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Lysine Glutarylation Is a Protein Posttranslational Modification Regulated by SIRT5
Open accessAbstract
We report the identification and characterization of a five-carbon protein posttranslational modification (PTM) called lysine glutarylation (Kglu). This protein modification was detected by immunoblot and mass spectrometry (MS), and then comprehensively validated by chemical and biochemical methods. We demonstrated that the previously annotated deacetylase, sirtuin 5 (SIRT5), is a lysine deglutarylase. Proteome-wide analysis identified 683 Kglu sites in 191 proteins and showed that Kglu is highly enriched on metabolic enzymes and mitochondrial proteins. We validated carbamoyl phosphate synthase 1 (CPS1), the rate-limiting enzyme in urea cycle, as a glutarylated protein and demonstrated that CPS1 is targeted by SIRT5 for deglutarylation. We further showed that glutarylation suppresses CPS1 enzymatic activity in cell lines, mice, and a model of glutaric acidemia type I disease, the last of which has elevated glutaric acid and glutaryl-CoA. This study expands the landscape of lysine acyl modifications and increases our understanding of the deacylase SIRT5.
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“This work resulted in the identification of novel modifications targeted by SIRT5: succinylation, malonylation and glutarylation as described in details below ((Du et al. 2011{Zhang, 2011 #16);(Peng et al. 2011);(Tan et al. 2014)}.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“SIRT5 positively regulates CPS1 activity by mediating desuccinylation, deglutarylation and possibly by deacetylation across multiple sites ((Du et al. 2011))((Tan et al. 2014))((Nakagawa et al. 2009)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Mice lacking SIRT5 fail to upregulate CPS1 activity and show elevated blood ammonia under these conditions ((Nakagawa et al. 2009))((Tan et al. 2014)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Moreover, HMGCS2 is also subject to glutarylation and malonylation ((Tan et al. 2014))((Nishida et al. 2015)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Interestingly, lysine 88 is also a target of succinylation and glutarylation ((Rardin, He, et al. 2013))((Tan et al. 2014)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Both MnSOD and the various mitochondrial superoxide sources are acylated ((Rardin, Newman, et al. 2013), (Rardin, He, et al. 2013);(Tan et al. 2014)); MnSOD also carries glutarylation, succinylation, and acetylation at functionally required lysine residues near its active site, K122 in particular bears all three modifications ((Tao et al. 2010)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Mass-spectrometry data has shown that there are an abundance of histone crotonylation sites in all four core histones22,40.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [40]
In the citing paper
“For example, SIRT5 exhibits efficient activity to lysine desuccinylation, demalonylation and glutarylation12-14”
From HDAC8 catalyzes the hydrolysis of long chain fatty acyl lysine (2016) · cites this paper as [14]
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Citations
Cites
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MethodThe metabolic and molecular bases of inherited disease
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“SIRT5 is specific for negatively charged acyl groups, especially succinyl, malonyl, and glutaryl groups (360, 366).”
BackgroundMetabolic intermediates – Cellular messengers talking to chromatin modifiers
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“…and enzymatic processes including mitochondrial functions and metabolic processes including amino acid metabolism, fatty acid metabolism, co-enzyme metabolism, mitochondrial metabolism and cellular respiration (Hirschey & Zhao, 2015; Tan et al., 2014) in eukaryotic and prokaryotic cells.”
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“2-hydroxyisobutyrylation (Khib) [25], and glutarylation (Kglu) [26].”
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Self-citationAGO2 Protects Against Diabetic Cardiomyopathy by Activating Mitochondrial Gene Translation
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BackgroundA Novel Continuous Assay for the Deacylase Sirtuin 5 and Other Deacetylases
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“3 Succinylation has been shown to occur in the active site of homoserine trans-succinylase, although a succinyl group was transferred from succinyl-CoA to homoserine in the intermediate reaction.”
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“Sirt5 has robust lysine desuccinylase, demalonylase [80,81] and deglutarylase [82] activities.”
BackgroundDetecting Succinylation sites from protein sequences using ensemble support vector machine
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“Proteomic investigations have demonstrated that the loss of Sirt5 drives the upregulation of succinylated, malonylated, and glutarylated proteins in multiple cellular compartments (Nishida et al., 2015; Park et al., 2013; Rardin et al., 2013; Tan et al., 2014).”
BackgroundThe Function and related Diseases of Protein Crotonylation
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“last ten years, a variety of histone acylation modifications have been discovered, including histone propionylation (Kpr) [2], butyrylation (Kbu) [2], 2-hydroxyisobutylacylation (Khib) [3], succinylation (Ksucc) [4], malonylation (Kma) [4], glutarylation (Kglu) [5], crotonylation (Kcr) [6],”
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Self-citationOverview of SIRT5 as a potential therapeutic target: Structure, function and inhibitors
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Aryl Fluorosulfate Based Inhibitors That Covalently Target the SIRT5 Lysine Deacylase**
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SIRT3 controls brown fat thermogenesis by deacetylation regulation of pathways upstream of UCP1
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“However, desuccinylation is known to be catalyzed by NAD+-dependent mitochondrial desuccinylase, sirtuin 5 (SIRT5), which also possesses other deacylation activities [64,140,141].”
BackgroundDeacylation Mechanism by SIRT2 Revealed in the 1′-SH-2′-O-Myristoyl Intermediate Structure
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“nylation (7), malonylation (8, 9), glutarylation (10), 2-hydroxy-”
Self-citationSirtuin-4 (SIRT4), a therapeutic target with oncogenic and tumor-suppressive activity in cancer
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“6 For example, SIRT1–3 and SIRT7 are primarily lysine deacetylases, 7,8 SIRT4 serves as both an ADP-ribosyl-transferase and lysine deacylase, 9,10 SIRT5 serves as a lysine demalonylase, 11 desuccinylase, 12 and deglutarylase, 13 and SIRT6 is an ADP-ribose transferase and deacetylase.”
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Self-citationThe mechanisms, regulations, and functions of histone lysine crotonylation
Xie, J., Ju, J., Zhou, P., Chen, H., Wang, S., Wang, K., Wang, T., Chen, Y.-C., Chen, Y.-C., & Wang, K. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01830-w · Cited by 55
Self-citationde Moura, M. B., Uppala, R., Zhang, Y., Houten, B. V., & Goetzman, E. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106028 · Cited by 51
Self-citationClinical and therapeutic significance of sirtuin-4 expression in colorectal cancer
Huang, G., Cheng, J., Yu, F., Liu, X., Yuan, C., Liu, C., Chen, X.-L., & Peng, Z. (2016) · Oncology Reports · doi:10.3892/or.2016.4685 · Cited by 52
Epigenetic Regulation of Metabolism and Inflammation by Calorie Restriction
Hernández‐Saavedra, D., Moody, L., Xu, G. B., Chen, H., & Pan, Y. (2018) · Advances in Nutrition · doi:10.1093/advances/nmy129 · Cited by 52
Self-citationOrganic acidurias: Major gaps, new challenges, and a yet unfulfilled promise
Dimitrov, B., Molema, F., Williams, M., Schmiesing, J., Mühlhausen, C., Baumgartner, M. R., Schumann, A., & Kölker, S. (2020) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12254 · Cited by 51
“In line with these assumptions, Gcdh mice revealed markedly increased global protein glutarylation already under standard conditions.(81) Among them, hyperglutarylated carbamylphosphate synthetase 1 (EC 6.”
BackgroundSelf-citationNRF2 mediates melanoma addiction to GCDH by modulating apoptotic signalling
Verma, S. K., Crawford, D., Khateb, A., Feng, Y., Sergienko, E. A., Pathria, G., Ma, C.-T., Olson, S. H., Scott, D. A., Murad, R., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00985-x · Cited by 49
Zhu, D., Liang, H., Du, Z., Liu, Q., Li, G., Zhang, W., Wu, D., Zhou, X., Song, Y., & Cao, Y. (2024) · Research · doi:10.34133/research.0350 · Cited by 54
“SIRT5 selectively focuses on modifications other than lysine acetylation, including malonylation [94], succinylation [95], and glutarylation [96].”
BackgroundWang, X., Luo, X., Xiao, R., Liu, X., Zhou, F., Jiang, D., Bai, J., Cui, M., You, L., & Yupei, Z. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02334-4 · Cited by 59
Comparison of the Deacylase and Deacetylase Activity of Zinc-Dependent HDACs
McClure, J. J., Inks, E. S., Zhang, C., Peterson, Y. K., Li, J., Chundru, K. J., Lee, B., Buchanan, A., Miao, S., & Chou, C. J. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00321 · Cited by 52
Potent and Specific Activators for Mitochondrial Sirtuins Sirt3 and Sirt5
Suenkel, B., Valente, S., Zwergel, C., Weiss, S., Bello, E. D., Fioravanti, R., Aventaggiato, M., Amorim, J. A., Garg, N., Kumar, S., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01215 · Cited by 49
Self-citationSirtuins and their influence on autophagy
Baeken, M. W. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30377 · Cited by 52
“5,74 A previous investigation revealed that SIRT5 activity might influence autophagic, or rather mitophagic, processes.”
Natural and Synthetic Macrocyclic Inhibitors of the Histone Deacetylase Enzymes
Maolanon, A. R., Kristensen, H. M. E., Leman, L. J., Ghadiri, M. R., & Olsen, C. A. (2016) · ChemBioChem · doi:10.1002/cbic.201600519 · Cited by 49
Self-citationBiagosch, C., Ediga, R. D., Hensler, S.-V., Faerberboeck, M., Kuehn, R., Wurst, W., Meitinger, T., Kölker, S., Sauer, S. W., & Prokisch, H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.05.018 · Cited by 51
Pathways of Non-enzymatic Lysine Acylation
Baldensperger, T., & Glomb, M. A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.664553 · Cited by 47
“…of lysine modifications are acidic acylations (Figure 1) by malonylation (Peng et al., 2011), succinylation (Zhang et al., 2011), glutarylation (Tan et al., 2014), 3-hydroxy-3-methylglutarylation, 3-methylglutaconylation (Wagner et al., 2017), and 3-methylglutarylation (Anderson et al., 2017).”
BackgroundSIRT5 functions as a tumor suppressor in renal cell carcinoma by reversing the Warburg effect
Liu, Y., Xiaojing, W., Liu, A., Chuanjie, Z., Wang, H., Shen, Y., & He, H. (2021) · Journal of Translational Medicine · doi:10.1186/s12967-021-03178-6 · Cited by 49
“Eukaryotic cells evolved hierarchical regulatory strategies through posttranslational modification, such as phosphorylation [16], acetylation [16, 21], succinylation [17, 18, 22, 24], glutarylation [26], malonylation [19, 27], and aminoacylation [28].”
BackgroundEmerging Roles of SIRT3 in Cardiac Metabolism
Murugasamy, K., Munjal, A., & Sundaresan, N. R. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.850340 · Cited by 48
Characterization of Trypanosoma cruzi Sirtuins as Possible Drug Targets for Chagas Disease
Moretti, N. S., Augusto, L. D. S., Clemente, T. M., Antunes, R. P. P., Yoshida, N., Torrecilhas, A. C., Cano, M. I. N., & Schenkman, S. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.04694-14 · Cited by 48
Signalling functions of coenzyme A and its derivatives in mammalian cells
Davaapil, H., Tsuchiya, Y., & Gout, I. T. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140146 · Cited by 49
Sun, M., Xu, J., Wu, Z., Zhai, L., Liu, C., Cheng, Z., Xu, G., Tao, S., Ye, B., Zhao, Y., et al. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00798 · Cited by 49
Self-citationWan, L., Zhou, J., Gu, Y., Chen, Y., Huang, Y., Yang, J., Zhu, X., Zhao, K., Yan, Q., Zhao, Z., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2409132121 · Cited by 49
Self-citationWu, T., Zhao, Y., Zhang, X., Wang, Y., Chen, Q., Zhang, M., Sheng, H., Zhang, Y., Guo, J., Li, J., et al. (2025) · 癌症：英文版 · doi:10.1002/cac2.70048 · Cited by 50
“…derived short-chain acylation modifications (with acyl groups containing fewer than six carbon atoms) [6], including butyrylation [7], succinylation [8], crotonylation [9], mal-onylation [10], glutarylation [11], 2-hydroxyisobutyrylation [12], β -hydroxybutyrylation [13], and lactylation [14].”
Self-citationMitochondrial sirtuins in the heart
Bugger, H., Witt, C. N., & Bode, C. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9570-7 · Cited by 47
Hershberger, K. A., Abraham, D., Liu, J., Locasale, J. W., Grimsrud, P. A., & Hirschey, M. D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002187 · Cited by 46
“Sirtuin 5 (SIRT5) is an NAD -dependent demalonylase (1, 2), desuccinylase (2), and deglutarylase (3) that resides primarily in mitochondria.”
BackgroundSelf-citationSirtuins and Their Implications in Neurodegenerative Diseases from a Drug Discovery Perspective
Yeong, K. Y., Berdigaliyev, N., & Chang, Y. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00696 · Cited by 46
The deacylase SIRT5 supports melanoma viability by influencing chromatin dynamics
Giblin, W., Bringman, L. R., Guo, A. H., Kumar, S., Monovich, A. C., Mostafa, A. M., Skinner, M. E., Azar, M., Mady, A. S. A., Chung, C. H., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci138926 · Cited by 47
Self-citationRoles of sirtuin family members in chronic obstructive pulmonary disease
Zhang, X.-Y., Li, W., Zhang, J., Li, C., Zhang, J., & Lv, X. (2022) · Respiratory Research · doi:10.1186/s12931-022-01986-y · Cited by 50
“In addition, because of its ability to modify the negatively charged acyl group, the protein can be desuccinylated, deacylated, and deglutarated [87, 88].”
BackgroundMeng, X., Mujahid, H., Zhang, Y., Peng, X., Redoña, E. D., Wang, C., & Peng, Z. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001426 · Cited by 46
“Certain lysine acylation regulatory enzymes could have influences on various lysine acylation categories in a comparable manner (1, 8, 12, 50, 51).”
BackgroundSelf-citationGoetzman, E. S., Bharathi, S. S., Zhang, Y., Zhao, X., Dobrowolski, S. F., Peasley, K., Sims‐Lucas, S., & Monga, S. P. (2020) · Scientific Reports · doi:10.1038/s41598-020-75615-3 · Cited by 46
Self-citationPost-translational modifications on mitochondrial metabolic enzymes in cancer
Peng, Y., Liu, H., Liu, J., & Long, J. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.12.264 · Cited by 49
Deciphering functional roles of protein succinylation and glutarylation using genetic code expansion
Weyh, M., Jokisch, M., Nguyen, T., Fottner, M., & Lang, K. (2024) · Nature Chemistry · doi:10.1038/s41557-024-01500-5 · Cited by 49
“Interestingly, the GAPDH-K194GluK variant showed a four-to five-fold reduction in both V max and K m , indicating that, indeed, glutarylation of this lysine residue impacts enzymatic activity.”
BackgroundInfluentialRumpf, T., Gerhardt, S., Einsle, O., & Jung, M. (2015) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x15019986 · Cited by 44
“…proteins containing succinylated, malonylated and glutarylated lysines, while the isotypes Sirt1, Sirt2, Sirt3 and Sirt6 preferentially cleave off fatty-acid moieties from the "-amino group of lysines (Du et al., 2011; Bao et al., 2014; Tan et al., 2014; Liu et al., 2015; Teng et al., 2015).”
BackgroundHong, J., Mei, C., Raza, S. H. A., Khan, R., Cheng, G., & Zan, L. (2019) · Genomics · doi:10.1016/j.ygeno.2019.12.004 · Cited by 45
Hatchwell, L., Harney, D., Cielesh, M., Young, K., Koay, Y. C., O’Sullivan, J., & Larance, M. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.051 · Cited by 41
Glutamine Metabolism: Molecular Regulation, Biological Functions, and Diseases
Kumar, M. A., Baba, S. K., Khan, I. R., Khan, M. S., Husain, F. M., Ahmad, S., Haris, M., Singh, M., Akil, A. A., Macha, M. A., et al. (2025) · MedComm · doi:10.1002/mco2.70120 · Cited by 52
Defining the Orphan Functions of Lysine Acetyltransferases
Montgomery, D. C., Sorum, A. W., & Meier, J. L. (2015) · ACS Chemical Biology · doi:10.1021/cb500853p · Cited by 44
Global Proteomics Analysis of Protein Lysine Methylation
Cao, X., & Garcia, B. A. (2016) · Current Protocols in Protein Science · doi:10.1002/cpps.16 · Cited by 44
“By means of this strategy, hundreds to thousands of protein lysine acetylation, ubiquitylation, and other PTM sites have been identified (Choudhary et al., 2009; Kim et al., 2011; Lundby et al., 2012; Tan et al., 2014).”
BackgroundRole of Sirtuins in Tumor Angiogenesis
Edatt, L., Poyyakkara, A., Raji, G. R., Ramachandran, V., Shankar, S. S., & Kumar, V. B. S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2019.01516 · Cited by 43
“In contrast to other KDACs, whose only function include deacetylation (31), sirtuins can also remove other groups like glutaryl (32), crotonyl (33), succinyl (34), palmitoyl (35), and myristoyl (36) groups.”
BackgroundSirtuins: To Be or Not To Be in Diabetic Cardiomyopathy
Palomer, X., Aguilar-Recarte, D., García, R., Nistal, J. F., & Vázquez‐Carrera, M. (2021) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2021.03.004 · Cited by 44
Site-Specific Identification of Lysine Acetylation Stoichiometries in Mammalian Cells
Zhou, T., Chung, Y., Chen, J., & Chen, Y. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b01097 · Cited by 41
Self-citationXu, J., Xu, Z., Zhou, Y. Q., & Ye, B. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00131 · Cited by 43
Establishment of Dimethyl Labeling-based Quantitative Acetylproteomics in Arabidopsis
Liu, S., Yu, F., Yang, Z., Wang, T., Xiong, H., Chang, C., Yu, W., & Li, N. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra117.000530 · Cited by 41
“-hydroxybutyrylation (119), glutarylation sites (120), etc.”
Ammonia and autophagy: An emerging relationship with implications for disorders with hyperammonemia
Soria, L. R., & Brunetti‐Pierri, N. (2019) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12061 · Cited by 43
Metadata
- Authors
- Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., Ro, J., Wagner, G. R., Green, M. F., Madsen, A. S., Schmiesing, J., Peterson, B. S., Xu, G., Ilkayeva, O. R., Muehlbauer, M. J., Braulke, T., Mühlhausen, C., Backos, D. S., Olsen, C. A., McGuire, P. J., Pletcher, S. D., Lombard, D. B., Hirschey, M. D., & Zhao, Y.
- Affiliations
- Chinese Academy of Sciences (CN)
- University of Chicago (US)
- Duke University (US)
- University of Michigan (US)
- Technical University of Denmark (DK)
- University Medical Center Hamburg-Eppendorf (DE)
- University of Colorado Anschutz (US)
- National Institutes of Health (US)
- Corresponding author
- Hirschey, Matthew D.
- Zhao, Yingming
- ORCID
- Tan, Minjia
- Peng, Chao
- Chhoy, Peter
- Xie, Zhongyu
- Dai, Lunzhi
- Huang, He
- Zhang, Yi
- Ro, Jennifer
- Green, Michelle F.
- Madsen, Andreas S.
- Xu, Guofeng
- Ilkayeva, Olga R.
- Muehlbauer, Michael J.
- Braulke, Thomas
- Mühlhausen, Chris
- Backos, Donald S.
- Olsen, Christian A.
- McGuire, Peter J.
- Pletcher, Scott D.
- Lombard, David B.
- Hirschey, Matthew D.
- Zhao, Yingming
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2014-04
- Volume
- 19
- Issue
- 4
- Pages
- 605-617
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4108075
- OpenAlex
- W2088511656
- Cited by
- 844
- References
- 45
- Citations by year
- 2026: 49 · 2025: 63 · 2024: 86 · 2023: 50 · 2022: 79 · 2021: 106 · 2020: 67 · 2019: 74 · 2018: 80 · 2017: 53 · 2016: 70 · 2015: 50 · 2014: 16
- FWCI
- 32.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU) (submittedVersion)
- Funders
- Lundbeckfonden (R52-2010-5054)
- National Institutes of Health (UL1TR000430)
- National Institute on Alcohol Abuse and Alcoholism (AA022146, R01AA022146)
- National Institute on Aging (F31AG047696, R01AG045351, AG045351, P30AG013283, T32AG000114)
- National Cancer Institute (R21CA177925, CA160036, CA059365-19, U24CA160036, T32CA059365, CA177925)
- National Institute of General Medical Sciences (GM105933, T32GM007105, GM101171, T32GM007315, R01GM101171, R01GM105933)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30DK096493, P30DK020572)
- National Center for Research Resources (RR020839, U54RR020839)
- National Center for Advancing Translational Sciences
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- SIRT5, protein posttranslational modification, urea cycle, glutaric aciduria type I, glutaryl-CoA, mitochondrial proteins, metabolic enzymes
- MeSH terms
- Acyl Coenzyme A, Animals, Carbamoyl-Phosphate Synthase (Ammonia), Lysine, Models, Biological, Protein Processing, Post-Translational, Mass Spectrometry, Immunoblotting, Molecular Structure, Sirtuins, Proteomics, Mice
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