메뉴 건너뛰기




Volumn 404, Issue 2, 2010, Pages 247-259

Structural Insights on the New Mechanism of Trehalose Synthesis by Trehalose Synthase TreT from Pyrococcus horikoshii

Author keywords

Glycosyltransferase; Pyrococcus horikoshii; Trehalose synthase; TreT; X ray structure

Indexed keywords

GLYCOSYLTRANSFERASE; TREHALASE; TREHALOSE; TREHALOSE SYNTHASE; UNCLASSIFIED DRUG;

EID: 78349313324     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.09.056     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 0035968318 scopus 로고    scopus 로고
    • Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals
    • Benaroudj N., Lee D.H., Goldberg A.L. Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals. J. Biol. Chem. 2001, 276:24261-24267.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24261-24267
    • Benaroudj, N.1    Lee, D.H.2    Goldberg, A.L.3
  • 3
    • 0016305880 scopus 로고
    • The metabolism of alpha,alpha-trehalose
    • Elbein A.D. The metabolism of alpha,alpha-trehalose. Adv. Carbohydr. Chem. Biochem. 1974, 30:227-256.
    • (1974) Adv. Carbohydr. Chem. Biochem. , vol.30 , pp. 227-256
    • Elbein, A.D.1
  • 5
    • 18744415120 scopus 로고    scopus 로고
    • Trehalose-phosphate synthase of Mycobacterium tuberculosis. Cloning, expression and properties of the recombinant enzyme
    • Pan Y.T., Carroll J.D., Elbein A.D. Trehalose-phosphate synthase of Mycobacterium tuberculosis. Cloning, expression and properties of the recombinant enzyme. Eur. J. Biochem. 2002, 269:6091-6100.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 6091-6100
    • Pan, Y.T.1    Carroll, J.D.2    Elbein, A.D.3
  • 6
    • 0036909547 scopus 로고    scopus 로고
    • Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA
    • Gibson R.P., Turkenburg J.P., Charnock S.J., Lloyd R., Davies G.J. Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA. Chem. Biol. 2002, 9:1337-1346.
    • (2002) Chem. Biol. , vol.9 , pp. 1337-1346
    • Gibson, R.P.1    Turkenburg, J.P.2    Charnock, S.J.3    Lloyd, R.4    Davies, G.J.5
  • 10
    • 0030573162 scopus 로고    scopus 로고
    • Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius
    • Maruta K., Mitsuzumi H., Nakada T., Kubota M., Chaen H., Fukuda S., et al. Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius. Biochim. Biophys. Acta 1996, 1291:177-181.
    • (1996) Biochim. Biophys. Acta , vol.1291 , pp. 177-181
    • Maruta, K.1    Mitsuzumi, H.2    Nakada, T.3    Kubota, M.4    Chaen, H.5    Fukuda, S.6
  • 12
    • 9144221530 scopus 로고    scopus 로고
    • TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis
    • Qu Q., Lee S.J., Boos W. TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 2004, 279:47890-47897.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47890-47897
    • Qu, Q.1    Lee, S.J.2    Boos, W.3
  • 13
    • 14644387569 scopus 로고    scopus 로고
    • A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization
    • Ryu S.I., Park C.S., Cha J., Woo E.J., Lee S.B. A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. Biochem. Biophys. Res. Commun. 2005, 329:429-436.
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , pp. 429-436
    • Ryu, S.I.1    Park, C.S.2    Cha, J.3    Woo, E.J.4    Lee, S.B.5
  • 14
    • 49749149995 scopus 로고    scopus 로고
    • A novel trehalose synthesizing pathway in the hyperthermophilic Crenarchaeon Thermoproteus tenax: the unidirectional TreT pathway
    • Kouril T., Zaparty M., Marrero J., Brinkmann H., Siebers B. A novel trehalose synthesizing pathway in the hyperthermophilic Crenarchaeon Thermoproteus tenax: the unidirectional TreT pathway. Arch. Microbiol. 2008, 190:355-369.
    • (2008) Arch. Microbiol. , vol.190 , pp. 355-369
    • Kouril, T.1    Zaparty, M.2    Marrero, J.3    Brinkmann, H.4    Siebers, B.5
  • 15
    • 57349146679 scopus 로고    scopus 로고
    • A unique combination of genetic systems for the synthesis of trehalose in Rubrobacter xylanophilus: properties of a rare actinobacterial TreT
    • Nobre A., Alarico S., Fernandes C., Empadinhas N., da Costa M.S. A unique combination of genetic systems for the synthesis of trehalose in Rubrobacter xylanophilus: properties of a rare actinobacterial TreT. J. Bacteriol. 2008, 190:7939-7946.
    • (2008) J. Bacteriol. , vol.190 , pp. 7939-7946
    • Nobre, A.1    Alarico, S.2    Fernandes, C.3    Empadinhas, N.4    da Costa, M.S.5
  • 18
    • 11844280851 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in glycosyltransferases
    • Qasba P.K., Ramakrishnan B., Boeggeman E. Substrate-induced conformational changes in glycosyltransferases. Trends Biochem. Sci. 2005, 30:53-62.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 53-62
    • Qasba, P.K.1    Ramakrishnan, B.2    Boeggeman, E.3
  • 19
    • 0029779716 scopus 로고    scopus 로고
    • High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis
    • Xavier K.B., Martins L.O., Peist R., Kossmann M., Boos W., Santos H. High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis. J. Bacteriol. 1996, 178:4773-4777.
    • (1996) J. Bacteriol. , vol.178 , pp. 4773-4777
    • Xavier, K.B.1    Martins, L.O.2    Peist, R.3    Kossmann, M.4    Boos, W.5    Santos, H.6
  • 20
    • 35448957702 scopus 로고    scopus 로고
    • Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase: inhibitory effects on several disaccharidase activities
    • Kim H.M., Chang Y.K., Ryu S.I., Moon S.G., Lee S.B. Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase: inhibitory effects on several disaccharidase activities. J. Mol. Catal. B: Enzym. 2007, 49:98-103.
    • (2007) J. Mol. Catal. B: Enzym. , vol.49 , pp. 98-103
    • Kim, H.M.1    Chang, Y.K.2    Ryu, S.I.3    Moon, S.G.4    Lee, S.B.5
  • 21
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 1993, 233:123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 22
    • 57349141414 scopus 로고    scopus 로고
    • Crystal structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558
    • Ruane K.M., Davies G.J., Martinez-Fleites C. Crystal structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. Proteins 2008, 73:784-787.
    • (2008) Proteins , vol.73 , pp. 784-787
    • Ruane, K.M.1    Davies, G.J.2    Martinez-Fleites, C.3
  • 23
    • 0034938546 scopus 로고    scopus 로고
    • Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics
    • Mulichak A.M., Losey H.C., Walsh C.T., Garavito R.M. Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics. Structure 2001, 9:547-557.
    • (2001) Structure , vol.9 , pp. 547-557
    • Mulichak, A.M.1    Losey, H.C.2    Walsh, C.T.3    Garavito, R.M.4
  • 24
    • 0033623762 scopus 로고    scopus 로고
    • The 1.9 Å crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis
    • Ha S., Walker D., Shi Y., Walker S. The 1.9 Å crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis. Protein Sci. 2000, 9:1045-1052.
    • (2000) Protein Sci. , vol.9 , pp. 1045-1052
    • Ha, S.1    Walker, D.2    Shi, Y.3    Walker, S.4
  • 25
    • 0037417869 scopus 로고    scopus 로고
    • Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases
    • Hu Y., Chen L., Ha S., Gross B., Falcone B., Walker D., et al. Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. Proc. Natl Acad. Sci. USA 2003, 100:845-849.
    • (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
  • 26
    • 4444373841 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation
    • Buschiazzo A., Ugalde J.E., Guerin M.E., Shepard W., Ugalde R.A., Alzari P.M. Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation. EMBO J. 2004, 23:3196-3205.
    • (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
  • 27
    • 33646338642 scopus 로고    scopus 로고
    • Crystal structure of an archaeal glycogen synthase: insights into oligomerization and substrate binding of eukaryotic glycogen synthases
    • Horcajada C., Guinovart J.J., Fita I., Ferrer J.C. Crystal structure of an archaeal glycogen synthase: insights into oligomerization and substrate binding of eukaryotic glycogen synthases. J. Biol. Chem. 2006, 281:2923-2931.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2923-2931
    • Horcajada, C.1    Guinovart, J.J.2    Fita, I.3    Ferrer, J.C.4
  • 28
    • 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 2 Å resolution
    • Gibson R.P., Tarling C.A., Roberts S., Withers S.G., Davies G.J. The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 Å resolution. J. Biol. Chem. 2004, 279:1950-1955.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1950-1955
    • Gibson, R.P.1    Tarling, C.A.2    Roberts, S.3    Withers, S.G.4    Davies, G.J.5
  • 29
    • 17644373124 scopus 로고    scopus 로고
    • The OtsAB pathway is essential for trehalose biosynthesis in Mycobacterium tuberculosis
    • Murphy H.N., Stewart G.R., Mischenko V.V., Apt A.S., Harris R., McAlister M.S., et al. The OtsAB pathway is essential for trehalose biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 2005, 280:14524-14529.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14524-14529
    • Murphy, H.N.1    Stewart, G.R.2    Mischenko, V.V.3    Apt, A.S.4    Harris, R.5    McAlister, M.S.6
  • 30
    • 78650252130 scopus 로고    scopus 로고
    • Catalytic reversibility of Pyrococcus horikoshii trehalose synthase: efficient synthesis of several nucleoside diphosphate glucoses with enzyme recycling
    • Ryu S.-I., Kim J.-E., Kim E.-J., Chung S.-K., Lee S.-B. Catalytic reversibility of Pyrococcus horikoshii trehalose synthase: efficient synthesis of several nucleoside diphosphate glucoses with enzyme recycling. Process Biochem. 2010, 10.1016/j.procbio.2010.07.030.
    • (2010) Process Biochem.
    • Ryu, S.-I.1    Kim, J.-E.2    Kim, E.-J.3    Chung, S.-K.4    Lee, S.-B.5
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 1993, 231:1049-1067.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.