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Volumn 8, Issue 1, 2012, Pages 72-77

A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase

Author keywords

[No Author keywords available]

Indexed keywords

CARBAMIC ACID DERIVATIVE; CARBONYL DERIVATIVE; CYSTEINE; GLYCOSYLTRANSFERASE; LYSINE; NUCLEOTIDE; O LINKED N ACETYLGLUCOSAMINE TRANSFERASE; PYROPHOSPHATE; SCAFFOLD PROTEIN; SUGAR; UNCLASSIFIED DRUG;

EID: 83655163673     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.711     Document Type: Article
Times cited : (90)

References (48)
  • 1
    • 0004106191 scopus 로고    scopus 로고
    • 2nd edn. Cold Spring Harbor Laboratory Press
    • Varki, A., et al. Essentials of Glycobiology 2nd edn. (Cold Spring Harbor Laboratory Press, 2009).
    • (2009) Essentials of Glycobiology
    • Varki, A.1
  • 2
  • 3
    • 77957201940 scopus 로고    scopus 로고
    • Glycosyltransferases and their assays
    • Wagner, G.K. & Pesnot, T. Glycosyltransferases and their assays. ChemBioChem 11, 1939-1949 (2010).
    • (2010) ChemBioChem , vol.11 , pp. 1939-1949
    • Wagner, G.K.1    Pesnot, T.2
  • 5
    • 77951298440 scopus 로고    scopus 로고
    • Structural and mechanistic basis for a new mode of glycosyltransferase inhibition
    • Pesnot, T., Jorgensen, R., Palcic, M.M. & Wagner, G.K. Structural and mechanistic basis for a new mode of glycosyltransferase inhibition. Nat. Chem. Biol. 6, 321-323 (2010).
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 321-323
    • Pesnot, T.1    Jorgensen, R.2    Palcic, M.M.3    Wagner, G.K.4
  • 6
    • 77952396239 scopus 로고    scopus 로고
    • UDP-(5F) -GlcNAc acts as a slow-binding inhibitor of MshA, a retaining glycosyltransferase
    • Frantom, P.A., Coward, J.K. & Blanchard, J.S. UDP-(5F)-GlcNAc acts as a slow-binding inhibitor of MshA, a retaining glycosyltransferase. J. Am. Chem. Soc. 132, 6626-6627 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6626-6627
    • Frantom, P.A.1    Coward, J.K.2    Blanchard, J.S.3
  • 8
    • 77950026621 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli glycosyltransferase MurG and Mycobacterium tuberculosis Gal transferase by uridine-linked transition state mimics
    • Trunkfield, A.E., Gurcha, S.S., Besra, G.S. & Bugg, T.D. Inhibition of Escherichia coli glycosyltransferase MurG and Mycobacterium tuberculosis Gal transferase by uridine-linked transition state mimics. Bioorg. Med. Chem. 18, 2651-2663 (2010).
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 2651-2663
    • Trunkfield, A.E.1    Gurcha, S.S.2    Besra, G.S.3    Bugg, T.D.4
  • 9
    • 63249100328 scopus 로고    scopus 로고
    • Bisubstrate analogues as glycosyltransferase inhibitors
    • Izumi, M., Yuasa, H. & Hashimoto, H. Bisubstrate analogues as glycosyltransferase inhibitors. Curr. Top. Med. Chem. 9, 87-105 (2009).
    • (2009) Curr. Top. Med. Chem. , vol.9 , pp. 87-105
    • Izumi, M.1    Yuasa, H.2    Hashimoto, H.3
  • 10
    • 6344244586 scopus 로고    scopus 로고
    • Asymmetric synthesis and affinity of potent sialyltransferase inhibitors based on transition-state analogues
    • DOI 10.1023/B:GLYC.0000045093.96413.62
    • Skropeta, D., Schworer, R., Haag, T. & Schmidt, R.R. Asymmetric synthesis and affinity of potent sialyltransferase inhibitors based on transition-state analogues. Glycoconj. J. 21, 205-219 (2004). (Pubitemid 39388739)
    • (2004) Glycoconjugate Journal , vol.21 , Issue.5 , pp. 205-219
    • Skropeta, D.1    Schworer, R.2    Haag, T.3    Schmidt, R.R.4
  • 11
    • 0030915738 scopus 로고    scopus 로고
    • A search for pyrophosphate mimics for the development of substrates and inhibitors of glycosyltransferases
    • DOI 10.1016/S0968-0896(97)00005-9, PII S0968089697000059
    • Wang, R., et al. A search for pyrophosphate mimics for the development of substrates and inhibitors of glycosyltransferases. Bioorg. Med. Chem. 5, 661-672 (1997). (Pubitemid 27199390)
    • (1997) Bioorganic and Medicinal Chemistry , vol.5 , Issue.4 , pp. 661-672
    • Wang, R.1    Steensma, D.H.2    Takaoka, Y.3    Yun, J.W.4    Kajimoto, T.5    Wong, C.-H.6
  • 12
    • 0041692300 scopus 로고    scopus 로고
    • Identification of active-site inhibitors of MurG using a generalizable, high-throughput glycosyltransferase screen
    • DOI 10.1021/ja036494s
    • Helm, J.S., Hu, Y., Chen, L., Gross, B. & Walker, S. Identification of active-site inhibitors of MurG using a generalizable, high-throughput glycosyltransferase screen. J. Am. Chem. Soc. 125, 11168-11169 (2003). (Pubitemid 37108032)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.37 , pp. 11168-11169
    • Helm, J.S.1    Hu, Y.2    Chen, L.3    Gross, B.4    Walker, S.5
  • 14
    • 79951855712 scopus 로고    scopus 로고
    • Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells
    • Gloster, T.M., et al. Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells. Nat. Chem. Biol. 7, 174-181 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 174-181
    • Gloster, T.M.1
  • 15
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
    • DOI 10.1038/nature05815, PII NATURE05815
    • Hart, G.W., Housley, M.P. & Slawson, C. Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 446, 1017-1022 (2007). (Pubitemid 46676063)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 16
    • 33644874204 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: Deciphering the "o-GlcNAc code"
    • re13
    • Love, D.C. & Hanover, J.A. The hexosamine signaling pathway: deciphering the O-GlcNAc code. Sci. STKE 2005, re13 (2005).
    • (2005) Sci. STKE 2005
    • Love, D.C.1    Hanover, J.A.2
  • 17
    • 79952747341 scopus 로고    scopus 로고
    • Metabolic cross-talk allows labeling of O-linked β-N- acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway
    • Boyce, M., et al. Metabolic cross-talk allows labeling of O-linked β-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway. Proc. Natl. Acad. Sci. USA 108, 3141-3146 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3141-3146
    • Boyce, M.1
  • 18
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol
    • Dong, D.L. & Hart, G.W. Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol. J. Biol. Chem. 269, 19321-19330 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 19321-19330
    • Dong, D.L.1    Hart, G.W.2
  • 19
    • 77949305110 scopus 로고    scopus 로고
    • Increasing O-GlcNAc levels: An overview of small-molecule inhibitors of O-GlcNAcase
    • Macauley, M.S. & Vocadlo, D.J. Increasing O-GlcNAc levels: an overview of small-molecule inhibitors of O-GlcNAcase. Biochim. Biophys. Acta 1800, 107-121 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 107-121
    • MacAuley, M.S.1    Vocadlo, D.J.2
  • 20
    • 77949295164 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine
    • Hanover, J.A., Krause, M.W. & Love, D.C. The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine. Biochim. Biophys. Acta 1800, 80-95 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 80-95
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 21
    • 72449187655 scopus 로고    scopus 로고
    • The intersections between O-GlcNAcylation and phosphorylation: Implications for multiple signaling pathways
    • Zeidan, Q. & Hart, G.W. The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways. J. Cell Sci. 123, 13-22 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 13-22
    • Zeidan, Q.1    Hart, G.W.2
  • 22
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • Hart, G.W., Slawson, C., Ramirez-Correa, G. & Lagerlof, O. Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu. Rev. Biochem. 80, 825-858 (2011).
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 23
    • 77953138098 scopus 로고    scopus 로고
    • Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation
    • Hu, P., Shimoji, S. & Hart, G.W. Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation. FEBS Lett. 584, 2526-2538 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 2526-2538
    • Hu, P.1    Shimoji, S.2    Hart, G.W.3
  • 24
    • 77956396629 scopus 로고    scopus 로고
    • O-GlcNAc signaling: A metabolic link between diabetes and cancer?
    • Slawson, C., Copeland, R.J. & Hart, G.W. O-GlcNAc signaling: a metabolic link between diabetes and cancer? Trends Biochem. Sci. 35, 547-555 (2010).
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 547-555
    • Slawson, C.1    Copeland, R.J.2    Hart, G.W.3
  • 28
    • 27744466783 scopus 로고    scopus 로고
    • Mechanism of carbamate inactivation of FAAH: Implications for the design of covalent inhibitors and in vivo functional probes for enzymes
    • DOI 10.1016/j.chembiol.2005.08.011, PII S107455210500267X
    • Alexander, J.P. & Cravatt, B.F. Mechanism of carbamate inactivation of FAAH: implications for the design of covalent inhibitors and in vivo functional probes for enzymes. Chem. Biol. 12, 1179-1187 (2005). (Pubitemid 41628253)
    • (2005) Chemistry and Biology , vol.12 , Issue.11 , pp. 1179-1187
    • Alexander, J.P.1    Cravatt, B.F.2
  • 29
    • 0033527739 scopus 로고    scopus 로고
    • Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
    • Kreppel, L.K. & Hart, G.W. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J. Biol. Chem. 274, 32015-32022 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32015-32022
    • Kreppel, L.K.1    Hart, G.W.2
  • 30
    • 0032538435 scopus 로고    scopus 로고
    • Cloning and expression of a novel, tissue specifically expressed member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family
    • DOI 10.1074/jbc.273.42.27749
    • Ten Hagen, K.G., et al. Cloning and expression of a novel, tissue specifically expressed member of the UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferase family. J. Biol. Chem. 273, 27749-27754 (1998). (Pubitemid 28500502)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.42 , pp. 27749-27754
    • Ten Hagen, K.G.1    Hagen, F.K.2    Balys, M.M.3    Beres, T.M.4    Van Wuyckhuyse, B.5    Tabak, L.A.6
  • 31
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus, M.B., Nam, Y., Jiang, J., Sliz, P. & Walker, S. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469, 564-567 (2011).
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 36
    • 38049168981 scopus 로고    scopus 로고
    • A convenient synthesis of the C-1-phosphonate analogue of UDP-GlcNAc and its evaluation as an inhibitor of O-linked GlcNAc transferase (OGT)
    • Hajduch, J., et al. A convenient synthesis of the C-1-phosphonate analogue of UDP-GlcNAc and its evaluation as an inhibitor of O-linked GlcNAc transferase (OGT). Carbohydr. Res. 343, 189-195 (2008).
    • (2008) Carbohydr. Res. , vol.343 , pp. 189-195
    • Hajduch, J.1
  • 37
    • 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. 12, 539-555 (2008).
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 539-555
    • Vocadlo, D.J.1    Davies, G.J.2
  • 38
    • 72949107086 scopus 로고    scopus 로고
    • Glycosidase inhibition: Assessing mimicry of the transition state
    • Gloster, T.M. & Davies, G.J. Glycosidase inhibition: assessing mimicry of the transition state. Org. Biomol. Chem. 8, 305-320 (2010).
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 305-320
    • Gloster, T.M.1    Davies, G.J.2
  • 39
    • 48349138645 scopus 로고    scopus 로고
    • Covalent inhibitors of glycosidases and their applications in biochemistry and biology
    • Rempel, B.P. & Withers, S.G. Covalent inhibitors of glycosidases and their applications in biochemistry and biology. Glycobiology 18, 570-586 (2008).
    • (2008) Glycobiology , vol.18 , pp. 570-586
    • Rempel, B.P.1    Withers, S.G.2
  • 40
    • 78649383623 scopus 로고    scopus 로고
    • Cell-penetrant, nanomolar O-GlcNAcase inhibitors selective against lysosomal hexosaminidases
    • Dorfmueller, H.C., et al. Cell-penetrant, nanomolar O-GlcNAcase inhibitors selective against lysosomal hexosaminidases. Chem. Biol. 17, 1250-1255 (2010).
    • (2010) Chem. Biol. , vol.17 , pp. 1250-1255
    • Dorfmueller, H.C.1
  • 41
    • 33645469261 scopus 로고    scopus 로고
    • An O-GlcNAcase-specific inhibitor and substrate engineered by the extension of the N-acetyl moiety
    • Kim, E.J., Perreira, M., Thomas, C.J. & Hanover, J.A. An O-GlcNAcase-specific inhibitor and substrate engineered by the extension of the N-acetyl moiety. J. Am. Chem. Soc. 128, 4234-4235 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4234-4235
    • Kim, E.J.1    Perreira, M.2    Thomas, C.J.3    Hanover, J.A.4
  • 42
    • 0025980157 scopus 로고
    • Structural study of porcine pancreatic elastase complexed with 7-amino-3-(2-bromoethoxy)-4-chloroisocoumarin as a nonreactivatable doubly covalent enzyme-inhibitor complex
    • Vijayalakshmi, J., Meyer, E.F. Jr., Kam, C.M. & Powers, J.C. Structural study of porcine pancreatic elastase complexed with 7-amino-3-(2-bromoethoxy)-4-chloroisocoumarin as a nonreactivatable doubly covalent enzyme-inhibitor complex. Biochemistry 30, 2175-2183 (1991).
    • (1991) Biochemistry , vol.30 , pp. 2175-2183
    • Vijayalakshmi, J.1    Meyer, Jr.E.F.2    Kam, C.M.3    Powers, J.C.4
  • 43
    • 74249108028 scopus 로고    scopus 로고
    • Three decades of beta-lactamase inhibitors
    • Drawz, S.M. & Bonomo, R.A. Three decades of beta-lactamase inhibitors. Clin. Microbiol. Rev. 23, 160-201 (2010).
    • (2010) Clin. Microbiol. Rev. , vol.23 , pp. 160-201
    • Drawz, S.M.1    Bonomo, R.A.2
  • 45
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D., et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 48
    • 33749641136 scopus 로고    scopus 로고
    • The PyMOL G molecular graphics system
    • DeLano, W.L. The PyMOL GMolecular Graphics System. (Delano Scientific, 2002).
    • (2002) Delano Scientific
    • Delano, W.L.1


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