메뉴 건너뛰기




Volumn 403, Issue 4, 2010, Pages 578-590

Chemoenzymatic Synthesis, Inhibition Studies, and X-ray Crystallographic Analysis of the Phosphono Analog of UDP-Galp as an Inhibitor and Mechanistic Probe for UDP-Galactopyranose Mutase

Author keywords

Enzyme inhibition and binding; Phosphonate analog; UDP galactopyranose mutase

Indexed keywords

ARGININE; FURAN DERIVATIVE; GALACTOFURANOSE; GALACTOPYRANOSE MUTASE; GLYCOCONJUGATE; HEXOSE; MUTASE; PHOSPHONIC ACID DERIVATIVE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE; URIDINE DIPHOSPHATE ALPHA DEXTRO GALACTOFURANOSE; URIDINE DIPHOSPHATE GALACTOSE; URIDINE DIPHOSPHATE PHOSPHONOGALACTOPYRANOSE; ARABIDOPSIS PROTEIN; GALACTOSE; MOLECULAR PROBE; NUCLEOTIDYLTRANSFERASE; RECOMBINANT PROTEIN; UDP-GALACTOPYRANOSE MUTASE; UDP-SUGAR PYROPHOSPHORYLASE, ARABIDOPSIS; URIDINE DIPHOSPHATE GALACTOFURANOSE;

EID: 77957900135     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.08.053     Document Type: Article
Times cited : (41)

References (50)
  • 1
    • 0034971311 scopus 로고    scopus 로고
    • Cell wall core galactofuran synthesis is essential for growth of mycobacteria
    • Pan F., Jackson M., Ma Y., McNeil M. Cell wall core galactofuran synthesis is essential for growth of mycobacteria. J. Bacteriol. 2001, 183:3991-3998.
    • (2001) J. Bacteriol. , vol.183 , pp. 3991-3998
    • Pan, F.1    Jackson, M.2    Ma, Y.3    McNeil, M.4
  • 2
    • 0034255342 scopus 로고    scopus 로고
    • Lipophosphoglycan is a virulence factor distinct from related glycoconjugates in the protozoan parasite Leishmania major
    • Späth G., Epstein L., Leader B., Singer S., Avila H., Turco S., Beverley S. Lipophosphoglycan is a virulence factor distinct from related glycoconjugates in the protozoan parasite Leishmania major. Proc. Natl Acad. Sci. 2000, 97:9258-9263.
    • (2000) Proc. Natl Acad. Sci. , vol.97 , pp. 9258-9263
    • Späth, G.1    Epstein, L.2    Leader, B.3    Singer, S.4    Avila, H.5    Turco, S.6    Beverley, S.7
  • 3
    • 0028789599 scopus 로고
    • Galactofuranose-containing glycoconjugates in trypanosomatids
    • de Lederkremer R., Colli W. Galactofuranose-containing glycoconjugates in trypanosomatids. Glycobiology 1995, 5:547-552.
    • (1995) Glycobiology , vol.5 , pp. 547-552
    • de Lederkremer, R.1    Colli, W.2
  • 4
    • 0028393188 scopus 로고
    • Novel structures of N-linked high-mannose type oligosaccharides containing alpha-d-galactofuranosyl linkages in Aspergillus niger alpha-d-glucosidase
    • Takayanagi T., Kimura A., Chiba S., Ajisaka K. Novel structures of N-linked high-mannose type oligosaccharides containing alpha-d-galactofuranosyl linkages in Aspergillus niger alpha-d-glucosidase. Carbohydr. Res. 1994, 256:149-158.
    • (1994) Carbohydr. Res. , vol.256 , pp. 149-158
    • Takayanagi, T.1    Kimura, A.2    Chiba, S.3    Ajisaka, K.4
  • 5
    • 0036045346 scopus 로고    scopus 로고
    • Current status and future development of antitubercular chemotherapy
    • Kremer L., Besra G. Current status and future development of antitubercular chemotherapy. Expert Opin. Invest. Drugs 2002, 11:1033-1049.
    • (2002) Expert Opin. Invest. Drugs , vol.11 , pp. 1033-1049
    • Kremer, L.1    Besra, G.2
  • 6
    • 70349554368 scopus 로고    scopus 로고
    • Chemistry and biology of galactofuranose-containing polysaccharides
    • Richards M.R., Lowary T.L. Chemistry and biology of galactofuranose-containing polysaccharides. ChemBioChem 2009, 10:1920-1938.
    • (2009) ChemBioChem , vol.10 , pp. 1920-1938
    • Richards, M.R.1    Lowary, T.L.2
  • 7
    • 33646726968 scopus 로고    scopus 로고
    • Expression, purification, and characterization of a galactofuranosyltransferase involved in Mycobacterium tuberculosis arabinogalactan biosynthesis
    • Rose N., Completo G., Lin S., McNeil M., Palcic M., Lowary T. Expression, purification, and characterization of a galactofuranosyltransferase involved in Mycobacterium tuberculosis arabinogalactan biosynthesis. J. Am. Chem. Soc. 2006, 128:6721-6729.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6721-6729
    • Rose, N.1    Completo, G.2    Lin, S.3    McNeil, M.4    Palcic, M.5    Lowary, T.6
  • 10
    • 2942705936 scopus 로고    scopus 로고
    • Efficient synthesis of a nucleoside-diphospho-exo-glycal displaying time-dependent inactivation of UDP-galactopyranose mutase
    • Caravano A., Vincent S., Sinaÿ P. Efficient synthesis of a nucleoside-diphospho-exo-glycal displaying time-dependent inactivation of UDP-galactopyranose mutase. Chem. Commun. (Cambridge) 2004, 1216-1217.
    • (2004) Chem. Commun. (Cambridge) , pp. 1216-1217
    • Caravano, A.1    Vincent, S.2    Sinaÿ, P.3
  • 11
    • 33947176612 scopus 로고    scopus 로고
    • Synthesis and analysis of substrate analogues for UDP-galactopyranose mutase: implication for an oxocarbenium ion intermediate in the catalytic mechanism
    • Itoh K., Huang Z., Liu H. Synthesis and analysis of substrate analogues for UDP-galactopyranose mutase: implication for an oxocarbenium ion intermediate in the catalytic mechanism. Org. Lett. 2007, 9:879-882.
    • (2007) Org. Lett. , vol.9 , pp. 879-882
    • Itoh, K.1    Huang, Z.2    Liu, H.3
  • 12
    • 0344407501 scopus 로고    scopus 로고
    • Potentiometric analysis of UDP-galactopyranose mutase: stabilization of the flavosemiquinone by substrate
    • Fullerton S., Daff S., Sanders D., Ingledew W., Whitfield C., Chapman S., Naismith J. Potentiometric analysis of UDP-galactopyranose mutase: stabilization of the flavosemiquinone by substrate. Biochemistry 2003, 42:2104-2109.
    • (2003) Biochemistry , vol.42 , pp. 2104-2109
    • Fullerton, S.1    Daff, S.2    Sanders, D.3    Ingledew, W.4    Whitfield, C.5    Chapman, S.6    Naismith, J.7
  • 13
    • 0033612742 scopus 로고    scopus 로고
    • Positional isotope exchange catalyzed by UDP-galactopyranose mutase
    • Barlow J., Girvin M., Blanchard J. Positional isotope exchange catalyzed by UDP-galactopyranose mutase. J. Am. Chem. Soc. 1999, 121:6968-6969.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 6968-6969
    • Barlow, J.1    Girvin, M.2    Blanchard, J.3
  • 14
    • 70449674082 scopus 로고    scopus 로고
    • Structural basis of substrate binding to UDP-galactopyranose mutase: crystal structures in the reduced and oxidized state complexed with UDP-galactopyranose and UDP
    • Partha S., van Straaten K., Sanders D. Structural basis of substrate binding to UDP-galactopyranose mutase: crystal structures in the reduced and oxidized state complexed with UDP-galactopyranose and UDP. J. Mol. Biol. 2009, 394:864-877.
    • (2009) J. Mol. Biol. , vol.394 , pp. 864-877
    • Partha, S.1    van Straaten, K.2    Sanders, D.3
  • 15
    • 70349620864 scopus 로고    scopus 로고
    • X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin
    • Gruber T., Westler W., Kiessling L., Forest K. X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin. Biochemistry 2009, 48:9171-9173.
    • (2009) Biochemistry , vol.48 , pp. 9171-9173
    • Gruber, T.1    Westler, W.2    Kiessling, L.3    Forest, K.4
  • 16
    • 34250211471 scopus 로고    scopus 로고
    • Site-directed mutagenesis of UDP-galactopyranose mutase reveals a critical role for the active-site, conserved arginine residues
    • Chad J., Sarathy K., Gruber T., Addala E., Kiessling L., Sanders D. Site-directed mutagenesis of UDP-galactopyranose mutase reveals a critical role for the active-site, conserved arginine residues. Biochemistry 2007, 46:6723-6732.
    • (2007) Biochemistry , vol.46 , pp. 6723-6732
    • Chad, J.1    Sarathy, K.2    Gruber, T.3    Addala, E.4    Kiessling, L.5    Sanders, D.6
  • 17
    • 41449091694 scopus 로고    scopus 로고
    • Investigation of binding of UDP-Galf and UDP-[3-F]Galf to UDP-galactopyranose mutase by STD-NMR spectroscopy, molecular dynamics, and CORCEMA-ST calculations
    • Yuan Y., Bleile D., Wen X., Sanders D., Itoh K., Liu H., Pinto B. Investigation of binding of UDP-Galf and UDP-[3-F]Galf to UDP-galactopyranose mutase by STD-NMR spectroscopy, molecular dynamics, and CORCEMA-ST calculations. J. Am. Chem. Soc. 2008, 130:3157-3168.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 3157-3168
    • Yuan, Y.1    Bleile, D.2    Wen, X.3    Sanders, D.4    Itoh, K.5    Liu, H.6    Pinto, B.7
  • 18
    • 61449147047 scopus 로고    scopus 로고
    • Substrate directs enzyme dynamics by bridging distal sites: UDP-galactopyranose mutase
    • Yao X., Bleile D., Yuan Y., Chao J., Sarathy K., Sanders D., et al. Substrate directs enzyme dynamics by bridging distal sites: UDP-galactopyranose mutase. Proteins 2009, 74:972-979.
    • (2009) Proteins , vol.74 , pp. 972-979
    • Yao, X.1    Bleile, D.2    Yuan, Y.3    Chao, J.4    Sarathy, K.5    Sanders, D.6
  • 19
    • 1542690351 scopus 로고
    • Phosphonates as analogs of natural phosphates
    • Engel R. Phosphonates as analogs of natural phosphates. Chem. Rev. 1977, 349-367.
    • (1977) Chem. Rev. , pp. 349-367
    • Engel, R.1
  • 20
    • 77949537262 scopus 로고    scopus 로고
    • Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF-3 rather than by phosphoranes
    • Baxter N., Bowler M., Alizadeh T., Cliff M., Hounslow A., Wu B., et al. Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF-3 rather than by phosphoranes. Proc. Natl Acad. Sci. 2010, 107:4555-4560.
    • (2010) Proc. Natl Acad. Sci. , vol.107 , pp. 4555-4560
    • Baxter, N.1    Bowler, M.2    Alizadeh, T.3    Cliff, M.4    Hounslow, A.5    Wu, B.6
  • 21
    • 33749857513 scopus 로고    scopus 로고
    • Fluorinated phosphonates: synthesis and biomedical application
    • Romanenko V., Kukhar V. Fluorinated phosphonates: synthesis and biomedical application. Chem. Rev. 2006, 106:3868-3935.
    • (2006) Chem. Rev. , vol.106 , pp. 3868-3935
    • Romanenko, V.1    Kukhar, V.2
  • 22
    • 70349191367 scopus 로고    scopus 로고
    • The alpha,alpha-difluorinated phosphonate l-pSer-analogue: an accessible chemical tool for studying kinase-dependent signal transduction
    • Panigrahi K., Eggen M., Maeng J., Shen Q., Berkowitz D. The alpha,alpha-difluorinated phosphonate l-pSer-analogue: an accessible chemical tool for studying kinase-dependent signal transduction. Chem. Biol. 2009, 16:928-936.
    • (2009) Chem. Biol. , vol.16 , pp. 928-936
    • Panigrahi, K.1    Eggen, M.2    Maeng, J.3    Shen, Q.4    Berkowitz, D.5
  • 23
    • 43049112098 scopus 로고    scopus 로고
    • Prodrugs of phosphates and phosphonates
    • Hecker S., Erion M. Prodrugs of phosphates and phosphonates. J. Med. Chem. 2008, 51:2328-2345.
    • (2008) J. Med. Chem. , vol.51 , pp. 2328-2345
    • Hecker, S.1    Erion, M.2
  • 24
    • 43049109229 scopus 로고    scopus 로고
    • Mechanisms of action of bisphosphonates: similarities and differences and their potential influence on clinical efficacy
    • Russell R., Watts N., Ebetino F., Rogers M. Mechanisms of action of bisphosphonates: similarities and differences and their potential influence on clinical efficacy. Osteoporosis Int. 2008, 19:733-759.
    • (2008) Osteoporosis Int. , vol.19 , pp. 733-759
    • Russell, R.1    Watts, N.2    Ebetino, F.3    Rogers, M.4
  • 25
    • 33745246850 scopus 로고    scopus 로고
    • X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues
    • Gordon R., Sivarajah P., Satkunarajah M., Ma D., Tarling C., Vizitiu D., et al. X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues. J. Mol. Biol. 2006, 360:67-79.
    • (2006) J. Mol. Biol. , vol.360 , pp. 67-79
    • Gordon, R.1    Sivarajah, P.2    Satkunarajah, M.3    Ma, D.4    Tarling, C.5    Vizitiu, D.6
  • 26
    • 64149126767 scopus 로고    scopus 로고
    • Synthesis of three C-glycoside analogues of UDP-galactopyranose as conformational probes for the mutase-catalyzed furanose/pyranose interconversion
    • Caravano A., Vincent S. Synthesis of three C-glycoside analogues of UDP-galactopyranose as conformational probes for the mutase-catalyzed furanose/pyranose interconversion. Eur. J. Org. Chem. 2009, 2009:1771-1780.
    • (2009) Eur. J. Org. Chem. , vol.2009 , pp. 1771-1780
    • Caravano, A.1    Vincent, S.2
  • 27
  • 30
    • 34147131735 scopus 로고    scopus 로고
    • Stereoselective chemical synthesis of sugar nucleotides via direct displacement of acylated glycosyl bromides
    • Timmons S., Jakeman D. Stereoselective chemical synthesis of sugar nucleotides via direct displacement of acylated glycosyl bromides. Org. Lett. 2007, 9:1227-1230.
    • (2007) Org. Lett. , vol.9 , pp. 1227-1230
    • Timmons, S.1    Jakeman, D.2
  • 31
    • 45049085548 scopus 로고    scopus 로고
    • Development of a coupled spectrophotometric assay for GlfT2, a bifunctional mycobacterial galactofuranosyltransferase
    • Rose N., Zheng R., Pearcey J., Zhou R., Completo G., Lowary T. Development of a coupled spectrophotometric assay for GlfT2, a bifunctional mycobacterial galactofuranosyltransferase. Carbohydr. Res. 2008, 343:2130-2139.
    • (2008) Carbohydr. Res. , vol.343 , pp. 2130-2139
    • Rose, N.1    Zheng, R.2    Pearcey, J.3    Zhou, R.4    Completo, G.5    Lowary, T.6
  • 32
    • 0038351058 scopus 로고    scopus 로고
    • Anhydride and halogenated-anhydride trihalogenacetic acid interaction with thymidine-5′-phosphate: ways to new activating reagents in nucleotide phosphorylation reactions
    • Bogachev V., Ulanov P. Anhydride and halogenated-anhydride trihalogenacetic acid interaction with thymidine-5′-phosphate: ways to new activating reagents in nucleotide phosphorylation reactions. Bioorg. Khim. 2003, 29:64-74.
    • (2003) Bioorg. Khim. , vol.29 , pp. 64-74
    • Bogachev, V.1    Ulanov, P.2
  • 33
    • 0035833723 scopus 로고    scopus 로고
    • Improved chemical synthesis of UDP-galactofuranose
    • Marlow A., Kiessling L. Improved chemical synthesis of UDP-galactofuranose. Org. Lett. 2001, 3:2517-2519.
    • (2001) Org. Lett. , vol.3 , pp. 2517-2519
    • Marlow, A.1    Kiessling, L.2
  • 34
    • 28744444216 scopus 로고    scopus 로고
    • An improved method for the synthesis of nucleoside triphosphate analogues
    • Mohamady S., Jakeman D. An improved method for the synthesis of nucleoside triphosphate analogues. J. Org. Chem. 2005, 70:10588-10591.
    • (2005) J. Org. Chem. , vol.70 , pp. 10588-10591
    • Mohamady, S.1    Jakeman, D.2
  • 35
    • 70349765004 scopus 로고    scopus 로고
    • A survey of chemical methods for sugar-nucleotide synthesis
    • Wagner G., Pesnot T., Field R. A survey of chemical methods for sugar-nucleotide synthesis. Nat. Prod. Rep. 2009, 26:1172-1194.
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 1172-1194
    • Wagner, G.1    Pesnot, T.2    Field, R.3
  • 36
    • 65349124747 scopus 로고    scopus 로고
    • Opportunities for enzyme engineering in natural product biosynthesis
    • Bernhardt P., O'Connor S. Opportunities for enzyme engineering in natural product biosynthesis. Curr. Opin. Chem. Biol. 2009, 13:35-42.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 35-42
    • Bernhardt, P.1    O'Connor, S.2
  • 38
    • 0034833650 scopus 로고    scopus 로고
    • Mechanistic investigation of UDP-galactopyranose mutase from Escherichia coli using 2- and 3-fluorinated UDP-galactofuranose as probes
    • Zhang Q., Liu H. Mechanistic investigation of UDP-galactopyranose mutase from Escherichia coli using 2- and 3-fluorinated UDP-galactofuranose as probes. J. Am. Chem. Soc. 2001, 123:6756-6766.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6756-6766
    • Zhang, Q.1    Liu, H.2
  • 39
    • 37049087186 scopus 로고
    • Synthesis of alpha-fluoroalkylphosphonates and gamma-fluoroalkylphosphonates
    • Blackburn G.M., Kent D.E. Synthesis of alpha-fluoroalkylphosphonates and gamma-fluoroalkylphosphonates. J. Chem. Soc. Perkin Trans. 1 1986, 913-917.
    • (1986) J. Chem. Soc. Perkin Trans. 1 , pp. 913-917
    • Blackburn, G.M.1    Kent, D.E.2
  • 41
    • 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., Frohlich R., Hanover J., Kirk K. 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. 2008, 343:189-195.
    • (2008) Carbohydr. Res. , vol.343 , pp. 189-195
    • Hajduch, J.1    Nam, G.2    Kim, E.3    Frohlich, R.4    Hanover, J.5    Kirk, K.6
  • 42
    • 77953104442 scopus 로고    scopus 로고
    • Halogenated β,γ-methylene- and ethylidene-dGTP-DNA ternary complexes with DNA polymerase β: structural evidence for stereospecific binding of the fluoromethylene analogues
    • Batra V.K., Pedersen L.C., Beard W.A., Wilson S.H., Kashemirov B.A., Upton T.G., et al. Halogenated β,γ-methylene- and ethylidene-dGTP-DNA ternary complexes with DNA polymerase β: structural evidence for stereospecific binding of the fluoromethylene analogues. J. Am. Chem. Soc. 2010, 132:7617-7625.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7617-7625
    • Batra, V.K.1    Pedersen, L.C.2    Beard, W.A.3    Wilson, S.H.4    Kashemirov, B.A.5    Upton, T.G.6
  • 44
    • 68649118360 scopus 로고    scopus 로고
    • Expression, purification and preliminary X-ray crystallographic analysis of UDP-galactopyranose mutase from Deinococcus radiodurans
    • Karunan Partha S., Bonderoff S., van Straaten K., Sanders D. Expression, purification and preliminary X-ray crystallographic analysis of UDP-galactopyranose mutase from Deinococcus radiodurans. Acta Crystallogr. Sect. F 2009, 65:843-845.
    • (2009) Acta Crystallogr. Sect. F , vol.65 , pp. 843-845
    • Karunan Partha, S.1    Bonderoff, S.2    van Straaten, K.3    Sanders, D.4
  • 45
    • 33747335931 scopus 로고    scopus 로고
    • Chemical probes of UDP-galactopyranose mutase
    • Carlson E., May J., Kiessling L. Chemical probes of UDP-galactopyranose mutase. Chem. Biol. 2006, 13:825-837.
    • (2006) Chem. Biol. , vol.13 , pp. 825-837
    • Carlson, E.1    May, J.2    Kiessling, L.3
  • 48
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath J. The finer things in X-ray diffraction data collection. Acta Crystallogr. Sect. D 1999, 55:1718-1725.
    • (1999) Acta Crystallogr. Sect. D , vol.55 , pp. 1718-1725
    • Pflugrath, J.1
  • 50
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.