메뉴 건너뛰기




Volumn 1800, Issue 2, 2010, Pages 122-133

Structural analyses of enzymes involved in the O-GlcNAc modification

Author keywords

Carbohydrate active enzyme; Enzyme; GH84; GT41; Hydrolase; O GlcNAc; Reaction mechanism; Structure; Transferase

Indexed keywords

ACETYLGLUCOSAMINIDASE; AZAPENE; ENZYME INHIBITOR; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINE THIAZOLINE; N ACETYLGLUCOSAMINYLTRANSFERASE; N BUTYL THIAZOLINE; O (2 ACETAMIDO 2 DEOXY DEXTRO GLYCOPYRANOSYLIDENE)AMINO N PHENYLCARBAMIC ACID; STREPTOZOCIN; SUGAR IMIDAZOLE DERIVATIVE; THIAZOLINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 77949309755     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2009.07.019     Document Type: Review
Times cited : (35)

References (87)
  • 1
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres C.R., and Hart G.W. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem. 259 (1984) 3308-3317
    • (1984) J. Biol. Chem. , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 2
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins
    • Hart G.W., Housley M.P., and Slawson C. Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 446 (2007) 1017-1022
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 3
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc
    • Wells L., Vosseller K., and Hart G.W. Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 291 (2001) 2376-2378
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 4
    • 0037117511 scopus 로고    scopus 로고
    • Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3 T3-L1 adipocytes
    • Vosseller K., Wells L., Lane M.D., and Hart G.W. Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3 T3-L1 adipocytes. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 5313-5318
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5313-5318
    • Vosseller, K.1    Wells, L.2    Lane, M.D.3    Hart, G.W.4
  • 6
    • 0025193520 scopus 로고
    • Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosaminyltransferase
    • Haltiwanger R.S., Holt G.D., and Hart G.W. Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosaminyltransferase. J. Biol. Chem. 265 (1990) 2563-2568
    • (1990) J. Biol. Chem. , vol.265 , pp. 2563-2568
    • Haltiwanger, R.S.1    Holt, G.D.2    Hart, G.W.3
  • 7
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • Kreppel L.K., Blomberg M.A., and Hart G.W. Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272 (1997) 9308-9315
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 8
    • 0030944105 scopus 로고    scopus 로고
    • O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • Lubas W.A., Frank D.W., Krause M., and Hanover J.A. O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272 (1997) 9316-9324
    • (1997) J. Biol. Chem. , vol.272 , pp. 9316-9324
    • Lubas, W.A.1    Frank, D.W.2    Krause, M.3    Hanover, J.A.4
  • 9
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol
    • Dong D.L., and Hart G.W. Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol. J. Biol. Chem. 269 (1994) 19321-19330
    • (1994) J. Biol. Chem. , vol.269 , pp. 19321-19330
    • Dong, D.L.1    Hart, G.W.2
  • 10
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain
    • Gao Y., Wells L., Comer F.I., Parker G.J., and Hart G.W. Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain. J. Biol. Chem. 276 (2001) 9838-9845
    • (2001) J. Biol. Chem. , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3    Parker, G.J.4    Hart, G.W.5
  • 11
    • 0016271953 scopus 로고
    • Separation and properties of human brain hexosaminidase C
    • Braidman I., Carroll M., Dance N., and Robinson D. Separation and properties of human brain hexosaminidase C. Biochem. J. 143 (1974) 295-301
    • (1974) Biochem. J. , vol.143 , pp. 295-301
    • Braidman, I.1    Carroll, M.2    Dance, N.3    Robinson, D.4
  • 13
    • 53849121583 scopus 로고    scopus 로고
    • Mechanistic insights into glycosidase chemistry
    • Vocadlo D., and Davies G.J. Mechanistic insights into glycosidase chemistry. Curr. Opin. Chem. Biol. 12 (2008) 539-555
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 539-555
    • Vocadlo, D.1    Davies, G.J.2
  • 14
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat B., and Davies G. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7 (1997) 637-644
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 15
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G., and Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 3 (1995) 853-859
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 17
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: anatomy of a finely tuned catalyst
    • Zechel D.L., and Withers S.G. Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc. Chem. Rev. 33 (2000) 11-18
    • (2000) Acc. Chem. Rev. , vol.33 , pp. 11-18
    • Zechel, D.L.1    Withers, S.G.2
  • 19
    • 67650266244 scopus 로고    scopus 로고
    • Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes
    • 10.1042/BJ20080382 (online only)
    • Davies G.J., and Sinnott M.L. Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (2008) 10.1042/BJ20080382 (online only)
    • (2008) Biochem. J.
    • Davies, G.J.1    Sinnott, M.L.2
  • 20
    • 0030843984 scopus 로고    scopus 로고
    • A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities
    • Campbell J.A., Davies G.J., Bulone V., and Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 326 (1997) 929-939
    • (1997) Biochem. J. , vol.326 , pp. 929-939
    • Campbell, J.A.1    Davies, G.J.2    Bulone, V.3    Henrissat, B.4
  • 21
    • 0037466315 scopus 로고    scopus 로고
    • An evolving heirarchical family classification for glycosyltransferases
    • Coutinho P., Deleury E., Davies G.J., and Henrissat B. An evolving heirarchical family classification for glycosyltransferases. J. Mol. Biol. 328 (2003) 307-317
    • (2003) J. Mol. Biol. , vol.328 , pp. 307-317
    • Coutinho, P.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 23
    • 0027965664 scopus 로고
    • Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose
    • Vrielink A., Rüger W., Driessen H.P.C., and Freemont P.S. Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose. EMBO J. 13 (1994) 3413-3422
    • (1994) EMBO J. , vol.13 , pp. 3413-3422
    • Vrielink, A.1    Rüger, W.2    Driessen, H.P.C.3    Freemont, P.S.4
  • 24
    • 0033580656 scopus 로고    scopus 로고
    • Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms
    • Charnock S.J., and Davies G.J. Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms. Biochemistry 38 (1999) 6380-6385
    • (1999) Biochemistry , vol.38 , pp. 6380-6385
    • Charnock, S.J.1    Davies, G.J.2
  • 25
    • 27944434246 scopus 로고    scopus 로고
    • Recent structural insights into the expanding world of carbohydrate-active enzymes
    • Davies G.J., Gloster T.M., and Henrissat B. Recent structural insights into the expanding world of carbohydrate-active enzymes. Curr. Opin. Struct. Biol. 15 (2005) 637-645
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 637-645
    • Davies, G.J.1    Gloster, T.M.2    Henrissat, B.3
  • 26
    • 53249091825 scopus 로고    scopus 로고
    • Glycosyltransferases, glycoside hydrolases: surprise, surprise!
    • Henrissat B., Sulzenbacher G., and Bourne Y. Glycosyltransferases, glycoside hydrolases: surprise, surprise!. Curr. Opin. Struct. Biol. 18 (2008) 527-533
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 527-533
    • Henrissat, B.1    Sulzenbacher, G.2    Bourne, Y.3
  • 27
    • 77949288470 scopus 로고    scopus 로고
    • M.S. Macauley, D.J. Vocadlo, Pharmacological elevation of O-GlcNAc levels: overview of small molecule inhibitors of O-GlcNAcase, Biochim. Biophys. Acta this special issue, (in press).
    • M.S. Macauley, D.J. Vocadlo, Pharmacological elevation of O-GlcNAc levels: overview of small molecule inhibitors of O-GlcNAcase, Biochim. Biophys. Acta this special issue, (in press).
  • 29
    • 4744341309 scopus 로고    scopus 로고
    • The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha
    • Jinek M., Rehwinkel J., Lazarus B.D., Izaurralde E., Hanover J.A., and Conti E. The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha. Nat. Struct. Mol. Biol. 11 (2004) 1001-1007
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1001-1007
    • Jinek, M.1    Rehwinkel, J.2    Lazarus, B.D.3    Izaurralde, E.4    Hanover, J.A.5    Conti, E.6
  • 30
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha
    • Conti E., Uy M., Leighton L., Blobel G., and Kuriyan J. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. Cell 94 (1998) 193-204
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 31
    • 0035805117 scopus 로고    scopus 로고
    • The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin
    • Huber A.H., and Weis W.I. The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin. Cell 105 (2001) 391-402
    • (2001) Cell , vol.105 , pp. 391-402
    • Huber, A.H.1    Weis, W.I.2
  • 34
    • 0035976715 scopus 로고    scopus 로고
    • Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily
    • Wrabl J.O., and Grishin N.V. Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. J. Mol. Biol 314 (2001) 365-374
    • (2001) J. Mol. Biol , vol.314 , pp. 365-374
    • Wrabl, J.O.1    Grishin, N.V.2
  • 35
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: the versatile helix
    • D'Andrea L.D., and Regan L. TPR proteins: the versatile helix. Trends Biochem. Sci. 28 (2003) 655-662
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 36
    • 0034646669 scopus 로고    scopus 로고
    • Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity
    • Lubas W.A., and Hanover J.A. Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. J. Biol. Chem. 275 (2000) 10983-10988
    • (2000) J. Biol. Chem. , vol.275 , pp. 10983-10988
    • Lubas, W.A.1    Hanover, J.A.2
  • 37
    • 0042090275 scopus 로고    scopus 로고
    • Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity
    • Iyer S.P., and Hart G.W. Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity. J. Biol. Chem. 278 (2003) 24608-24616
    • (2003) J. Biol. Chem. , vol.278 , pp. 24608-24616
    • Iyer, S.P.1    Hart, G.W.2
  • 38
    • 34250309514 scopus 로고    scopus 로고
    • A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates
    • Leavy T.M., and Bertozzi C.R. A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates. Bioorg. Med. Chem. Lett. 17 (2007) 3851-3854
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 3851-3854
    • Leavy, T.M.1    Bertozzi, C.R.2
  • 40
    • 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., Nam G., Kim E.J., Frohlich R., Hanover J.A., and Kirk K.L. 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 (2008) 189-195
    • (2008) Carbohydr. Res. , vol.343 , pp. 189-195
    • Hajduch, J.1    Nam, G.2    Kim, E.J.3    Frohlich, R.4    Hanover, J.A.5    Kirk, K.L.6
  • 43
    • 11144246904 scopus 로고    scopus 로고
    • Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities
    • Toleman C., Paterson A.J., Whisenhunt T.R., and Kudlow J.E. Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities. J. Biol. Chem. 279 (2004) 53665-53673
    • (2004) J. Biol. Chem. , vol.279 , pp. 53665-53673
    • Toleman, C.1    Paterson, A.J.2    Whisenhunt, T.R.3    Kudlow, J.E.4
  • 44
    • 53049097590 scopus 로고    scopus 로고
    • Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3 during apoptosis
    • Butkinaree C., Cheung W.D., Park S., Park K., Barber M., and Hart G.W. Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3 during apoptosis. J. Biol. Chem. 283 (2008) 23557-23566
    • (2008) J. Biol. Chem. , vol.283 , pp. 23557-23566
    • Butkinaree, C.1    Cheung, W.D.2    Park, S.3    Park, K.4    Barber, M.5    Hart, G.W.6
  • 45
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies G.J., Wilson K.S., and Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321 (1997) 557-559
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 46
    • 33645735070 scopus 로고    scopus 로고
    • Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis
    • Rao F.V., Dorfmueller H.C., Villa F., Allwood M., Eggleston I.M., and van Aalten D.M. Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. EMBO J. 25 (2006) 1569-1578
    • (2006) EMBO J. , vol.25 , pp. 1569-1578
    • Rao, F.V.1    Dorfmueller, H.C.2    Villa, F.3    Allwood, M.4    Eggleston, I.M.5    van Aalten, D.M.6
  • 47
    • 62549165181 scopus 로고    scopus 로고
    • Structural insight into the mechanism of streptozotocin inhibition of O-GlcNAcase
    • He Y., Martinez-Fleites C., Bubb A., Gloster T.M., and Davies G.J. Structural insight into the mechanism of streptozotocin inhibition of O-GlcNAcase. Carbohydr. Res. 344 (2009) 627-631
    • (2009) Carbohydr. Res. , vol.344 , pp. 627-631
    • He, Y.1    Martinez-Fleites, C.2    Bubb, A.3    Gloster, T.M.4    Davies, G.J.5
  • 48
    • 67650070343 scopus 로고    scopus 로고
    • Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ
    • Balcewich M.D., Stubbs K.A., He Y., James T.W., Davies G.J., Vocadlo D.J., and Mark B.L. Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ. Protein Sci. 18 (2009) 1541-1551
    • (2009) Protein Sci. , vol.18 , pp. 1541-1551
    • Balcewich, M.D.1    Stubbs, K.A.2    He, Y.3    James, T.W.4    Davies, G.J.5    Vocadlo, D.J.6    Mark, B.L.7
  • 49
    • 21844464281 scopus 로고    scopus 로고
    • O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors
    • Macauley M.S., Whitworth G.E., Debowski A.W., Chin D., and Vocadlo D.J. O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors. J. Biol. Chem. 280 (2005) 25313-25322
    • (2005) J. Biol. Chem. , vol.280 , pp. 25313-25322
    • Macauley, M.S.1    Whitworth, G.E.2    Debowski, A.W.3    Chin, D.4    Vocadlo, D.J.5
  • 50
    • 33750006857 scopus 로고    scopus 로고
    • Analysis of a group A streptococcal glycoside hydrolase from family 84 reveals it is a β-N-acetylglucosaminidase and not a hyaluronidase
    • Sheldon W.L., Macauley M.S., Taylor E.J., Robinson C.E., Charnock S.J., Davies G.J., Vocadlo D.J., and Black G.W. Analysis of a group A streptococcal glycoside hydrolase from family 84 reveals it is a β-N-acetylglucosaminidase and not a hyaluronidase. Biochem. J. 399 (2006) 241-247
    • (2006) Biochem. J. , vol.399 , pp. 241-247
    • Sheldon, W.L.1    Macauley, M.S.2    Taylor, E.J.3    Robinson, C.E.4    Charnock, S.J.5    Davies, G.J.6    Vocadlo, D.J.7    Black, G.W.8
  • 51
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • Koshland D.E. Stereochemistry and the mechanism of enzymatic reactions. Biol. Rev. 28 (1953) 416-436
    • (1953) Biol. Rev. , vol.28 , pp. 416-436
    • Koshland, D.E.1
  • 52
    • 25444533563 scopus 로고    scopus 로고
    • Detailed comparative analysis of the catalytic mechanisms of beta-N-acetylglucosaminidases from families 3 and 20 of glycoside hydrolases
    • Vocadlo D.J., and Withers S.G. Detailed comparative analysis of the catalytic mechanisms of beta-N-acetylglucosaminidases from families 3 and 20 of glycoside hydrolases. Biochemistry 44 (2005) 12809-12818
    • (2005) Biochemistry , vol.44 , pp. 12809-12818
    • Vocadlo, D.J.1    Withers, S.G.2
  • 54
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and x-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis
    • Terwisscha Van Scheltinga A.C., Armand S., Kalk K.H., Isogai A., Henrissat B., and Dijkstra B.W. Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and x-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry 34 (1995) 15619-15623
    • (1995) Biochemistry , vol.34 , pp. 15619-15623
    • Terwisscha Van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 55
    • 0029940470 scopus 로고    scopus 로고
    • Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease
    • Tews I., Perrakis A., Oppenheim A., Dauter Z., Wilson K.S., and Vorgias C.E. Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat. Struct. Biol. 3 (1996) 638-648
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 638-648
    • Tews, I.1    Perrakis, A.2    Oppenheim, A.3    Dauter, Z.4    Wilson, K.S.5    Vorgias, C.E.6
  • 57
    • 0035971079 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase
    • Mark B.L., Vocadlo D.J., Knapp S., Triggs-Raine B.L., Withers S.G., and James M.N. Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase. J. Biol. Chem. 276 (2001) 10330-10337
    • (2001) J. Biol. Chem. , vol.276 , pp. 10330-10337
    • Mark, B.L.1    Vocadlo, D.J.2    Knapp, S.3    Triggs-Raine, B.L.4    Withers, S.G.5    James, M.N.6
  • 60
    • 65649151773 scopus 로고    scopus 로고
    • Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens
    • Ficko-Blean E., Gregg K.J., Adams J.J., Hehemann J.H., Czjzek M., Smith S.P., and Boraston A.B. Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens. J. Biol. Chem. 284 (2009) 9876-9884
    • (2009) J. Biol. Chem. , vol.284 , pp. 9876-9884
    • Ficko-Blean, E.1    Gregg, K.J.2    Adams, J.J.3    Hehemann, J.H.4    Czjzek, M.5    Smith, S.P.6    Boraston, A.B.7
  • 61
    • 68949170989 scopus 로고    scopus 로고
    • The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration
    • Martinez-Fleites C., Korczynska J.E., Davies G.J., Cope M.J., Turkenburg J.P., and Taylor E.J. The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration. Carbohydr. Res. 344 (2009) 1753-1757
    • (2009) Carbohydr. Res. , vol.344 , pp. 1753-1757
    • Martinez-Fleites, C.1    Korczynska, J.E.2    Davies, G.J.3    Cope, M.J.4    Turkenburg, J.P.5    Taylor, E.J.6
  • 62
    • 66449099328 scopus 로고    scopus 로고
    • Streptococcus pneumoniae endohexosaminidase D: structural and mechanistic insight into substrate-assisted catalysis in family 85 glycoside hydrolases
    • Abbott D.W., Macauley M.S., Vocadlo D.J., and Boraston A.B. Streptococcus pneumoniae endohexosaminidase D: structural and mechanistic insight into substrate-assisted catalysis in family 85 glycoside hydrolases. J. Biol. Chem. 284 (2009) 11676-11689
    • (2009) J. Biol. Chem. , vol.284 , pp. 11676-11689
    • Abbott, D.W.1    Macauley, M.S.2    Vocadlo, D.J.3    Boraston, A.B.4
  • 64
    • 33645226771 scopus 로고    scopus 로고
    • Identification of Asp(174) and Asp(175) as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants
    • Cetinbas N., Macauley M.S., Stubbs K.A., Drapala R., and Vocadlo D.J. Identification of Asp(174) and Asp(175) as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants. Biochemistry 45 (2006) 3835-3844
    • (2006) Biochemistry , vol.45 , pp. 3835-3844
    • Cetinbas, N.1    Macauley, M.S.2    Stubbs, K.A.3    Drapala, R.4    Vocadlo, D.J.5
  • 66
    • 0037865396 scopus 로고    scopus 로고
    • Mapping the conformational itinerary of β-glycosidases by X-ray crystallography
    • Davies G.J., Ducros V.M.-A., Varrot A., and Zechel D.L. Mapping the conformational itinerary of β-glycosidases by X-ray crystallography. Biochem. Soc. Trans. 31 (2003) 523-527
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 523-527
    • Davies, G.J.1    Ducros, V.M.-A.2    Varrot, A.3    Zechel, D.L.4
  • 67
    • 0029947945 scopus 로고    scopus 로고
    • NAG-thiazoline, an N-acetyl-beta-hexosaminidase inhibitor that implicates acetamido participation
    • Knapp S., Vocadlo D., Gao Z.N., Kirk B., Lou J.P., and Withers S.G. NAG-thiazoline, an N-acetyl-beta-hexosaminidase inhibitor that implicates acetamido participation. J. Am. Chem. Soc. 118 (1996) 6804-6805
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6804-6805
    • Knapp, S.1    Vocadlo, D.2    Gao, Z.N.3    Kirk, B.4    Lou, J.P.5    Withers, S.G.6
  • 68
    • 33846412613 scopus 로고    scopus 로고
    • Analysis of PUGNAc and NAG-thiazoline as transition state analogues for human O-GlcNAcase: mechanistic and structural insights into inhibitor selectivity and transition state poise
    • Whitworth G.E., Macauley M.S., Stubbs K.A., Dennis R.J., Taylor E.J., Davies G.J., Greig I.R., and Vocadlo D.J. Analysis of PUGNAc and NAG-thiazoline as transition state analogues for human O-GlcNAcase: mechanistic and structural insights into inhibitor selectivity and transition state poise. J. Am. Chem. Soc. 129 (2007) 635-644
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 635-644
    • Whitworth, G.E.1    Macauley, M.S.2    Stubbs, K.A.3    Dennis, R.J.4    Taylor, E.J.5    Davies, G.J.6    Greig, I.R.7    Vocadlo, D.J.8
  • 69
    • 67749092463 scopus 로고    scopus 로고
    • Molecular Basis for Inhibition of GH84 Glycoside Hydrolases by Substituted Azepanes: Conformational Flexibility Enables Probing of Substrate Distortion
    • Marcelo F., He Y., Yuzwa S.A., Nieto L., Jimenez-Barbero J., Sollogoub M., Vocadlo D.J., Davies G.D., and Bleriot Y. Molecular Basis for Inhibition of GH84 Glycoside Hydrolases by Substituted Azepanes: Conformational Flexibility Enables Probing of Substrate Distortion. J. Am. Chem. Soc. 131 (2009) 5390-5392
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5390-5392
    • Marcelo, F.1    He, Y.2    Yuzwa, S.A.3    Nieto, L.4    Jimenez-Barbero, J.5    Sollogoub, M.6    Vocadlo, D.J.7    Davies, G.D.8    Bleriot, Y.9
  • 70
  • 71
    • 58049197848 scopus 로고    scopus 로고
    • Elevation of global O-GlcNAc levels in 3 T3-L1 adipocytes by selective inhibition of O-GlcNAcase does not induce insulin resistance
    • Macauley M.S., Bubb A.K., Martinez-Fleites C., Davies G.J., and Vocadlo D.J. Elevation of global O-GlcNAc levels in 3 T3-L1 adipocytes by selective inhibition of O-GlcNAcase does not induce insulin resistance. J. Biol. Chem. 283 (2008) 34687-34695
    • (2008) J. Biol. Chem. , vol.283 , pp. 34687-34695
    • Macauley, M.S.1    Bubb, A.K.2    Martinez-Fleites, C.3    Davies, G.J.4    Vocadlo, D.J.5
  • 72
    • 0035872219 scopus 로고    scopus 로고
    • The potential mechanism of the diabetogenic action of streptozotocin: inhibition of pancreatic beta-cell O-GlcNAc-selective N-acetyl-beta-D-glucosaminidase
    • Konrad R.J., Mikolaenko I., Tolar J.F., Liu K., and Kudlow J.E. The potential mechanism of the diabetogenic action of streptozotocin: inhibition of pancreatic beta-cell O-GlcNAc-selective N-acetyl-beta-D-glucosaminidase. Biochem. J. 356 (2001) 31-41
    • (2001) Biochem. J. , vol.356 , pp. 31-41
    • Konrad, R.J.1    Mikolaenko, I.2    Tolar, J.F.3    Liu, K.4    Kudlow, J.E.5
  • 73
    • 0019812690 scopus 로고
    • Streptozotocin and alloxan induce dna strand breaks and poly(adp-ribose) synthetase in pancreatic-islets
    • Yamamoto H., Uchigata Y., and Okamoto H. Streptozotocin and alloxan induce dna strand breaks and poly(adp-ribose) synthetase in pancreatic-islets. Nature 294 (1981) 284-286
    • (1981) Nature , vol.294 , pp. 284-286
    • Yamamoto, H.1    Uchigata, Y.2    Okamoto, H.3
  • 74
    • 0029257151 scopus 로고
    • Nitric oxide generation during cellular metabolization of the diabetogenic N-methyl-N-nitroso-urea streptozotozin contributes to islet cell DNA damage
    • Kroncke K.D., Fehsel K., Sommer A., Rodriguez M.L., and Kolb-Bachofen V. Nitric oxide generation during cellular metabolization of the diabetogenic N-methyl-N-nitroso-urea streptozotozin contributes to islet cell DNA damage. Biol. Chem. Hoppe Seyler 376 (1995) 179-185
    • (1995) Biol. Chem. Hoppe Seyler , vol.376 , pp. 179-185
    • Kroncke, K.D.1    Fehsel, K.2    Sommer, A.3    Rodriguez, M.L.4    Kolb-Bachofen, V.5
  • 75
    • 49449101898 scopus 로고    scopus 로고
    • Chemical dissection of the link between streptozotocin, O-GlcNAc, and pancreatic cell death
    • Pathak S., Dorfmueller H.C., Borodkin V.S., and van Aalten D.M. Chemical dissection of the link between streptozotocin, O-GlcNAc, and pancreatic cell death. Chem. Biol. 15 (2008) 799-807
    • (2008) Chem. Biol. , vol.15 , pp. 799-807
    • Pathak, S.1    Dorfmueller, H.C.2    Borodkin, V.S.3    van Aalten, D.M.4
  • 76
    • 0025015612 scopus 로고
    • Synthesis of 2-acetamido-2-deoxy-d-gluconhydroximolactone-derived and chitobionhydroximolactone-derived n-phenylcarbamates, potential inhibitors of beta-N-acetylglucosaminidase
    • Beer D., Maloisel J.L., Rast D.M., and Vasella A. Synthesis of 2-acetamido-2-deoxy-d-gluconhydroximolactone-derived and chitobionhydroximolactone-derived n-phenylcarbamates, potential inhibitors of beta-N-acetylglucosaminidase. Helv. Chim. Acta 73 (1990) 1918-1922
    • (1990) Helv. Chim. Acta , vol.73 , pp. 1918-1922
    • Beer, D.1    Maloisel, J.L.2    Rast, D.M.3    Vasella, A.4
  • 77
    • 60149092312 scopus 로고    scopus 로고
    • A selective inhibitor Gal-PUGNAc of human lysosomal beta-hexosaminidases modulates levels of the ganglioside GM2 in neuroblastoma cells
    • Stubbs K.A., Macauley M.S., and Vocdlo D.J. A selective inhibitor Gal-PUGNAc of human lysosomal beta-hexosaminidases modulates levels of the ganglioside GM2 in neuroblastoma cells. Angew. Chem. Int. Ed. 48 (2009) 1300-1303
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 1300-1303
    • Stubbs, K.A.1    Macauley, M.S.2    Vocdlo, D.J.3
  • 80
    • 33744798282 scopus 로고    scopus 로고
    • Crystallographic structure of human beta-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis
    • Lemieux M.J., Mark B.L., Cherney M.M., Withers S.G., Mahuran D.J., and James M.N. Crystallographic structure of human beta-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis. J. Mol. Biol. 359 (2006) 913-929
    • (2006) J. Mol. Biol. , vol.359 , pp. 913-929
    • Lemieux, M.J.1    Mark, B.L.2    Cherney, M.M.3    Withers, S.G.4    Mahuran, D.J.5    James, M.N.6
  • 81
    • 0344837327 scopus 로고    scopus 로고
    • Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease
    • Mark B.L., Mahuran D.J., Cherney M.M., Zhao D., Knapp S., and James M.N. Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease. J. Mol. Biol. 327 (2003) 1093-1109
    • (2003) J. Mol. Biol. , vol.327 , pp. 1093-1109
    • Mark, B.L.1    Mahuran, D.J.2    Cherney, M.M.3    Zhao, D.4    Knapp, S.5    James, M.N.6
  • 82
    • 0035233113 scopus 로고    scopus 로고
    • Naturally occurring mutations in GM2 gangliosidosis: a compendium
    • Triggs-Raine B., Mahuran D.J., and Gravel R.A. Naturally occurring mutations in GM2 gangliosidosis: a compendium. Adv. Genet. 44 (2001) 199-224
    • (2001) Adv. Genet. , vol.44 , pp. 199-224
    • Triggs-Raine, B.1    Mahuran, D.J.2    Gravel, R.A.3
  • 84
    • 66549119673 scopus 로고    scopus 로고
    • GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation
    • Dorfmueller H.C., Borodkin V.S., Schimpl M., and van Aalten D.M. GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation. Biochem. J. 420 (2009) 221-227
    • (2009) Biochem. J. , vol.420 , pp. 221-227
    • Dorfmueller, H.C.1    Borodkin, V.S.2    Schimpl, M.3    van Aalten, D.M.4
  • 86
    • 33845944034 scopus 로고    scopus 로고
    • GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels
    • Dorfmueller H.C., Borodkin V.S., Schimpl M., Shepherd S.M., Shpiro N.A., and van Aalten D.M. GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels. J. Am. Chem. Soc. 128 (2006) 16484-16485
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16484-16485
    • Dorfmueller, H.C.1    Borodkin, V.S.2    Schimpl, M.3    Shepherd, S.M.4    Shpiro, N.A.5    van Aalten, D.M.6
  • 87
    • 27144455345 scopus 로고    scopus 로고
    • Discovery of O-GlcNAc transferase inhibitors
    • Gross B.J., Kraybill B.C., and Walker S. Discovery of O-GlcNAc transferase inhibitors. J. Am. Chem. Soc. 127 (2005) 14588-14589
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 14588-14589
    • Gross, B.J.1    Kraybill, B.C.2    Walker, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.