메뉴 건너뛰기




Volumn 16, Issue 5-6, 2012, Pages 535-543

Sirtuins: NAD+-dependent deacetylase mechanism and regulation

Author keywords

[No Author keywords available]

Indexed keywords

2' O ACETYL ADENOSINE DIPHOSPHATE RIBOSE; ACETYL COENZYME A; ADENOSINE DIPHOSPHATE RIBOSE; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE DEPENDENT DEACETYLASE; PYRUVIC ACID; SIRTUIN; SUCCINYL COENZYME A; UNCLASSIFIED DRUG;

EID: 84872268055     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2012.10.003     Document Type: Review
Times cited : (76)

References (59)
  • 3
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 2006, 23:607-618.
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3    Xu, Y.4    Ball, H.5    Pei, J.6    Cheng, T.7    Kho, Y.8    Xiao, H.9    Xiao, L.10
  • 5
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability
    • Brachmann C.B., Sherman J.M., Devine S.E., Cameron E.E., Pillus L., Boeke J.D. The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev 1995, 9:2888-2902.
    • (1995) Genes Dev , vol.9 , pp. 2888-2902
    • Brachmann, C.B.1    Sherman, J.M.2    Devine, S.E.3    Cameron, E.E.4    Pillus, L.5    Boeke, J.D.6
  • 7
    • 69249235740 scopus 로고    scopus 로고
    • Calorie restriction and the exercise of chromatin
    • Vaquero A., Reinberg D. Calorie restriction and the exercise of chromatin. Genes Dev 2009, 23:1849-1869.
    • (2009) Genes Dev , vol.23 , pp. 1849-1869
    • Vaquero, A.1    Reinberg, D.2
  • 10
    • 79958206937 scopus 로고    scopus 로고
    • Franklin H. Epstein Lecture: sirtuins, aging, and medicine
    • Guarente L. Franklin H. Epstein Lecture: sirtuins, aging, and medicine. N Engl J Med 2011, 364:2235-2244.
    • (2011) N Engl J Med , vol.364 , pp. 2235-2244
    • Guarente, L.1
  • 11
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S., Armstrong C.M., Kaeberlein M., Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 2000, 403:795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 12
    • 0034735990 scopus 로고    scopus 로고
    • Role of NAD(+) in the deacetylase activity of the SIR2-like proteins
    • Landry J., Slama J.T., Sternglanz R. Role of NAD(+) in the deacetylase activity of the SIR2-like proteins. Biochem Biophys Res Commun 2000, 278:685-690.
    • (2000) Biochem Biophys Res Commun , vol.278 , pp. 685-690
    • Landry, J.1    Slama, J.T.2    Sternglanz, R.3
  • 13
    • 0035951072 scopus 로고    scopus 로고
    • Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions
    • Sauve A.A., Celic I., Avalos J., Deng H., Boeke J.D., Schramm V.L. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. Biochemistry 2001, 40:15456-15463.
    • (2001) Biochemistry , vol.40 , pp. 15456-15463
    • Sauve, A.A.1    Celic, I.2    Avalos, J.3    Deng, H.4    Boeke, J.D.5    Schramm, V.L.6
  • 14
    • 0034687694 scopus 로고    scopus 로고
    • Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose
    • Tanner K.G., Landry J., Sternglanz R., Denu J.M. Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci USA 2000, 97:14178-14182.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14178-14182
    • Tanner, K.G.1    Landry, J.2    Sternglanz, R.3    Denu, J.M.4
  • 15
    • 0037166269 scopus 로고    scopus 로고
    • Structural identification of 2'- and 3'-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta-NAD+-dependent histone/protein deacetylases
    • Jackson M.D., Denu J.M. Structural identification of 2'- and 3'-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta-NAD+-dependent histone/protein deacetylases. J Biol Chem 2002, 277:18535-18544.
    • (2002) J Biol Chem , vol.277 , pp. 18535-18544
    • Jackson, M.D.1    Denu, J.M.2
  • 16
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • Min J., Landry J., Sternglanz R., Xu R.M. Crystal structure of a SIR2 homolog-NAD complex. Cell 2001, 105:269-279.
    • (2001) Cell , vol.105 , pp. 269-279
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4
  • 17
    • 84981810839 scopus 로고
    • Carboxonium compounds in carbohydrate chemistry. 7. Valence isomerism in acyloxonium cations of 1,2,3-triols. Simple synthesis of acyloxonium salts
    • Paulsen H., Behre H. Carboxonium compounds in carbohydrate chemistry. 7. Valence isomerism in acyloxonium cations of 1,2,3-triols. Simple synthesis of acyloxonium salts. Angew Chem Int Ed 1969, 8. 886.
    • (1969) Angew Chem Int Ed , vol.8 , pp. 886
    • Paulsen, H.1    Behre, H.2
  • 18
    • 0033615721 scopus 로고    scopus 로고
    • Selective diesterification of diols through cyclic ketene acetal intermediates
    • Wu Z., Stanley R.R., Pittman C.U. Selective diesterification of diols through cyclic ketene acetal intermediates. J Org Chem 1999, 64:8386-8395.
    • (1999) J Org Chem , vol.64 , pp. 8386-8395
    • Wu, Z.1    Stanley, R.R.2    Pittman, C.U.3
  • 19
    • 0347623385 scopus 로고    scopus 로고
    • Mechanistic studies of the biomimetic epoxy ester-orthoester and orthoester-cyclic ether rearrangements
    • Giner J.L., Li X., Mullins J.J. Mechanistic studies of the biomimetic epoxy ester-orthoester and orthoester-cyclic ether rearrangements. J Org Chem 2003, 68:10079-10086.
    • (2003) J Org Chem , vol.68 , pp. 10079-10086
    • Giner, J.L.1    Li, X.2    Mullins, J.J.3
  • 20
    • 30144431571 scopus 로고    scopus 로고
    • Sir2 protein deacetylases: evidence for chemical intermediates and functions of a conserved histidine
    • Smith B.C., Denu J.M. Sir2 protein deacetylases: evidence for chemical intermediates and functions of a conserved histidine. Biochemistry 2006, 45:272-282.
    • (2006) Biochemistry , vol.45 , pp. 272-282
    • Smith, B.C.1    Denu, J.M.2
  • 21
    • 0041571570 scopus 로고    scopus 로고
    • Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry
    • Sauve A.A., Schramm V.L. Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry. Biochemistry 2003, 42:9249-9256.
    • (2003) Biochemistry , vol.42 , pp. 9249-9256
    • Sauve, A.A.1    Schramm, V.L.2
  • 22
    • 0346435109 scopus 로고    scopus 로고
    • Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases
    • Jackson M.D., Schmidt M.T., Oppenheimer N.J., Denu J.M. Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. J Biol Chem 2003, 278:50985-50998.
    • (2003) J Biol Chem , vol.278 , pp. 50985-50998
    • Jackson, M.D.1    Schmidt, M.T.2    Oppenheimer, N.J.3    Denu, J.M.4
  • 24
    • 0036009145 scopus 로고    scopus 로고
    • A view at the millennium: the efficiency of enzymatic catalysis
    • Bruice T.C. A view at the millennium: the efficiency of enzymatic catalysis. Acc Chem Res 2002, 35:139-148.
    • (2002) Acc Chem Res , vol.35 , pp. 139-148
    • Bruice, T.C.1
  • 25
    • 77953291365 scopus 로고    scopus 로고
    • Sirtuin chemical mechanisms
    • Sauve A.A. Sirtuin chemical mechanisms. Biochim Biophys Acta 2010, 1804:1591-1603.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1591-1603
    • Sauve, A.A.1
  • 26
    • 34248595983 scopus 로고    scopus 로고
    • Sir2 deacetylases exhibit nucleophilic participation of acetyl-lysine in NAD+ cleavage
    • Smith B.C., Denu J.M. Sir2 deacetylases exhibit nucleophilic participation of acetyl-lysine in NAD+ cleavage. J Am Chem Soc 2007, 129:5802-5803.
    • (2007) J Am Chem Soc , vol.129 , pp. 5802-5803
    • Smith, B.C.1    Denu, J.M.2
  • 27
    • 77953289094 scopus 로고    scopus 로고
    • Structural basis for sirtuin function: what we know and what we don't
    • Sanders B.D., Jackson B., Marmorstein R. Structural basis for sirtuin function: what we know and what we don't. Biochim Biophys Acta 2010, 1804:1604-1616.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1604-1616
    • Sanders, B.D.1    Jackson, B.2    Marmorstein, R.3
  • 28
    • 52249090638 scopus 로고    scopus 로고
    • Plasmodium falciparum Sir2 is an NAD+-dependent deacetylase and an acetyllysine-dependent and acetyllysine-independent NAD+ glycohydrolase
    • French J.B., Cen Y., Sauve A.A. Plasmodium falciparum Sir2 is an NAD+-dependent deacetylase and an acetyllysine-dependent and acetyllysine-independent NAD+ glycohydrolase. Biochemistry 2008, 47:10227-10239.
    • (2008) Biochemistry , vol.47 , pp. 10227-10239
    • French, J.B.1    Cen, Y.2    Sauve, A.A.3
  • 29
    • 84859973887 scopus 로고    scopus 로고
    • Insights into the mechanism of bovine CD38/NAD+glycohydrolase from the X-ray structures of its michaelis complex and covalently-trapped intermediates
    • Egea P.F., Muller-Steffner H., Kuhn I., Cakir-Kiefer C., Oppenheimer N.J., Stroud R.M., Kellenberger E., Schuber F. Insights into the mechanism of bovine CD38/NAD+glycohydrolase from the X-ray structures of its michaelis complex and covalently-trapped intermediates. PLoS ONE 2012, 7:e34918.
    • (2012) PLoS ONE , vol.7
    • Egea, P.F.1    Muller-Steffner, H.2    Kuhn, I.3    Cakir-Kiefer, C.4    Oppenheimer, N.J.5    Stroud, R.M.6    Kellenberger, E.7    Schuber, F.8
  • 30
    • 42649085059 scopus 로고    scopus 로고
    • Transition-state analysis of the DNA repair enzyme MutY
    • McCann J.A., Berti P.J. Transition-state analysis of the DNA repair enzyme MutY. J Am Chem Soc 2008, 130:5789-5797.
    • (2008) J Am Chem Soc , vol.130 , pp. 5789-5797
    • McCann, J.A.1    Berti, P.J.2
  • 31
    • 79959420922 scopus 로고    scopus 로고
    • Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes
    • Schramm V.L. Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes. Annu Rev Biochem 2011, 80:703-732.
    • (2011) Annu Rev Biochem , vol.80 , pp. 703-732
    • Schramm, V.L.1
  • 32
    • 57549110245 scopus 로고    scopus 로고
    • Highly dissociative and concerted mechanism for the nicotinamide cleavage reaction in Sir2Tm enzyme suggested by ab initio QM/MM molecular dynamics simulations
    • Hu P., Wang S., Zhang Y. Highly dissociative and concerted mechanism for the nicotinamide cleavage reaction in Sir2Tm enzyme suggested by ab initio QM/MM molecular dynamics simulations. J Am Chem Soc 2008, 130:16721-16728.
    • (2008) J Am Chem Soc , vol.130 , pp. 16721-16728
    • Hu, P.1    Wang, S.2    Zhang, Y.3
  • 33
    • 77956246695 scopus 로고    scopus 로고
    • Transition state of ADP-ribosylation of acetyllysine catalyzed by Archaeoglobus fulgidus Sir2 determined by kinetic isotope effects and computational approaches
    • Cen Y., Sauve A.A. Transition state of ADP-ribosylation of acetyllysine catalyzed by Archaeoglobus fulgidus Sir2 determined by kinetic isotope effects and computational approaches. J Am Chem Soc 2010, 132:12286-12298.
    • (2010) J Am Chem Soc , vol.132 , pp. 12286-12298
    • Cen, Y.1    Sauve, A.A.2
  • 35
    • 0000031580 scopus 로고
    • Dilute acid-catalyzed amide hydrolysis - efficiency of N-protonation mechanism
    • Williams A. Dilute acid-catalyzed amide hydrolysis - efficiency of N-protonation mechanism. J Am Chem Soc 1976, 98:5645-5651.
    • (1976) J Am Chem Soc , vol.98 , pp. 5645-5651
    • Williams, A.1
  • 36
    • 33746824192 scopus 로고    scopus 로고
    • Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction
    • Qin W., Yang T., Ho L., Zhao Z., Wang J., Chen L., Zhao W., Thiyagarajan M., MacGrogan D., Rodgers J.T., et al. Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction. J Biol Chem 2006, 281:21745-21754.
    • (2006) J Biol Chem , vol.281 , pp. 21745-21754
    • Qin, W.1    Yang, T.2    Ho, L.3    Zhao, Z.4    Wang, J.5    Chen, L.6    Zhao, W.7    Thiyagarajan, M.8    MacGrogan, D.9    Rodgers, J.T.10
  • 37
    • 13944258164 scopus 로고    scopus 로고
    • Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition
    • Sauve A.A., Moir R.D., Schramm V.L., Willis I.M. Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition. Mol Cell 2005, 17:595-601.
    • (2005) Mol Cell , vol.17 , pp. 595-601
    • Sauve, A.A.1    Moir, R.D.2    Schramm, V.L.3    Willis, I.M.4
  • 38
    • 84862292333 scopus 로고    scopus 로고
    • Isonicotinamide enhances Sir2 protein-mediated silencing and longevity in yeast by raising intracellular NAD+ concentration
    • McClure J.M., Wierman M.B., Maqani N., Smith J.S. Isonicotinamide enhances Sir2 protein-mediated silencing and longevity in yeast by raising intracellular NAD+ concentration. J Biol Chem 2012, 287:20957-20966.
    • (2012) J Biol Chem , vol.287 , pp. 20957-20966
    • McClure, J.M.1    Wierman, M.B.2    Maqani, N.3    Smith, J.S.4
  • 39
    • 0038329323 scopus 로고    scopus 로고
    • Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • Anderson R.M., Bitterman K.J., Wood J.G., Medvedik O., Sinclair D.A. Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature 2003, 423:181-185.
    • (2003) Nature , vol.423 , pp. 181-185
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3    Medvedik, O.4    Sinclair, D.A.5
  • 40
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman K.J., Anderson R.M., Cohen H.Y., Latorre-Esteves M., Sinclair D.A. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem 2002, 277:45099-45107.
    • (2002) J Biol Chem , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 41
    • 53849121583 scopus 로고    scopus 로고
    • Mechanistic insights into glycosidase chemistry
    • Vocadlo D.J., Davies G.J. Mechanistic insights into glycosidase chemistry. Curr Opin Chem Biol 2008, 12:539-555.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 539-555
    • Vocadlo, D.J.1    Davies, G.J.2
  • 43
    • 61849111654 scopus 로고    scopus 로고
    • New principles for glycoside-bond formation
    • Zhu X., Schmidt R.R. New principles for glycoside-bond formation. Angew Chem Int Ed Engl 2009, 48:1900-1934.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 1900-1934
    • Zhu, X.1    Schmidt, R.R.2
  • 44
    • 33746484522 scopus 로고    scopus 로고
    • N-epsilon-thioacetyl-lysine: a multi-facet functional probe for enzymatic protein lysine N-epsilon-deacetylation
    • Fatkins D.G., Monnot A.D., Zheng W.P. N-epsilon-thioacetyl-lysine: a multi-facet functional probe for enzymatic protein lysine N-epsilon-deacetylation. Bioorg Med Chem Lett 2006, 16:3651-3656.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 3651-3656
    • Fatkins, D.G.1    Monnot, A.D.2    Zheng, W.P.3
  • 46
    • 37349110743 scopus 로고    scopus 로고
    • Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide
    • Smith B.C., Denu J.M. Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide. Biochemistry 2007, 46:14478-14486.
    • (2007) Biochemistry , vol.46 , pp. 14478-14486
    • Smith, B.C.1    Denu, J.M.2
  • 47
    • 39349113616 scopus 로고    scopus 로고
    • Substituting N(epsilon)-thioacetyl-lysine for N(epsilon)-acetyl-lysine in peptide substrates as a general approach to inhibiting human NAD(+)-dependent protein deacetylases
    • Fatkins D.G., Zheng W. Substituting N(epsilon)-thioacetyl-lysine for N(epsilon)-acetyl-lysine in peptide substrates as a general approach to inhibiting human NAD(+)-dependent protein deacetylases. Int J Mol Sci 2008, 9:1-11.
    • (2008) Int J Mol Sci , vol.9 , pp. 1-11
    • Fatkins, D.G.1    Zheng, W.2
  • 50
    • 69949102163 scopus 로고    scopus 로고
    • Identification of a cell-active non-peptide sirtuin inhibitor containing N-thioacetyl lysine
    • Suzuki T., Asaba T., Imai E., Tsumoto H., Nakagawa H., Miyata N. Identification of a cell-active non-peptide sirtuin inhibitor containing N-thioacetyl lysine. Bioorg Med Chem Lett 2009, 19:5670-5672.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 5670-5672
    • Suzuki, T.1    Asaba, T.2    Imai, E.3    Tsumoto, H.4    Nakagawa, H.5    Miyata, N.6
  • 51
    • 78650107007 scopus 로고    scopus 로고
    • Discovery of potent, proteolytically stable, and cell permeable human sirtuin peptidomimetic inhibitors containing N-epsilon-thioacetyl-lysine
    • Hirsch B.M., Gallo C.A., Du Z.W., Wang Z.H., Zheng W.P. Discovery of potent, proteolytically stable, and cell permeable human sirtuin peptidomimetic inhibitors containing N-epsilon-thioacetyl-lysine. Medchemcomm 2010, 1:233-238.
    • (2010) Medchemcomm , vol.1 , pp. 233-238
    • Hirsch, B.M.1    Gallo, C.A.2    Du, Z.W.3    Wang, Z.H.4    Zheng, W.P.5
  • 54
    • 84862573534 scopus 로고    scopus 로고
    • Protein lysine acylation and cysteine succination by intermediates of energy metabolism
    • Lin H., Su X., He B. Protein lysine acylation and cysteine succination by intermediates of energy metabolism. ACS Chem Biol 2012, 7:947-960.
    • (2012) ACS Chem Biol , vol.7 , pp. 947-960
    • Lin, H.1    Su, X.2    He, B.3
  • 55
    • 84862907582 scopus 로고    scopus 로고
    • Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine
    • Zhu A.Y., Zhou Y., Khan S., Deitsch K.W., Hao Q., Lin H. Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine. ACS Chem Biol 2011, 7:155-159.
    • (2011) ACS Chem Biol , vol.7 , pp. 155-159
    • Zhu, A.Y.1    Zhou, Y.2    Khan, S.3    Deitsch, K.W.4    Hao, Q.5    Lin, H.6
  • 58
    • 84863010942 scopus 로고    scopus 로고
    • Thiosuccinyl peptides as Sirt5-specific inhibitors
    • He B., Du J., Lin H. Thiosuccinyl peptides as Sirt5-specific inhibitors. J Am Chem Soc 2012, 134:1922-1925.
    • (2012) J Am Chem Soc , vol.134 , pp. 1922-1925
    • He, B.1    Du, J.2    Lin, H.3
  • 59
    • 84865225339 scopus 로고    scopus 로고
    • The bicyclic intermediate structure provides insights into the desuccinylation mechanism of human sirtuin 5 (SIRT5)
    • Zhou Y., Zhang H., He B., Du J., Lin H., Cerione R.A., Hao Q. The bicyclic intermediate structure provides insights into the desuccinylation mechanism of human sirtuin 5 (SIRT5). J Biol Chem 2012, 287:28307-28314.
    • (2012) J Biol Chem , vol.287 , pp. 28307-28314
    • Zhou, Y.1    Zhang, H.2    He, B.3    Du, J.4    Lin, H.5    Cerione, R.A.6    Hao, Q.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.