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Volumn 15, Issue 6, 2005, Pages 637-645

Recent structural insights into the expanding world of carbohydrate-active enzymes

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; ENZYME; GLYCOSIDASE; GLYCOSYLTRANSFERASE; POLYSACCHARIDE LYASE; SIALIDASE;

EID: 27944434246     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2005.10.008     Document Type: Review
Times cited : (249)

References (59)
  • 1
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated approach
    • H.J. Gilbert G.J. Davies B. Svensson B. Henrissat Royal Society of Chemistry
    • P.M. Coutinho, and B. Henrissat Carbohydrate-active enzymes: an integrated approach H.J. Gilbert G.J. Davies B. Svensson B. Henrissat Recent Advances in Carbohydrate Engineering 1999 Royal Society of Chemistry 3 12
    • (1999) Recent Advances in Carbohydrate Engineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 2
    • 0036716927 scopus 로고    scopus 로고
    • Glycogen metabolism loss: A common marker of parasitic behaviour in bacteria?
    • B. Henrissat, E. Deleury, and P.M. Coutinho Glycogen metabolism loss: a common marker of parasitic behaviour in bacteria? Trends Genet 18 2002 437 440
    • (2002) Trends Genet , vol.18 , pp. 437-440
    • Henrissat, B.1    Deleury, E.2    Coutinho, P.M.3
  • 3
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • G. Davies, and B. Henrissat Structures and mechanisms of glycosyl hydrolases Structure 3 1995 853 859
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 4
    • 1842477147 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima alpha-l-fucosidase - Insights into the catalytic mechanism and the molecular basis for fucosidosis
    • G. Sulzenbacher, C. Bignon, T. Nishimura, C.A. Tarling, S.G. Withers, B. Henrissat, and Y. Bourne Crystal structure of Thermotoga maritima alpha-l-fucosidase - insights into the catalytic mechanism and the molecular basis for fucosidosis J Biol Chem 279 2004 13119 13128
    • (2004) J Biol Chem , vol.279 , pp. 13119-13128
    • Sulzenbacher, G.1    Bignon, C.2    Nishimura, T.3    Tarling, C.A.4    Withers, S.G.5    Henrissat, B.6    Bourne, Y.7
  • 5
    • 2442458877 scopus 로고    scopus 로고
    • The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases
    • F. Alberto, C. Bignon, G. Sulzenbacher, B. Henrissat, and M. Czjzek The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases J Biol Chem 279 2004 18903 18910
    • (2004) J Biol Chem , vol.279 , pp. 18903-18910
    • Alberto, F.1    Bignon, C.2    Sulzenbacher, G.3    Henrissat, B.4    Czjzek, M.5
  • 6
    • 0242490546 scopus 로고    scopus 로고
    • Structural framework of fructosyl transfer in Bacillus subtilis levansucrase
    • G. Meng, and K. Futterer Structural framework of fructosyl transfer in Bacillus subtilis levansucrase Nat Struct Biol 10 2003 935 941
    • (2003) Nat Struct Biol , vol.10 , pp. 935-941
    • Meng, G.1    Futterer, K.2
  • 7
    • 1842554929 scopus 로고    scopus 로고
    • Parallel substrate binding sites in a beta-agarase suggest a novel mode of action on double-helical agarose
    • J. Allouch, W. Helbert, B. Henrissat, and M. Czjzek Parallel substrate binding sites in a beta-agarase suggest a novel mode of action on double-helical agarose Structure 12 2004 623 632
    • (2004) Structure , vol.12 , pp. 623-632
    • Allouch, J.1    Helbert, W.2    Henrissat, B.3    Czjzek, M.4
  • 8
    • 0042334876 scopus 로고    scopus 로고
    • Dextranase from Penicillum minioluteum: Reaction course, crystal structure, and product complex
    • A.M. Larsson, R. Andersson, J. Stahlberg, L. Kenne, and T.A. Jones Dextranase from Penicillum minioluteum: reaction course, crystal structure, and product complex Structure 11 2003 1111 1121
    • (2003) Structure , vol.11 , pp. 1111-1121
    • Larsson, A.M.1    Andersson, R.2    Stahlberg, J.3    Kenne, L.4    Jones, T.A.5
  • 9
    • 12544256784 scopus 로고    scopus 로고
    • Mechanistic and structural analysis of a family 31 alpha-glycosidase and its glycosyl-enzyme intermediate
    • A.L. Lovering, S.S. Lee, Y.W. Kim, S.G. Withers, and N.C.J. Strynadka Mechanistic and structural analysis of a family 31 alpha-glycosidase and its glycosyl-enzyme intermediate J Biol Chem 280 2005 2105 2115
    • (2005) J Biol Chem , vol.280 , pp. 2105-2115
    • Lovering, A.L.1    Lee, S.S.2    Kim, Y.W.3    Withers, S.G.4    Strynadka, N.C.J.5
  • 10
    • 3142572747 scopus 로고    scopus 로고
    • Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase
    • K. Yaoi, H. Kondo, N. Noro, M. Suzuki, S. Tsuda, and Y. Mitsuishi Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase Structure 12 2004 1209 1217
    • (2004) Structure , vol.12 , pp. 1209-1217
    • Yaoi, K.1    Kondo, H.2    Noro, N.3    Suzuki, M.4    Tsuda, S.5    Mitsuishi, Y.6
  • 11
    • 1842813472 scopus 로고    scopus 로고
    • Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding
    • P. Johansson, H. Brumer, M.J. Baumann, A.M. Kallas, H. Henriksson, S.E. Denman, T.T. Teeri, and T.A. Jones Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding Plant Cell 16 2004 874 886 Arguably one of the most sought-after three-dimensional structures in plant biochemistry. XET catalyses the cleavage and remodelling of plant cell-wall xyloglucan. This masterful work reveals the three-dimensional structure and the basis of its acceptor substrate specificity.
    • (2004) Plant Cell , vol.16 , pp. 874-886
    • Johansson, P.1    Brumer, H.2    Baumann, M.J.3    Kallas, A.M.4    Henriksson, H.5    Denman, S.E.6    Teeri, T.T.7    Jones, T.A.8
  • 12
    • 2442542178 scopus 로고    scopus 로고
    • Activation of crystalline cellulose surfaces through the chemoenzymatic modification of xyloglucan
    • ••], the XET enzyme is used to graft functional groups onto cellulosic (paper) surfaces without damaging the integrity of the cellulose.
    • (2004) J Am Chem Soc , vol.126 , pp. 5715-5721
    • Brumer, H.1    Zhou, Q.2    Baumann, M.J.3    Carlsson, K.4    Teeri, T.T.5
  • 13
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • D.E. Koshland 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
  • 14
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • D.L. Zechel, and S.G. Withers Glycosidase mechanisms: anatomy of a finely tuned catalyst Acc Chem Res 33 2000 11 18
    • (2000) Acc Chem Res , vol.33 , pp. 11-18
    • Zechel, D.L.1    Withers, S.G.2
  • 15
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • D.J. Vocadlo, G.J. Davies, R. Laine, and S.G. Withers Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate Nature 412 2001 835 838
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 21
    • 12144288130 scopus 로고    scopus 로고
    • The structure and receptor binding properties of the 1918 influenza hemagglutinin
    • S.J. Gamblin, L.F. Haire, R.J. Russell, D.J. Stevens, B. Xiao, Y. Ha, N. Vasisht, D.A. Steinhauer, R.S. Daniels, and A. Elliot The structure and receptor binding properties of the 1918 influenza hemagglutinin Science 303 2004 1838 1842 This article, and another in the same issue, analyses the three-dimensional structures of influenza virus haemagglutinins from various 'flu strains, including the fabled 1918 'flu. Mutations in the ligand-binding site allow 'flu to cross the species barrier by changing the specificity from sialic acid linked α-2,3 to galactose in avian intestines to the α-2,6 linkage of human respiratory tract glycans.
    • (2004) Science , vol.303 , pp. 1838-1842
    • Gamblin, S.J.1    Haire, L.F.2    Russell, R.J.3    Stevens, D.J.4    Xiao, B.5    Ha, Y.6    Vasisht, N.7    Steinhauer, D.A.8    Daniels, R.S.9    Elliot, A.10
  • 22
    • 0038546856 scopus 로고    scopus 로고
    • Trypanosoma cruzi trans-sialidase operates through a covalent sialyl-enzyme intermediate: Tyrosine is the catalytic nucleophile
    • A.G. Watts, I. Damager, M.L. Amaya, A. Buschiazzo, P. Alzari, A.C. Frasch, and S.G. Withers Trypanosoma cruzi trans-sialidase operates through a covalent sialyl-enzyme intermediate: tyrosine is the catalytic nucleophile J Am Chem Soc 125 2003 7532 7533 The first experimental demonstration that sialidases operate through the formation and subsequent breakdown of a covalent tyrosyl-enzyme intermediate. It will be interesting to see if this is demonstrated for a range of different sialidases.
    • (2003) J Am Chem Soc , vol.125 , pp. 7532-7533
    • Watts, A.G.1    Damager, I.2    Amaya, M.L.3    Buschiazzo, A.4    Alzari, P.5    Frasch, A.C.6    Withers, S.G.7
  • 23
    • 0036809661 scopus 로고    scopus 로고
    • The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis
    • A. Buschiazzo, M.F. Amaya, M.L. Cremona, A.C. Frasch, and P.M. Alzari The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis Mol Cell 10 2002 757 768 A tour-de-force structure determination of a medically important enzyme, brought about through insightful biochemistry and the construction of surface 'crystallisation' mutants. Sialic acid is shown to trigger a conformational change that increases affinity for the acceptor and aids transglycosylation, which is crucial to trypanosomal infection.
    • (2002) Mol Cell , vol.10 , pp. 757-768
    • Buschiazzo, A.1    Amaya, M.F.2    Cremona, M.L.3    Frasch, A.C.4    Alzari, P.M.5
  • 24
    • 2342590568 scopus 로고    scopus 로고
    • Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase
    • M.F. Amaya, A.G. Watts, T. Damager, A. Wehenkel, T. Nguyen, A. Buschiazzo, G. Paris, A.C. Frasch, S.G. Withers, and P.M. Alzari Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase Structure 12 2004 775 784 An elegant and revealing series of structural snapshots along the reaction coordinate of trans-sialidase, including the trapping of the covalent tyrosyl-enzyme intermediate.
    • (2004) Structure , vol.12 , pp. 775-784
    • Amaya, M.F.1    Watts, A.G.2    Damager, T.3    Wehenkel, A.4    Nguyen, T.5    Buschiazzo, A.6    Paris, G.7    Frasch, A.C.8    Withers, S.G.9    Alzari, P.M.10
  • 25
    • 27744503583 scopus 로고    scopus 로고
    • Two nucleophilic mutants of the Micomonospora viridifaciens sialidase operate with retention of configuration by two different mechanisms
    • in press.
    • Watson JN, Newstead S, Narine A, Taylor G, Bennet AJ: Two nucleophilic mutants of the Micomonospora viridifaciens sialidase operate with retention of configuration by two different mechanisms. ChemBioChem 2005, in press.
    • (2005) ChemBioChem
    • Watson, J.N.1    Newstead, S.2    Narine, A.3    Taylor, G.4    Bennet, A.J.5
  • 27
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • P. Coutinho, E. Deleury, G.J. Davies, and B. Henrissat An evolving hierarchical 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
  • 28
    • 0027965664 scopus 로고
    • Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose
    • A. Vrielink, W. Rüger, H.P.C. Driessen, and P.S. Freemont 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
  • 29
    • 0033580656 scopus 로고    scopus 로고
    • Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms
    • S.J. Charnock, and G.J. Davies 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
  • 30
    • 2442440054 scopus 로고    scopus 로고
    • Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: Interactions with acceptor and nucleotide ligands
    • A.M. Mulichak, W. Lu, H.C. Losey, C.T. Walsh, and R.M. Garavito Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands Biochemistry 43 2004 5170 5180 One in a series of perceptive papers from this team, who have provided unparalleled views of the modification of antibiotics by glycosylation. The GtfD structure was determined in complex with both nucleotide and the desvancosaminyl vancomycin acceptor, giving an in-depth understanding of specificity and catalysis.
    • (2004) Biochemistry , vol.43 , pp. 5170-5180
    • Mulichak, A.M.1    Lu, W.2    Losey, H.C.3    Walsh, C.T.4    Garavito, R.M.5
  • 31
    • 4444373841 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase: Homologous enzymes catalyze glycogen synthesis and degradation
    • A. Buschiazzo, J.E. Ugalde, M.E. Guerin, W. Shepard, R.A. Ugalde, and P.M. Alzari Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation EMBO J 23 2004 3196 3205
    • (2004) EMBO J , vol.23 , pp. 3196-3205
    • Buschiazzo, A.1    Ugalde, J.E.2    Guerin, M.E.3    Shepard, W.4    Ugalde, R.A.5    Alzari, P.M.6
  • 33
    • 2342420346 scopus 로고    scopus 로고
    • Structure of Kre2p/Mnt1p - A yeast alpha 1,2-mannosyltransferase involved in mannoprotein biosynthesis
    • Y.D. Lobsanov, P.A. Romero, B. Sleno, B.M. Yu, P. Yip, A. Herscovics, and P.L. Howell Structure of Kre2p/Mnt1p - a yeast alpha 1,2-mannosyltransferase involved in mannoprotein biosynthesis J Biol Chem 279 2004 17921 17931
    • (2004) J Biol Chem , vol.279 , pp. 17921-17931
    • Lobsanov, Y.D.1    Romero, P.A.2    Sleno, B.3    Yu, B.M.4    Yip, P.5    Herscovics, A.6    Howell, P.L.7
  • 34
    • 0345826092 scopus 로고    scopus 로고
    • The donor subsite of trehalose-6-phosphate synthase: Binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro glucose at 2Å resolution
    • R. Gibson, C.A. Tarling, S. Roberts, S.G. Withers, and G.J. Davies The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro glucose at 2Å resolution J Biol Chem 279 2004 1950 1955
    • (2004) J Biol Chem , vol.279 , pp. 1950-1955
    • Gibson, R.1    Tarling, C.A.2    Roberts, S.3    Withers, S.G.4    Davies, G.J.5
  • 35
    • 7444220526 scopus 로고    scopus 로고
    • The beginnings of mucin biosynthesis: The crystal structure of UDP-GalNAc: Polypeptide alpha-N-acetylgalactosaminyltransferase-T1
    • T.A. Fritz, J.H. Hurley, L.B. Trinh, J. Shiloach, and L.A. Tabak The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase-T1 Proc Natl Acad Sci USA 101 2004 15307 15312 The authors report the structure of an extremely important enzyme, one that displays a modular architecture featuring a CBM appended to the glycosyltransferase domain. The structure confirms early suggestions that this family of enzymes, which act with retention of anomeric configuration during catalysis, would be similar in three-dimensional structure to GT-2 inverting enzymes, as proposed in [29].
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15307-15312
    • Fritz, T.A.1    Hurley, J.H.2    Trinh, L.B.3    Shiloach, J.4    Tabak, L.A.5
  • 36
    • 0037417869 scopus 로고    scopus 로고
    • Crystal structure of the MurG: UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases
    • Y. Hu, L. Chen, S. Ha, B. Gross, B. Falcone, D. Walker, M. Mokhtarzadeh, and S. Walker Crystal structure of the MurG: UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases Proc Natl Acad Sci USA 100 2003 845 849
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 845-849
    • Hu, Y.1    Chen, L.2    Ha, S.3    Gross, B.4    Falcone, B.5    Walker, D.6    Mokhtarzadeh, M.7    Walker, S.8
  • 37
    • 0742288006 scopus 로고    scopus 로고
    • Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog
    • C.P.C. Chiu, A.G. Watts, L.L. Lairson, M. Gilbert, D. Lim, W.W. Wakarchuk, S.G. Withers, and N.C.J. Strynadka Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog Nat Struct Mol Biol 11 2004 163 170 Cell-surface sialic acid is one of the most important glycosylations in nature. This paper reports the first sialyltransferase structure determination and was consequently one of the American Chemical Society 'Chemical Highlights' of 2004. The enzyme transfers sialic acid to cell-surface glycoproteins and glycolipids. It has an unusual deviation from the canonical GT-A fold, with the donor interactions revealed through crystallisation with a non-transferrable DMP-sialic acid mimic.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 163-170
    • Chiu, C.P.C.1    Watts, A.G.2    Lairson, L.L.3    Gilbert, M.4    Lim, D.5    Wakarchuk, W.W.6    Withers, S.G.7    Strynadka, N.C.J.8
  • 38
    • 23644460027 scopus 로고    scopus 로고
    • Structural basis for the function of Clostridium difficile toxin B
    • D.J. Reinert, T. Jank, K. Aktories, and G.E. Schulz Structural basis for the function of Clostridium difficile toxin B J Mol Biol 351 2005 973 981
    • (2005) J Mol Biol , vol.351 , pp. 973-981
    • Reinert, D.J.1    Jank, T.2    Aktories, K.3    Schulz, G.E.4
  • 39
    • 0012784535 scopus 로고    scopus 로고
    • Crystal structure of an alpha 1,4-N- acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis
    • L.C. Pedersen, J. Dong, F. Taniguchi, H. Kitagawa, J.M. Krahn, L.G. Pedersen, K. Sugahara, and M. Negishi Crystal structure of an alpha 1,4-N- acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis J Biol Chem 278 2003 14420 14428 A fine structure determination and very interesting piece of scientific writing. All those working on retaining glycosyltransferases should read this paper, which reports the first structures of members of the exostosin gene family and provides an important structural dissection of the mechanisms of heparan synthesis.
    • (2003) J Biol Chem , vol.278 , pp. 14420-14428
    • Pedersen, L.C.1    Dong, J.2    Taniguchi, F.3    Kitagawa, H.4    Krahn, J.M.5    Pedersen, L.G.6    Sugahara, K.7    Negishi, M.8
  • 40
    • 23944471080 scopus 로고    scopus 로고
    • Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase
    • L. Larivière, N. Sommer, and S. Moréra Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase J Mol Biol 352 2005 139 150
    • (2005) J Mol Biol , vol.352 , pp. 139-150
    • Larivière, L.1    Sommer, N.2    Moréra, S.3
  • 41
    • 22144432266 scopus 로고    scopus 로고
    • Structural dissection and high-throughput screening of mannosylglycerate synthase
    • J. Flint, E. Taylor, M. Yang, D.N. Bolam, L.E. Tailford, C. Martinez-Flietes, E.J. Dodson, B.G. Davis, H.J. Gilbert, and G.J. Davies Structural dissection and high-throughput screening of mannosylglycerate synthase Nat Struct Mol Biol 12 2005 608 614 This work suggests one possible route to the functional dissection of glycosyltransferase activity. Three-dimensional structure is mute without solution characterisation of activity. Nowhere is this more true than in glycosyltransferase studies, not least because the two known folds are also adopted by enzymes that are not glycosyltransferases.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 608-614
    • Flint, J.1    Taylor, E.2    Yang, M.3    Bolam, D.N.4    Tailford, L.E.5    Martinez-Flietes, C.6    Dodson, E.J.7    Davis, B.G.8    Gilbert, H.J.9    Davies, G.J.10
  • 43
    • 1842686201 scopus 로고    scopus 로고
    • The crystal structure of feruloyl esterase a from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family
    • J.A. Hermoso, J. Sanz-Aparicio, R. Molina, N. Juge, R. Gonzalez, and C.B. Faulds The crystal structure of feruloyl esterase a from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family J Mol Biol 338 2004 495 506
    • (2004) J Mol Biol , vol.338 , pp. 495-506
    • Hermoso, J.A.1    Sanz-Aparicio, J.2    Molina, R.3    Juge, N.4    Gonzalez, R.5    Faulds, C.B.6
  • 44
    • 0034655985 scopus 로고    scopus 로고
    • Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases
    • A. Mølgaard, S. Kauppinen, and S. Larsen Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases Structure 8 2000 373 383
    • (2000) Structure , vol.8 , pp. 373-383
    • Mølgaard, A.1    Kauppinen, S.2    Larsen, S.3
  • 45
    • 0035951291 scopus 로고    scopus 로고
    • Three-dimensional structure of Erwinia chrysanthemi pectin methyl esterase reveals a novel esterase active site
    • J. Jenkins, O. Mayans, D. Smith, K. Worboys, and R.W. Pickersgill Three-dimensional structure of Erwinia chrysanthemi pectin methyl esterase reveals a novel esterase active site J Mol Biol 305 2001 951 960
    • (2001) J Mol Biol , vol.305 , pp. 951-960
    • Jenkins, J.1    Mayans, O.2    Smith, D.3    Worboys, K.4    Pickersgill, R.W.5
  • 46
    • 9744244982 scopus 로고    scopus 로고
    • Zinc hydrolases: The mechanisms of zinc-dependent deacetylases
    • M. Hernick, and C.A. Fierke Zinc hydrolases: the mechanisms of zinc-dependent deacetylases Arch Biochem Biophys 433 2005 71 84
    • (2005) Arch Biochem Biophys , vol.433 , pp. 71-84
    • Hernick, M.1    Fierke, C.A.2
  • 47
  • 49
    • 0345306583 scopus 로고    scopus 로고
    • The crystal structure of 1-d-myo-inosityl-2-acetamido-2-deoxy-alpha-d- glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold
    • J.T. Maynes, C. Garen, M.M. Cherney, G. Newton, D. Arad, Y. Av-Gay, R.C. Fahey, and M.N.G. James The crystal structure of 1-d-myo-inosityl-2-acetamido-2- deoxy-alpha-d-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold J Biol Chem 278 2003 47166 47170
    • (2003) J Biol Chem , vol.278 , pp. 47166-47170
    • Maynes, J.T.1    Garen, C.2    Cherney, M.M.3    Newton, G.4    Arad, D.5    Av-Gay, Y.6    Fahey, R.C.7    James, M.N.G.8
  • 50
    • 27344441825 scopus 로고    scopus 로고
    • Structure and metal-dependent mechanism of peptidoglycan deacetylase, a Streptococcal virulence factor
    • in press.
    • Blair DE, Schuttelkopf AW, MacRae JA, van Aalten DMF: Structure and metal-dependent mechanism of peptidoglycan deacetylase, a Streptococcal virulence factor. Proc Natl Acad Sci USA 2005, in press.
    • (2005) Proc Natl Acad Sci USA
    • Blair, D.E.1    Schuttelkopf, A.W.2    MacRae, J.A.3    Van Aalten, D.M.F.4
  • 51
    • 1642576068 scopus 로고    scopus 로고
    • The 3-D structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: A member of the urease superfamily
    • F. Vincent, D. Yates, E. Garman, G.J. Davies, and J.A. Brannigan The 3-D structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily J Biol Chem 279 2004 2809 2816
    • (2004) J Biol Chem , vol.279 , pp. 2809-2816
    • Vincent, F.1    Yates, D.2    Garman, E.3    Davies, G.J.4    Brannigan, J.A.5
  • 52
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine tuning polysaccharide recognition
    • A.B. Boraston, D.N. Bolam, H.J. Gilbert, and G.J. Davies Carbohydrate-binding modules: fine tuning polysaccharide recognition Biochem J 382 2004 769 781 A long-overdue review of CBMs, their three-dimensional structures and their mechanism of binding.
    • (2004) Biochem J , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 53
    • 15744367514 scopus 로고    scopus 로고
    • Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21
    • G. Vaaje-Kolstad, D.R. Houston, A.H.K. Riemen, V.G.H. Eijsink, and D.M.F. van Aalten Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21 J Biol Chem 280 2005 11313 11319 This elegant work clearly demonstrates a highly significant enhancement of enzyme activity when the CBM is added 'in trans'. Furthermore, electron micrographs show clear physical impact on the substrate by the chitin-binding module. A rare piece of unambiguous work in this controversial area.
    • (2005) J Biol Chem , vol.280 , pp. 11313-11319
    • Vaaje-Kolstad, G.1    Houston, D.R.2    Riemen, A.H.K.3    Eijsink, V.G.H.4    Van Aalten, D.M.F.5
  • 54
    • 0842346119 scopus 로고    scopus 로고
    • Glycoside hydrolase carbohydrate-binding modules as molecular probes for the analysis of plant cell wall polymers
    • L. McCartney, H.J. Gilbert, D.N. Bolam, A.B. Boraston, and J.P. Knox Glycoside hydrolase carbohydrate-binding modules as molecular probes for the analysis of plant cell wall polymers Anal Biochem 326 2004 49 54 The fact that many prokaryotes harness very different families of CBMs on their enzymes has long been confusing. This work not only reveals that different CBM families target different 'substructures' of plant cell-wall polysaccharides, but also provides a method to exploit this specificity for the analysis of cellular 'glyco-architecture'.
    • (2004) Anal Biochem , vol.326 , pp. 49-54
    • McCartney, L.1    Gilbert, H.J.2    Bolam, D.N.3    Boraston, A.B.4    Knox, J.P.5
  • 55
    • 0041422487 scopus 로고    scopus 로고
    • A chemical approach for identifying O-GlcNAc-modified proteins in cells
    • D.J. Vocadlo, H.C. Hang, E.J. Kim, J.A. Hanover, and C.R. Bertozzi A chemical approach for identifying O-GlcNAc-modified proteins in cells Proc Natl Acad Sci USA 100 2003 9116 9121 An elegant 'chemical biology' approach to analysing the massively important O-GlcNAc modification in eukaryotes. One can expect to see similar approaches harnessed to study many of the complex glycosylation reactions in the cell.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9116-9121
    • Vocadlo, D.J.1    Hang, H.C.2    Kim, E.J.3    Hanover, J.A.4    Bertozzi, C.R.5
  • 56
    • 7244251649 scopus 로고    scopus 로고
    • A strategy for functional proteomic analysis of glycosidase activity from cell lysates
    • D.J. Vocadlo, and C.R. Bertozzi A strategy for functional proteomic analysis of glycosidase activity from cell lysates Angew Chem Int Ed Engl 43 2004 5338 5342
    • (2004) Angew Chem Int Ed Engl , vol.43 , pp. 5338-5342
    • Vocadlo, D.J.1    Bertozzi, C.R.2
  • 57
    • 21844464281 scopus 로고    scopus 로고
    • O-GlcNAcase uses substrate-assisted catalysis - Kinetic analysis and development of highly selective mechanism-inspired inhibitors
    • M.S. Macauley, G.E. Whitworth, A.W. Debowski, D. Chin, and D.J. Vocadlo O-GlcNAcase uses substrate-assisted catalysis - kinetic analysis and development of highly selective mechanism-inspired inhibitors J Biol Chem 280 2005 25313 25322 Again a vision of the future using the O-GlcNAc modification as an example. A panel of inhibitors both define the reaction mechanism and allow specific intervention.
    • (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
  • 58
    • 0037865396 scopus 로고    scopus 로고
    • Mapping the conformational itinerary of β-glycosidases by X-ray crystallography
    • G.J. Davies, V.M.-A. Ducros, A. Varrot, and D.L. Zechel 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
  • 59
    • 0034838385 scopus 로고    scopus 로고
    • The conquest of the last frontier of molecular and cell biology
    • N. Sharon The conquest of the last frontier of molecular and cell biology Biochimie 83 2001 555
    • (2001) Biochimie , vol.83 , pp. 555
    • Sharon, N.1


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