Affinage

SIRT5

NAD-dependent protein deacylase sirtuin-5, mitochondrial · UniProt Q9NXA8

Length
310 aa
Mass
33.9 kDa
Annotated
2026-06-10
100 papers in source corpus 48 papers cited in narrative 49 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SIRT5 is an NAD+-dependent lysine deacylase that hydrolyzes negatively charged acyl marks—succinyl, malonyl, and glutaryl groups—from hundreds of metabolic proteins, a specificity conferred by acyl-pocket residues Arg105 and Tyr102 that accommodate the carboxylate of these acyl groups (PMID:22076378, PMID:23806337). Although enriched in the mitochondrial matrix, where it deacylates urea-cycle and energy-metabolism enzymes, a substantial fraction is extramitochondrial in the cytosol and nucleus, and the enzyme is also present in peroxisomes (PMID:19410549, PMID:23806337, PMID:29491006). Through these activities SIRT5 sits at the hub of multiple metabolic axes: it deacetylates and activates CPS1 to drive ureagenesis and ammonia disposal during fasting (PMID:19410549, PMID:20097174); desuccinylates the rate-limiting ketogenic enzyme HMGCS2 and the fatty-acid-oxidation enzymes VLCAD and CPT2 to sustain lipid catabolism (PMID:24315375, PMID:25811481, PMID:38718533); and regulates glycolytic and TCA-cycle enzymes including GAPDH, PKM2, citrate synthase, OGDH, and SDHA (PMID:26073543, PMID:28614718, PMID:32284438, PMID:31247190, PMID:30703481). SIRT5 governs redox homeostasis by deacylating and activating the NADPH-generating enzymes IDH2 and G6PD and the peroxisomal oxidase ACOX1, with its loss producing elevated ROS and oxidative stress (PMID:27113762, PMID:29491006). Beyond metabolism, SIRT5 controls innate immune signaling by desuccinylating MAVS to restrain type I interferon responses and TBK1 to dampen inflammatory output (PMID:32301534, PMID:40087407, PMID:39673708), and modulates p53-dependent apoptosis through desuccinylation of p53 at K120 (PMID:34642466). SIRT5 expression is set transcriptionally by PGC-1α and ATF4 and opposed by AMPK (PMID:24687991, PMID:35963851). Many of these substrate relationships drive cancer cell proliferation and survival, linking SIRT5 to tumor metabolism in melanoma, colorectal, renal, and pancreatic cancers (PMID:29180469, PMID:34245764, PMID:33945506).

Mechanistic history

Synthesis pass · year-by-year structured walk · 10 steps
  1. 2008 Medium

    Established the first SIRT5 substrate and the principle that its dual import into mitochondrial intermembrane space and matrix shapes substrate access.

    Evidence In vitro deacetylation and mitochondrial import assays with cytochrome c

    PMID:18680753

    Open questions at the time
    • Physiological significance of cytochrome c deacetylation not established
    • Did not define the deacylase specificity later found to dominate SIRT5 activity
  2. 2009 High

    Defined SIRT5's first physiological role by showing it deacetylates and activates CPS1 to control ureagenesis and ammonia handling during fasting.

    Evidence Co-IP, in vitro deacetylation, subcellular fractionation, and SIRT5 KO mouse fasting phenotype

    PMID:19410549

    Open questions at the time
    • Framed SIRT5 as a deacetylase before its preferred desuccinylase/demalonylase activity was recognized
    • Mechanism limited to a single substrate
  3. 2011 High

    Reclassified SIRT5 as an efficient desuccinylase/demalonylase and mapped the acyl-pocket residues (Arg105, Tyr102) that explain its preference for acidic acyl groups, redefining its enzymatic identity.

    Evidence In vitro enzymatic assays, active-site mutagenesis, mass spectrometry, SIRT5 KO mouse (CPS1 succinylation)

    PMID:22076378

    Open questions at the time
    • Did not enumerate the full substrate landscape
    • Relative contribution of succinylation vs malonylation in vivo unresolved
  4. 2013 High

    Scaled SIRT5 function from single substrates to a proteome-wide regulator, showing it controls thousands of succinylation sites and that a substantial pool is extramitochondrial.

    Evidence Quantitative succinylome proteomics with enzymatic validation and subcellular fractionation; parallel study mapping HMGCS2 succinylation and ketogenesis

    PMID:23806337 PMID:24315375

    Open questions at the time
    • Functional consequence assigned to only a fraction of mapped sites
    • Mechanism of extramitochondrial targeting unclear
  5. 2014 High

    Added deglutarylation to the SIRT5 repertoire and connected it to glutaric acidemia, while identifying its upstream transcriptional control by PGC-1α and AMPK.

    Evidence Proteome-wide glutarylation mapping, enzymatic assays, disease models; PGC-1α/AMPK overexpression and metformin studies

    PMID:24687991 PMID:24703693

    Open questions at the time
    • PGC-1α/AMPK regulation is Medium confidence and from a single lab
    • Tissue-specificity of transcriptional control not defined
  6. 2016 High

    Connected SIRT5 to redox defense and cardiac energetics, showing it activates NADPH-producing enzymes and that its cardiac loss causes hypertrophic cardiomyopathy through impaired fatty acid oxidation.

    Evidence Enzymatic assays for IDH2/G6PD, NADPH/GSH measurement, acyl-CoA metabolomics and SIRT5 KO mouse cardiac phenotyping

    PMID:27051063 PMID:27113762

    Open questions at the time
    • Direct contribution of each substrate to in vivo redox phenotype not dissected
    • Whether antioxidant role is conserved across tissues unaddressed
  7. 2017 High

    Extended SIRT5 to glycolytic, serine-metabolism, and innate-immune control and showed membrane targeting via cardiolipin binding and electron-transport-chain regulation.

    Evidence Co-IP, enzymatic assays, mutagenesis and ChIP for PKM2/SHMT2; cardiolipin-binding and respirometry studies of ETC complexes

    PMID:28458255 PMID:28614718 PMID:29180469

    Open questions at the time
    • Opposing reports on whether PKM2 succinylation activates or inhibits its activity (#11 vs #12)
    • Quantitative contribution of cardiolipin binding to substrate selection unresolved
  8. 2020 High

    Defined a direct anti-inflammatory/antiviral function by showing SIRT5 desuccinylates MAVS to suppress type I IFN, establishing a non-metabolic signaling role.

    Evidence MS site mapping, Co-IP, in vitro desuccinylation, MAVS aggregation and IFN assays, catalytic mutant (H158Y), SIRT5 KO viral infection model

    PMID:32301534

    Open questions at the time
    • Reconciliation with later MAVS-independent immune effects (#29) not provided
    • Subcellular site of MAVS desuccinylation not pinpointed
  9. 2021 High

    Linked SIRT5 to apoptosis and to metabolite-driven epigenetic control of cancer cell gene expression, broadening its role beyond direct enzyme regulation.

    Evidence Co-IP, MS, p53 reporter and double-KO mouse for p53 K120; KO melanoma cell/mouse models with metabolite and transcriptomic profiling for chromatin marks; ATF4 epistasis for SIRT5 transcription

    PMID:33945506 PMID:34642466 PMID:35963851

    Open questions at the time
    • Epigenetic effects in melanoma are indirect and not traced to a specific desuccinylated substrate
    • ATF4 regulation is Medium confidence, single lab
  10. 2024 High

    Consolidated SIRT5 as a desuccinylase of inflammatory and autophagic regulators with translational relevance, including TBK1, RAB7A, and CPT2 in aging, sepsis, neurodegeneration, and diabetic cardiomyopathy.

    Evidence Site-mapping MS, mutagenesis, interaction assays, KO and adoptive-transfer/gene-therapy mouse models

    PMID:38718533 PMID:38837686 PMID:39673708 PMID:40087407

    Open questions at the time
    • Multiple TBK1 site reports (K137 vs K38/K154/K692) not fully reconciled
    • Some disease-rescue findings are Medium confidence from single labs

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how SIRT5 partitions among mitochondria, cytosol, nucleus, and peroxisomes to select among its hundreds of substrates, and which desuccinylation events are physiologically rate-limiting versus bystander modifications.
  • No unified model of compartmental substrate selection
  • Functional ranking of the proteome-wide acylation sites incomplete
  • Conflicting substrate-effect directions for PKM2 and TBK1 unsettled

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 7 GO:0016787 hydrolase activity 4 GO:0008289 lipid binding 2
Localization
GO:0005739 mitochondrion 4 GO:0005829 cytosol 2 GO:0005634 nucleus 1 GO:0005777 peroxisome 1
Pathway
R-HSA-1430728 Metabolism 7 R-HSA-168256 Immune System 3 R-HSA-8953854 Metabolism of RNA 3 R-HSA-9612973 Autophagy 2 R-HSA-5357801 Programmed Cell Death 1
Partners
AKT2CPS1GLSMAVSP53PKM2SHMT2TBK1

Evidence

Reading pass · 49 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2011 SIRT5 is an efficient protein lysine desuccinylase and demalonylase in vitro. The preference for succinyl and malonyl groups is explained by an arginine residue (Arg105) and tyrosine residue (Tyr102) in the acyl pocket of SIRT5. Deletion of SIRT5 in mice increases succinylation on carbamoyl phosphate synthase 1 (CPS1) in vivo. In vitro enzymatic assay, active-site mutagenesis (acyl pocket residues), mass spectrometry identification of substrates, SIRT5 knockout mouse Science High 22076378
2009 SIRT5 localizes to the mitochondrial matrix, interacts with and deacetylates CPS1, and upregulates CPS1 enzymatic activity. During fasting, NAD+ in liver mitochondria increases, triggering SIRT5-mediated CPS1 deacetylation. SIRT5 KO mice fail to upregulate CPS1 activity and exhibit elevated blood ammonia during fasting. Co-immunoprecipitation, in vitro deacetylation assay, SIRT5 KO mouse phenotyping, subcellular fractionation/localization Cell High 19410549
2013 Systematic profiling of the mammalian succinylome identified 2,565 succinylation sites on 779 proteins regulated by SIRT5. SIRT5 represses biochemical activity of pyruvate dehydrogenase complex and succinate dehydrogenase. A substantial fraction of SIRT5 is extramitochondrial (cytosolic and nuclear). Quantitative proteomics (affinity enrichment + mass spectrometry), enzymatic activity assays, subcellular fractionation Molecular Cell High 23806337
2014 SIRT5 is a lysine deglutarylase. Proteome-wide analysis identified 683 glutarylation sites in 191 proteins. CPS1 is glutarylated and targeted by SIRT5 for deglutarylation; glutarylation suppresses CPS1 enzymatic activity in cell lines, mice, and a model of glutaric acidemia type I. Immunoblot, mass spectrometry, biochemical validation, SIRT5 enzymatic assay, cell lines and mouse models Cell Metabolism High 24703693
2013 SIRT5 regulates succinylation of the rate-limiting ketogenic enzyme HMGCS2 both in vivo and in vitro. Mutation of hypersuccinylated residues K83 and K310 on HMGCS2 to glutamic acid strongly inhibits enzymatic activity. Loss of SIRT5 leads to accumulation of medium- and long-chain acylcarnitines and decreased β-hydroxybutyrate production in vivo. Label-free quantitative proteomics, in vitro desuccinylation assay, site-directed mutagenesis, SIRT5 KO mouse metabolic phenotyping Cell Metabolism High 24315375
2015 SIRT5 is a global regulator of lysine malonylation. 1,137 malonyllysine sites across 430 proteins were identified, with 183 significantly increased in SIRT5 KO mice. Glycolysis is the top SIRT5-regulated pathway; glycolytic flux is diminished in SIRT5 KO primary hepatocytes. Substitution of malonylated K184 in GAPDH with glutamic acid suppresses its enzymatic activity. Affinity enrichment and label-free quantitative proteomics, SIRT5 KO mouse, primary hepatocyte glycolytic flux assays, site-directed mutagenesis of GAPDH K184 Molecular Cell High 26073543
2008 SIRT5 can deacetylate cytochrome c (a mitochondrial intermembrane space protein) and can be translocated into both the mitochondrial intermembrane space and the matrix, suggesting localization contributes to substrate selection. In vitro deacetylation assay, mitochondrial import assay Journal of Molecular Biology Medium 18680753
2010 SIRT5 overexpression in transgenic mice leads to increased CPS1 deacetylation and activation, and upregulates urea production in hepatocytes, confirming SIRT5-mediated CPS1 deacetylation and activation in vivo. SIRT5 transgenic mouse model, 2D electrophoresis, enzymatic activity assay, urea production assay Biochemical and Biophysical Research Communications Medium 20097174
2013 SOD1 is succinylated, which decreases its activity. SIRT5 binds to, desuccinylates, and activates SOD1, and SOD1-mediated ROS reduction is increased when SIRT5 is co-expressed. Mutation of the SOD1 succinylation site inhibits lung tumor cell growth. Co-immunoprecipitation, in vitro desuccinylation assay, enzymatic activity assay, cell growth assay with succinylation-site mutant Biochemical and Biophysical Research Communications Medium 24140062
2016 SIRT5 desuccinylates IDH2 and deglutarylates G6PD, activating both NADPH-producing enzymes. SIRT5 knockdown/knockout leads to high cellular ROS, decreased NADPH, lower GSH, and increased susceptibility to oxidative stress. In vitro deacylation assay, enzymatic activity assays (IDH2, G6PD), siRNA knockdown, SIRT5 KO cells, NADPH/GSH measurement EMBO Reports High 27113762
2016 Succinyl-CoA is the most abundant acyl-CoA in the heart. SIRT5 deletion leads to predominant accumulation of lysine succinylation in cardiac proteins. ECHA (involved in fatty acid oxidation) is a major SIRT5 substrate in the heart, and Sirt5 KO mice develop hypertrophic cardiomyopathy with reduced ECHA activity, increased long-chain acyl-CoAs, and decreased cardiac ATP under fasting. Acyl-CoA profiling (metabolomics), proteomic succinylome analysis, SIRT5 KO mouse cardiac phenotyping (echocardiography, biochemical assays) PNAS High 27051063
2017 PKM2 is a physiological substrate of SIRT5. SIRT5-regulated hypersuccinylation inhibits pyruvate kinase activity of PKM2 by promoting its tetramer-to-dimer transition. A succinylation-mimetic PKM2 K311E mutation promotes nuclear accumulation and increases protein kinase activity, forming a PKM2-HIF1α complex at the IL-1β promoter in LPS-stimulated macrophages. SIRT5-deficient mice are more susceptible to DSS-induced colitis. Co-immunoprecipitation, enzymatic activity assay, site-directed mutagenesis (K311E), chromatin immunoprecipitation, SIRT5 KO mouse colitis model Cell Reports High 28614718
2017 PKM2 is succinylated at K498, which increases its activity. SIRT5 binds to, desuccinylates, and inhibits PKM2 activity. Increased ROS decreases succinylation and activity of PKM2 by increasing its binding to SIRT5. A succinylation-mimetic K498E mutant decreases cellular NADPH and inhibits cell proliferation and tumor growth. Co-immunoprecipitation, in vitro desuccinylation assay, enzymatic activity assay, site-directed mutagenesis (K498E), cell proliferation and tumor growth assays Oncotarget Medium 28036303
2015 SIRT5 and SIRT3 both regulate VLCAD (very long-chain acyl-CoA dehydrogenase). SIRT5 desuccinylates K299 (stabilizing FAD cofactor) and K482, K492, K507 (cardiolipin-binding domain). Succinylation of C-terminal lysines eliminates VLCAD binding to cardiolipin; SIRT5-mediated desuccinylation rescues membrane binding. VLCAD from SIRT5 KO mice shows reduced cardiolipin binding. In vitro desuccinylation assay, site-directed mutagenesis, cardiolipin-binding assay, SIRT5 KO mouse liver mitochondria PLOS ONE High 25811481
2015 SIRT5 regulates ammonia production in non-liver cells by controlling glutamine metabolism. SIRT5 co-immunoprecipitates with glutaminase, and SIRT5 inhibition increases succinylation of glutaminase. SIRT5 silencing increases ammonia production, and this triggers increased autophagy and mitophagy, which is prevented by glutaminase inhibition or glutamine withdrawal. Co-immunoprecipitation, ammonia measurement, succinylation assay, autophagy/mitophagy markers, siRNA knockdown, SIRT5 inhibitor (MC3482) Autophagy Medium 25700560
2017 SIRT5 directly desuccinylates SHMT2 at lysine 280, which is crucial for activating SHMT2 enzymatic activity and driving serine catabolism. Hypersuccinylation of SHMT2 at K280 inhibits its enzymatic activity and downregulates tumor cell growth in vitro and in vivo. Co-immunoprecipitation, in vitro desuccinylation assay, site-directed mutagenesis (K280), enzymatic activity assay, xenograft tumor model Cancer Research High 29180469
2018 SIRT5 is present in peroxisomes and ACOX1 is a physiological substrate of SIRT5. SIRT5-mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation in both cultured cells and mouse livers. SIRT5 deletion increases H2O2 production and oxidative DNA damage, reversible by ACOX1 knockdown. Subcellular fractionation (peroxisome isolation), Co-IP, in vitro desuccinylation assay, ACOX1 activity assay (dimer formation), H2O2 measurement, SIRT5 KO mouse EMBO Reports High 29491006
2017 SIRT5 binds to cardiolipin via an amphipathic helix on its N-terminus. SIRT5 desuccinylates inner mitochondrial membrane proteins, particularly targeting Complex I and Complex II. SIRT5-/- HEK293 cells show defects in Complex I- and Complex II-driven respiration. SIRT5-/- mice exhibit mild lactic acidosis consistent with Complex II deficiency. Cardiolipin-binding assay, in vitro succinylation/desuccinylation assay, quantitative mass spectrometry, Seahorse respirometry (SIRT5 KO cells), SIRT5 KO mouse metabolic phenotyping Journal of Biological Chemistry High 28458255
2018 SIRT5 deacetylates LDHB at lysine-329, promoting its enzymatic activity. SIRT5 KO or inhibition increases LDHB acetylation at K329 and inhibits LDHB activity, downregulating autophagy and colorectal cancer cell growth in vitro and in vivo. Mass spectrometry (substrate identification), Co-IP, in vitro deacetylation assay, enzymatic activity assay, SIRT5 KO/inhibitor, xenograft Molecular Oncology Medium 30443978
2019 SIRT5 stabilizes glutaminase (GLS) in transformed cells by desuccinylating GLS and thereby protecting it from ubiquitin-mediated degradation. Co-immunoprecipitation, in vitro desuccinylation assay, ubiquitination assay, GLS protein stability assay, SIRT5 KO/OE in cell lines and mouse models PNAS High 31843902
2014 SIRT5 expression is under the control of PGC-1α (via PPARα and ERRα) and AMPK, which have opposite effects: PGC-1α increases SIRT5 mRNA ~4-fold, while AMPK activation decreases SIRT5 mRNA by ~58%. SIRT5 overexpression increases ATP synthesis and oxygen consumption in HepG2 cells without affecting mitochondrial biogenesis. PGC-1α overexpression in mouse primary hepatocytes, AMPK overexpression, metformin treatment in vivo and in vitro, Seahorse respirometry FASEB Journal Medium 24687991
2020 MAVS is a physiological substrate of SIRT5. MAVS is succinylated upon viral challenge at Lysine 7. SIRT5-catalyzed desuccinylation of MAVS at K7 diminishes MAVS aggregation after viral infection, inhibiting MAVS activation and impairing type I IFN production. SIRT5 enzyme-deficient mutant (H158Y) loses suppressive role on MAVS activation. Sirt5-deficient mice are resistant to viral infection. Mass spectrometry, Co-IP, in vitro desuccinylation assay, MAVS aggregation assay, IFN production assay, catalytic mutant (H158Y), SIRT5 KO mouse viral infection model EMBO Journal High 32301534
2021 SIRT5 interacts with p53 and desuccinylates p53 at Lysine 120, suppressing p53 transcriptional activity. Succinylation of p53 at K120 is identified as a novel PTM. In p53/Sirt5 double KO mice, suppression of p53 target gene expression and cell apoptosis upon DNA damage is p53-dependent. Co-immunoprecipitation, mass spectrometry (K120 identification), in vitro desuccinylation assay, p53 transcriptional reporter, double KO mouse Cell Death and Differentiation High 34642466
2020 SIRT5 interacts with citrate synthase (CS) and desuccinylates CS at evolutionarily conserved residues K393 and K395. Hypersuccinylation of CS at K393 and K395 dramatically reduces its enzymatic activity and suppresses colon cancer cell proliferation and migration. Co-immunoprecipitation, in vitro desuccinylation assay, site-directed mutagenesis (K393, K395), enzymatic activity assay, cell proliferation/migration assays Biological Chemistry Medium 32284438
2019 SIRT5 directly interacts with and desuccinylates OGDH (2-oxoglutarate dehydrogenase), inhibiting OGDH complex activity. SIRT5 loss decreases mitochondrial membrane potential and ATP while increasing ROS through OGDH. OGDH inhibition reverses cell growth and migration increases induced by SIRT5 deletion. Co-immunoprecipitation, in vitro desuccinylation assay, OGDH activity assay, mitochondrial membrane potential, ATP/ROS measurement, siRNA epistasis Experimental Cell Research Medium 31247190
2019 SIRT5 desuccinylates SDHA at K547, inhibiting succinate dehydrogenase activity by suppressing SDH5 binding. SIRT5 silencing leads to hypersuccinylation and reactivation of SDHA, inhibiting ccRCC cell proliferation. Co-immunoprecipitation, in vitro desuccinylation assay, SDH activity assay, site-directed mutagenesis (K547R), SIRT5 siRNA knockdown Free Radical Biology and Medicine Medium 30703481
2016 PKCε activation increases SIRT5 levels and desuccinylation activity in isolated mitochondria from rat cortical cultures in a Nampt-dependent manner. SIRT5 regulates oxygen consumption with Complex I, Complex II, and Complex IV substrates. PKCε-mediated neuroprotection against ischemia is abolished in SIRT5-/- mice, establishing SIRT5 as a downstream effector of PKCε-mediated ischemic tolerance. Isolated mitochondria, PKCε activator treatment, desuccinylation activity assay, Seahorse respirometry, SIRT5 KO mouse ischemia model (OGD and MCAO) Scientific Reports Medium 27435822
2019 SIRT5 deficiency leads to suppression of mitochondrial NADH oxidation and inhibition of ATP synthase activity, decreasing mitochondrial ATP production, increasing AMP/ATP ratio, and activating AMPK in cultured cells and mouse hearts under energy stress. SIRT5 KO attenuates transverse aortic constriction-induced cardiac hypertrophy in mice via AMPK activation. SIRT5 KO cell lines, mouse heart SIRT5 KO, ATP synthase activity assay, Seahorse respirometry, AMP/ATP ratio, AMPK activation assay, TAC model PLOS ONE Medium 30759120
2023 SIRT5 desuccinylates ME2 (mitochondrial malic enzyme 2) at K346. Glutamine deprivation enhances SIRT5-ME2 interaction and promotes desuccinylation, activating ME2 enzymatic activity and enhancing mitochondrial respiration. Co-immunoprecipitation, in vitro desuccinylation assay, site-directed mutagenesis (K346), ME2 enzymatic activity assay, Seahorse respirometry, SIRT5 KO Cell Death and Differentiation Medium 38007551
2022 SIRT5 interacts with SARS-CoV-2 Nsp14 (but not Nsp10), suggesting SIRT5 and Nsp10 are parts of separate Nsp14 complexes. The SIRT5 catalytic domain is necessary for interaction with Nsp14, but Nsp14 does not appear to be directly deacylated by SIRT5. SIRT5 KO cells express higher basal innate immunity markers and mount a stronger antiviral response independently of MAVS. Co-immunoprecipitation, catalytic domain mutant analysis, SIRT5 KO cell lines, viral replication assays, innate immunity marker quantification PLOS Pathogens Medium 36095012
2018 SIRT5 isoforms 1-3 localize to mitochondria, while SIRT5iso4 localizes mainly to the cytoplasm. SIRT5iso2-4 have little deacylase activity compared to SIRT5iso1. Fluorescence microscopy (GFP-tagged isoforms), subcellular fractionation, in vitro deacylase activity assay Biochemical and Biophysical Research Communications Medium 29932920
2021 SIRT5 loss in PDAC enhances glutamine and glutathione metabolism via acetylation-mediated activation of GOT1. A selective SIRT5 activator (MC3138) diminishes nucleotide pools and sensitizes PDAC cells to gemcitabine. SIRT5 conditional KO mouse PDAC model, metabolomics, proteomics, siRNA knockdown in organoids, SIRT5 activator in patient-derived xenografts Gastroenterology Medium 34245764
2022 TRIM21 promotes SIRT5 ubiquitination and degradation upon LPS challenge, while HAUSP (a deubiquitinating enzyme) stabilizes SIRT5. In a feedback loop, SIRT5 degradation sustains acetylation of TRIM21 at K351, increasing its E3 ligase activity in LPS-activated macrophages and enhancing IL-1β production. Co-immunoprecipitation, ubiquitination assay, deubiquitinase binding assay, acetylation assay (TRIM21 K351), SIRT5 KO macrophages, LPS stimulation model EMBO Reports Medium 35770730
2019 SIRT5 desuccinylates SDHA (succinate dehydrogenase subunit A), which demalonylates and inactivates SDHA, leading to accumulation of succinate. Succinate then binds and activates thioredoxin reductase 2 (TrxR2) to confer chemotherapy resistance in SIRT5+ colorectal cancer cells. Elevated succinate-to-αKG ratio also inhibits αKG-dependent dioxygenases to maintain cetuximab resistance. SIRT5 knockdown/overexpression, succinate measurement, TrxR2 activity assay, epistasis experiments with succinate pathway, CRC cell resistance assays Cell Reports Medium 29514096
2023 SIRT5 selectively reduces malonylation of histones, and KAT2A acts as a malonyltransferase for histones (KAT2A knockdown reduced histone malonylation). H2B_K5 is highly malonylated and regulated by SIRT5 in mouse brain and liver. Histone malonylation increases nucleolar area and ribosomal RNA expression. Mass spectrometry, siRNA knockdown of 22 KATs, SIRT5 KO, nucleolar area quantification, rRNA expression analysis iScience Medium 36879797
2021 SIRT5 is required for maintenance of histone acetylation and methylation levels in melanoma cells, thereby promoting proper gene expression including MITF and c-MYC. SIRT5 loss impairs these epigenetic marks independent of direct histone deacylation. SIRT5 KO in multiple melanoma cell lines, metabolite profiling, transcriptomic analysis, xenograft mouse model, autochthonous melanoma mouse model Journal of Clinical Investigation Medium 33945506
2022 SIRT5 deglutarylates GCDH (glutaryl-CoA dehydrogenase), restoring its enzymatic activity. Glutarylation of GCDH decreases lysine oxidation; SIRT5 deglutarylation relieves this inhibition, supporting a feedback loop within the lysine/tryptophan oxidation pathway. In vitro deglutarylation assay, GCDH enzymatic activity assay, metabolomics, SIRT5 KO mouse Journal of Biological Chemistry Medium 35157847
2024 SIRT5 desuccinylates TBK1 at K137, leading to TBK1 dephosphorylation and suppression of downstream inflammatory signaling. SIRT5 expression is reduced in aged primate skeletal muscles. Lentiviral SIRT5 gene therapy in mice enhances physical performance and alleviates age-related muscle dysfunction. Co-immunoprecipitation, in vitro desuccinylation assay, site-directed mutagenesis (K137), TBK1 phosphorylation assay, SIRT5 KO in human myotubes, lentiviral gene therapy in mice Nature Metabolism High 40087407
2024 SIRT5 desuccinylates TBK1 at K38, K154, and K692. In endotoxemia/sepsis models, reduced SIRT5 in macrophages increases TBK1 succinylation, inhibiting TBK1 binding to IRF3 and TRAF2 and suppressing the NF-κB/IRF inflammatory response. Adoptive transfer of macrophages with succinylation-resistant TBK1-2KR (K154/692R) reversed cytokine suppression caused by SIRT5 deficiency. Mass spectrometry (succinylation site identification), Co-IP (TBK1-IRF3, TBK1-TRAF2), site-directed mutagenesis (K154/692R), adoptive macrophage transfer, SIRT5 KO mouse sepsis model Cell Reports High 39673708
2024 SIRT5 desuccinylates RAB7A at K31, maintaining RAB7A activity and autophagosome-lysosome fusion. Cd exposure reduces SIRT5 expression, increasing RAB7A K31 succinylation and inhibiting RAB7A activity, leading to autophagic flux blockade and APP accumulation. SIRT5 overexpression restores autophagic flux and reduces Aβ in Cd-exposed FAD4T mice. Proteomic analysis (IPA), Co-IP, in vitro desuccinylation, RAB7A activity assay, autophagy flux assay, SIRT5 OE in FAD4T mice Advanced Science Medium 38837686
2024 SIRT5 desuccinylates CPT2 (carnitine palmitoyltransferase 2) at K424. Succinylation of K424 inactivates CPT2 enzymatic activity, leading to accumulation of fatty acyl-carnitines and impaired fatty acid oxidation. CPT2 K424R mutation (reducing succinylation) counteracts SIRT5 deficiency-induced FAO impairment and lipid deposition in diabetic cardiomyopathy. Succinylomics proteomics, Co-IP, in vitro desuccinylation assay, site-directed mutagenesis (K424R), CPT2 enzymatic assay, SIRT5 KO mouse diabetic cardiomyopathy model Redox Biology High 38718533
2021 SIRT5 is required for proliferation and survival across cutaneous and uveal melanoma. SIRT5 loss disrupts histone acetylation and methylation, downregulating MITF and c-MYC expression. This demonstrates a metabolite-epigenetics link where SIRT5 controls chromatin dynamics in cancer cells. SIRT5 KO cell lines, xenograft mouse model, autochthonous Braf/Pten melanoma mouse model, metabolite profiling, transcriptomics Journal of Clinical Investigation Medium 33945506
2022 AKT2 inhibits PGC-1α to downregulate SIRT5; SIRT5 is identified as an AKT2 binding partner. SIRT5-AKT2 crosstalk facilitates TFEB-dependent lysosomal function in RPE cells. AKT2 overexpression causes a dry AMD-like phenotype in aging mice by impairing the AKT2/SIRT5/TFEB pathway. Co-immunoprecipitation (AKT2-SIRT5), SIRT5 KO/OE in RPE, AKT2 KI mouse model, lysosomal function assays, iPSC-derived RPE with CFH Y402H variant Nature Communications Medium 39034314
2023 SIRT5 desuccinylates AIFM1 (apoptosis-inducing factor mitochondria-associated 1); reduced SIRT5 leads to increased AIFM1 succinylation, abolishing the AIFM1-CHCHD4 interaction and reducing import of electron transport chain complex subunits into mitochondria, leading to mitochondrial dysfunction. IP-MS (interactome identification), Co-IP, succinylation assay, AIFM1-CHCHD4 interaction assay, ETC subunit quantification, SIRT5 KO mice Experimental & Molecular Medicine Medium 36653443
2019 SIRT5 deacetylates cytochrome c, and this deacetylation is proposed to regulate HCC cell apoptosis via the mitochondrial pathway. Co-IP, western blot for cytochrome c acetylation, SIRT5 KO/OE in HCC cell lines Journal of Cancer Low 31333804
2024 Set7/9 promotes binding of Cbx1 to H3K9me2/3 at the Sirt5 promoter, forming a transcription repressor complex that represses Sirt5 transcription. Reduced SIRT5 decreases deacetylation of glutaminase, promoting its expression and triggering glutamate/ammonia excitotoxicity in ischemic neurons. ChIP assay (Cbx1 at Sirt5 promoter), proteomic analysis, Set7/9 KD/KO in neurons, Sirt5-dependent rescue experiments Cell Death and Differentiation Medium 38365969
2023 Sodium butyrate activates HMGCS2 enzymatic activity through SIRT5-mediated desuccinylation at K221 and K358 to promote ketone body production in hepatocytes. This effect is significantly reduced by a SIRT5 inhibitor and in Sirt5 KO mice. Succinylomics proteomics (SB treatment), HMGCS2 activity assay, SIRT5 inhibitor pharmacological blockade, Sirt5 KO mice, blood BHB measurement Frontiers of Medicine Medium 36602721
2021 SIRT5 is identified as a key transcriptional target of ATF4 that promotes cancer cell survival during metabolic stress. SIRT5 protects glutaminase C (GAC) from degradation and supports glutamine metabolism. Ectopic SIRT5 expression compensates for ATF4 knockdown in cells under glutamine deprivation-induced stress. ATF4 KD with transcriptomic analysis, SIRT5 OE rescue of ATF4 KD, GLS/GAC stability assay, glutamine deprivation stress model Cell Death Discovery Medium 35963851
2019 SIRT5 promotes brown adipocyte differentiation and browning of subcutaneous white adipose tissue. SIRT5 knockdown reduces intracellular α-ketoglutarate concentration, leading to elevated H3K9me2 and H3K9me3 at promoters of Pparγ and Prdm16, inhibiting their transcription. SIRT5 KD/KO in preadipocytes and mice, α-ketoglutarate measurement, ChIP assay (H3K9me2/3 at Pparγ and Prdm16 promoters), cold tolerance test Diabetes Medium 31010955

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science (New York, N.Y.) 1150 22076378
2013 SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. Molecular cell 817 23806337
2014 Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. Cell metabolism 663 24703693
2009 SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 638 19410549
2013 SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks. Cell metabolism 604 24315375
2008 Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. Journal of molecular biology 448 18680753
2015 SIRT5 Regulates both Cytosolic and Mitochondrial Protein Malonylation with Glycolysis as a Major Target. Molecular cell 386 26073543
2016 Metabolomics-assisted proteomics identifies succinylation and SIRT5 as important regulators of cardiac function. Proceedings of the National Academy of Sciences of the United States of America 314 27051063
2017 SIRT5 Desuccinylates and Activates Pyruvate Kinase M2 to Block Macrophage IL-1β Production and to Prevent DSS-Induced Colitis in Mice. Cell reports 287 28614718
2015 SIRT5 regulation of ammonia-induced autophagy and mitophagy. Autophagy 283 25700560
2018 SIRT5 inhibits peroxisomal ACOX1 to prevent oxidative damage and is downregulated in liver cancer. EMBO reports 247 29491006
2016 SIRT5 promotes IDH2 desuccinylation and G6PD deglutarylation to enhance cellular antioxidant defense. EMBO reports 234 27113762
2013 SIRT5 desuccinylates and activates SOD1 to eliminate ROS. Biochemical and biophysical research communications 227 24140062
2018 Functions of the sirtuin deacylase SIRT5 in normal physiology and pathobiology. Critical reviews in biochemistry and molecular biology 211 29637793
2017 SHMT2 Desuccinylation by SIRT5 Drives Cancer Cell Proliferation. Cancer research 190 29180469
2022 Loss of SIRT5 promotes bile acid-induced immunosuppressive microenvironment and hepatocarcinogenesis. Journal of hepatology 138 35292350
2017 Desuccinylation of pyruvate kinase M2 by SIRT5 contributes to antioxidant response and tumor growth. Oncotarget 137 28036303
2014 SIRT5 facilitates cancer cell growth and drug resistance in non-small cell lung cancer. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 135 25070488
2015 SIRT3 and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase. PloS one 134 25811481
2024 Quercetin inhibits necroptosis in cardiomyocytes after ischemia-reperfusion via DNA-PKcs-SIRT5-orchestrated mitochondrial quality control. Phytotherapy research : PTR 120 38447978
2017 Emerging Roles for SIRT5 in Metabolism and Cancer. Antioxidants & redox signaling 117 28707979
2014 SIRT5 is under the control of PGC-1α and AMPK and is involved in regulation of mitochondrial energy metabolism. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 116 24687991
2019 SIRT5 stabilizes mitochondrial glutaminase and supports breast cancer tumorigenesis. Proceedings of the National Academy of Sciences of the United States of America 114 31843902
2021 Metabolic Rewiring by Loss of Sirt5 Promotes Kras-Induced Pancreatic Cancer Progression. Gastroenterology 113 34245764
2018 SIRT5-mediated deacetylation of LDHB promotes autophagy and tumorigenesis in colorectal cancer. Molecular oncology 112 30443978
2013 Metabolic characterization of a Sirt5 deficient mouse model. Scientific reports 110 24076663
2017 Lysine desuccinylase SIRT5 binds to cardiolipin and regulates the electron transport chain. The Journal of biological chemistry 98 28458255
2020 Desuccinylation-Triggered Peptide Self-Assembly: Live Cell Imaging of SIRT5 Activity and Mitochondrial Activity Modulation. Journal of the American Chemical Society 94 32991157
2019 SIRT5-mediated SDHA desuccinylation promotes clear cell renal cell carcinoma tumorigenesis. Free radical biology & medicine 94 30703481
2010 Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1. Biochemical and biophysical research communications 93 20097174
2024 Sirt5 improves cardiomyocytes fatty acid metabolism and ameliorates cardiac lipotoxicity in diabetic cardiomyopathy via CPT2 de-succinylation. Redox biology 75 38718533
2021 Pharmacological and genetic perturbation establish SIRT5 as a promising target in breast cancer. Oncogene 75 33479498
2025 Tanshinone IIA modulates Sirt5 and Metll3 interaction to govern mitochondria-endoplasmic reticulum unfolded protein response in coronary microvascular injury. Phytomedicine : international journal of phytotherapy and phytopharmacology 73 40543233
2017 SIRT5 promotes cell proliferation and invasion in hepatocellular carcinoma by targeting E2F1. Molecular medicine reports 69 29115436
2019 Sirt5 Attenuates Cisplatin-Induced Acute Kidney Injury through Regulation of Nrf2/HO-1 and Bcl-2. BioMed research international 68 31815138
2008 Alcohol alters hepatic FoxO1, p53, and mitochondrial SIRT5 deacetylation function. Biochemical and biophysical research communications 68 18555008
2020 SIRT5 impairs aggregation and activation of the signaling adaptor MAVS through catalyzing lysine desuccinylation. The EMBO journal 64 32301534
2009 Function and regulation of the mitochondrial sirtuin isoform Sirt5 in Mammalia. Biochimica et biophysica acta 64 19766741
2009 Urea cycle regulation by mitochondrial sirtuin, SIRT5. Aging 64 20157539
2018 CDK2 positively regulates aerobic glycolysis by suppressing SIRT5 in gastric cancer. Cancer science 62 29896817
2023 Quercetin inhibits DNA damage responses to induce apoptosis via SIRT5/PI3K/AKT pathway in non-small cell lung cancer. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 59 37390710
2023 SIRT5-related desuccinylation modification of AIFM1 protects against compression-induced intervertebral disc degeneration by regulating mitochondrial homeostasis. Experimental & molecular medicine 58 36653443
2023 Emerging Roles of SIRT5 in Metabolism, Cancer, and SARS-CoV-2 Infection. Cells 58 36980194
2018 SIRT5 deacylates metabolism-related proteins and attenuates hepatic steatosis in ob/ob mice. EBioMedicine 58 30279144
2025 Zishen Huoxue decoction (ZSHX) alleviates ischemic myocardial injury (MI) via Sirt5-β-tubulin mediated synergistic mechanism of "mitophagy-unfolded protein response" and mitophagy. Chinese journal of natural medicines 57 40122661
2019 SIRT5 IS A DRUGGABLE METABOLIC VULNERABILITY IN ACUTE MYELOID LEUKEMIA. Blood cancer discovery 57 34027418
2021 Repression of p53 function by SIRT5-mediated desuccinylation at Lysine 120 in response to DNA damage. Cell death and differentiation 55 34642466
2012 Inhibitors of the NAD(+)-Dependent Protein Desuccinylase and Demalonylase Sirt5. ACS medicinal chemistry letters 55 24900427
2019 SIRT5 deficiency suppresses mitochondrial ATP production and promotes AMPK activation in response to energy stress. PloS one 54 30759120
2023 SIRT5-mediated ME2 desuccinylation promotes cancer growth by enhancing mitochondrial respiration. Cell death and differentiation 52 38007551
2016 Protein Kinase C Epsilon Promotes Cerebral Ischemic Tolerance Via Modulation of Mitochondrial Sirt5. Scientific reports 52 27435822
2019 SIRT5 Regulates Brown Adipocyte Differentiation and Browning of Subcutaneous White Adipose Tissue. Diabetes 50 31010955
2021 SIRT5 Represses Neurotrophic Pathways and Aβ Production in Alzheimer's Disease by Targeting Autophagy. ACS chemical neuroscience 47 34788008
2017 SIRT5 and post-translational protein modifications: A potential therapeutic target for myocardial ischemia-reperfusion injury with regard to mitochondrial dynamics and oxidative metabolism. European journal of pharmacology 45 29154835
2024 SIRT5-Mediated Desuccinylation of RAB7A Protects Against Cadmium-Induced Alzheimer's Disease-Like Pathology by Restoring Autophagic Flux. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 44 38837686
2021 SIRT5 functions as a tumor suppressor in renal cell carcinoma by reversing the Warburg effect. Journal of translational medicine 44 34930316
2020 Citrate synthase desuccinylation by SIRT5 promotes colon cancer cell proliferation and migration. Biological chemistry 44 32284438
2019 OGDH mediates the inhibition of SIRT5 on cell proliferation and migration of gastric cancer. Experimental cell research 42 31247190
2019 SIRT5 Promotes Hepatocellular Carcinoma Progression by Regulating Mitochondrial Apoptosis. Journal of Cancer 42 31333804
2018 Targeting a Sirt5-Positive Subpopulation Overcomes Multidrug Resistance in Wild-Type Kras Colorectal Carcinomas. Cell reports 42 29514096
2024 SIRT5-related lysine demalonylation of GSTP1 contributes to cardiomyocyte pyroptosis suppression in diabetic cardiomyopathy. International journal of biological sciences 39 38169591
2022 Potent and Specific Activators for Mitochondrial Sirtuins Sirt3 and Sirt5. Journal of medicinal chemistry 39 36228194
2021 The deacylase SIRT5 supports melanoma viability by influencing chromatin dynamics. The Journal of clinical investigation 38 33945506
2018 Vimentin acetylation is involved in SIRT5-mediated hepatocellular carcinoma migration. American journal of cancer research 38 30662803
2019 SIRT5 inhibits bovine preadipocyte differentiation and lipid deposition by activating AMPK and repressing MAPK signal pathways. Genomics 37 31816429
2023 Histone malonylation is regulated by SIRT5 and KAT2A. iScience 33 36879797
2022 Aryl Fluorosulfate Based Inhibitors That Covalently Target the SIRT5 Lysine Deacylase. Angewandte Chemie (International ed. in English) 33 36130196
2022 SIRT5 is a proviral factor that interacts with SARS-CoV-2 Nsp14 protein. PLoS pathogens 32 36095012
2021 SIRT5 regulates autophagy and apoptosis in gastric cancer cells. The Journal of international medical research 32 33530803
2024 SIRT5 Regulates Ferroptosis through the Nrf2/HO-1 Signaling Axis to Participate in Ischemia-Reperfusion Injury in Ischemic Stroke. Neurochemical research 30 38170384
2024 The Role of Mitochondrial Sirtuins (SIRT3, SIRT4 and SIRT5) in Renal Cell Metabolism: Implication for Kidney Diseases. International journal of molecular sciences 29 39000044
2011 SIRT1 and SIRT5 activity expression and behavioral responses to calorie restriction. Journal of cellular biochemistry 29 21826711
2021 Sirt5 Deficiency Causes Posttranslational Protein Malonylation and Dysregulated Cellular Metabolism in Chondrocytes Under Obesity Conditions. Cartilage 28 33567897
2018 Metabolomics Based Identification of SIRT5 and Protein Kinase C Epsilon Regulated Pathways in Brain. Frontiers in neuroscience 28 29440987
2021 SIRT5 Inhibition Induces Brown Fat-Like Phenotype in 3T3-L1 Preadipocytes. Cells 27 34066961
2018 SIRT5 regulates pancreatic β-cell proliferation and insulin secretion in type 2 diabetes. Experimental and therapeutic medicine 27 30116390
2022 Investigation of Carboxylic Acid Isosteres and Prodrugs for Inhibition of the Human SIRT5 Lysine Deacylase Enzyme. Angewandte Chemie (International ed. in English) 26 35299278
2022 Functional skewing of TRIM21-SIRT5 interplay dictates IL-1β production in DSS-induced colitis. EMBO reports 26 35770730
2024 The AKT2/SIRT5/TFEB pathway as a potential therapeutic target in non-neovascular AMD. Nature communications 24 39034314
2025 SIRT5 safeguards against primate skeletal muscle ageing via desuccinylation of TBK1. Nature metabolism 23 40087407
2025 Ginsenoside Rb1 attenuates coronary microvascular inflammatory injury via NDUFS4-SIRT5-DUSP1-mediated mitochondrial quality control in a murine ischemia-reperfusion model. Journal of ginseng research 23 40843019
2022 SIRT5 Directly Inhibits the PI3K/AKT Pathway in Prostate Cancer Cell Lines. Cancer genomics & proteomics 23 34949659
2024 Desuccinylation of TBK1 by SIRT5 regulates inflammatory response of macrophages in sepsis. Cell reports 22 39673708
2018 Tissue distribution, subcellular localization, and enzymatic activity analysis of human SIRT5 isoforms. Biochemical and biophysical research communications 22 29932920
2023 Sodium butyrate activates HMGCS2 to promote ketone body production through SIRT5-mediated desuccinylation. Frontiers of medicine 21 36602721
2023 SIRT5 Activation and Inorganic Phosphate Binding Reduce Cancer Cell Vitality by Modulating Autophagy/Mitophagy and ROS. Antioxidants (Basel, Switzerland) 21 37627630
2020 SIRT5 Contributes to Colorectal Cancer Growth by Regulating T Cell Activity. Journal of immunology research 21 32953892
2025 A novel ligustrazine-based nanodelivery system protects against doxorubicin-induced cardiotoxicity by targeting the SIRT5-DUSP1 axis for mitochondrial repair. Journal of nanobiotechnology 20 41088207
2022 SIRT5 is involved in the proliferation and metastasis of breast cancer by promoting aerobic glycolysis. Pathology, research and practice 20 35576836
2022 Insights on the Modulation of SIRT5 Activity: A Challenging Balance. Molecules (Basel, Switzerland) 20 35889322
2022 Elucidation of an mTORC2-PKC-NRF2 pathway that sustains the ATF4 stress response and identification of Sirt5 as a key ATF4 effector. Cell death discovery 20 35963851
2022 SIRT5 alleviates hepatic ischemia and reperfusion injury by diminishing oxidative stress and inflammation via elevating SOD1 and IDH2 expression. Experimental cell research 19 35995176
2024 Sirt5-mediated lysine desuccinylation regulates oxidative stress adaptation in Magnaporthe oryzae during host intracellular infection. The New phytologist 18 38481385
2022 Deglutarylation of glutaryl-CoA dehydrogenase by deacylating enzyme SIRT5 promotes lysine oxidation in mice. The Journal of biological chemistry 17 35157847
2022 Sirt5 Inhibits BmNPV Replication by Promoting a Relish-Mediated Antiviral Pathway in Bombyx mori. Frontiers in immunology 17 35693834
2021 Dysregulation of the Sirt5/IDH2 axis contributes to sunitinib resistance in human renal cancer cells. FEBS open bio 17 33455080
2020 LncRNA SNHG14 aggravates invasion and migration as ceRNA via regulating miR-656-3p/SIRT5 pathway in hepatocellular carcinoma. Molecular and cellular biochemistry 17 32607966
2006 DNA pooling: a comprehensive, multi-stage association analysis of ACSL6 and SIRT5 polymorphisms in schizophrenia. Genes, brain, and behavior 17 16827919
2024 Set7/9 aggravates ischemic brain injury via enhancing glutamine metabolism in a blocking Sirt5 manner. Cell death and differentiation 16 38365969
2023 Role of SIRT5 in cancer. Friend or Foe? Biochimie 16 36813074

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