: 4 · 2012: 11
FWCI
4.42
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemical Journal (publishedVersion)
  • PubMed (publishedVersion)
  • CINECA IRIS Institutional Research Information System (University of Bari Aldo Moro) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
  • Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Keywords
coenzyme A, FAD, NAD+, flavin mononucleotide, AMP, PAP, mitochondrial carrier family, liposome reconstitution
MeSH terms
Adenosine Diphosphate, Adenosine Monophosphate, Coenzyme A, Escherichia coli, Flavin-Adenine Dinucleotide, Flavin Mononucleotide, Humans, Kinetics, Liposomes, Membrane Proteins, NAD, Organ Specificity, Recombinant Proteins, Gene Expression, Peroxisomes

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