메뉴 건너뛰기




Volumn 20, Issue 2, 2009, Pages 260-268

Trans-sialidase activity of Photobacterium damsela α2,6-sialyltransferase and its application in the synthesis of sialosides

Author keywords

Enzyme; Sialidase; Sialoside; Sialyltransferase; Trans sialidase

Indexed keywords

ALPHA 2,6 SIALYLTRANSFERASE; CYTIDINE 5 MONOPHOSPHATE; GLYCOSIDE; PHOSPHATE; SIALIDASE; SIALOSIDE; SIALYLTRANSFERASE; UNCLASSIFIED DRUG; BETA D GALACTOSIDE ALPHA 2 6 SIALYLTRANSFERASE; BETA-D-GALACTOSIDE ALPHA 2-6-SIALYLTRANSFERASE; GLYCOPROTEIN; N ACETYLNEURAMINIC ACID; TRANS SIALIDASE; TRANS-SIALIDASE;

EID: 77649221424     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwp172     Document Type: Article
Times cited : (55)

References (43)
  • 2
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary persepective
    • Angata T, Varki A. 2002. Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary persepective. Chem Rev. 102:439-469.
    • (2002) Chem Rev , vol.102 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 5
    • 0036809661 scopus 로고    scopus 로고
    • The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis
    • Buschiazzo A, Amaya MF, Cremona ML, Frasch AC, Alzari PM. 2002. The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis. Mol Cell. 10:757-768.
    • (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
  • 6
    • 0027319978 scopus 로고
    • Inhibition of CMP-N-acetylneuraminic acid: lactosylceramide sialyltransferase by nucleotides, nucleotide sugars and nucleotide dialdehydes
    • Cambron LD, Leskawa KC. 1993. Inhibition of CMP-N-acetylneuraminic acid: lactosylceramide sialyltransferase by nucleotides, nucleotide sugars and nucleotide dialdehydes. Biochem Biophys Res Commun. 193:585-590.
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 585-590
    • Cambron, L.D.1    Leskawa, K.C.2
  • 7
    • 0030843984 scopus 로고    scopus 로고
    • A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities
    • Campbell JA, Davies GJ, Bulone V, Henrissat B. 1997. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem J. 326(Pt 3):929-939.
    • (1997) Biochem J , vol.326 , Issue.PT 3 , pp. 929-939
    • Campbell, J.A.1    Davies, G.J.2    Bulone, V.3    Henrissat, B.4
  • 8
    • 37849002551 scopus 로고    scopus 로고
    • ′-monophosphate with alpha2,3-sialyl O-glycan-, glycolipid-, and macromolecule-based donors yields diverse sialylated products
    • Chandrasekaran EV, Xue J, Xia J, Locke RD, Matta KL, Neelamegham S. 2008. Reversible sialylation: synthesis of cytidine 5′-monophospho-N-acetylneuraminic acid from cytidine 5′-monophosphate with alpha2,3-sialyl O-glycan-, glycolipid-, and macromolecule-based donors yields diverse sialylated products. Biochemistry. 47:320-330.
    • (2008) Biochemistry , vol.47 , pp. 320-330
    • Chandrasekaran, E.V.1    Xue, J.2    Xia, J.3    Locke, R.D.4    Matta, K.L.5    Neelamegham, S.6
  • 9
    • 58249104082 scopus 로고    scopus 로고
    • Multifunctionality of Campylobacter jejuni sialyltransferase CstII: Characterization of GD3/GT3 oligosaccharide synthase, GD3 oligosaccharide sialidase, and trans-sialidase activities
    • Cheng J, Yu H, Lau K, Huang S, Chokhawala HA, Li Y, Tiwari VK, Chen X. 2008. Multifunctionality of Campylobacter jejuni sialyltransferase CstII: Characterization of GD3/GT3 oligosaccharide synthase, GD3 oligosaccharide sialidase, and trans-sialidase activities. Glycobiology. 18:686-697.
    • (2008) Glycobiology , vol.18 , pp. 686-697
    • Cheng, J.1    Yu, H.2    Lau, K.3    Huang, S.4    Chokhawala, H.A.5    Li, Y.6    Tiwari, V.K.7    Chen, X.8
  • 11
    • 33846927522 scopus 로고    scopus 로고
    • High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries
    • Chokhawala HA, Yu H, Chen X. 2007. High-throughput substrate specificity studies of sialidases by using chemoenzymatically synthesized sialoside libraries. Chembiochem. 8:194-201.
    • (2007) Chembiochem , vol.8 , pp. 194-201
    • Chokhawala, H.A.1    Yu, H.2    Chen, X.3
  • 12
    • 0027420552 scopus 로고
    • Trans-sialidase: A unique enzyme activity discovered in the protozoan Trypanosoma cruzi
    • Colli W. 1993. Trans-sialidase: A unique enzyme activity discovered in the protozoan Trypanosoma cruzi. FASEB J. 7:1257-1264.
    • (1993) FASEB J , vol.7 , pp. 1257-1264
    • Colli, W.1
  • 14
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho PM, Deleury E, Davies GJ, Henrissat B. 2003. An evolving hierarchical family classification for glycosyltransferases. J Mol Biol. 328:307-317.
    • (2003) J Mol Biol , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 15
    • 0027426946 scopus 로고
    • The surface trans-sialidase family of Trypanosoma cruzi
    • Cross GA, Takle GB. 1993. The surface trans-sialidase family of Trypanosoma cruzi. Annu Rev Microbiol. 47:385-411.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 385-411
    • Cross, G.A.1    Takle, G.B.2
  • 16
    • 40849118185 scopus 로고    scopus 로고
    • Kinetic and mechanistic analysis of Trypanosoma cruzi trans-sialidase reveals a classical ping-pong mechanism with acid/base catalysis
    • Damager I, Buchini S, Amaya MF, Buschiazzo A, Alzari P, Frasch AC, Watts A, Withers SG. 2008. Kinetic and mechanistic analysis of Trypanosoma cruzi trans-sialidase reveals a classical ping-pong mechanism with acid/base catalysis. Biochemistry. 47:3507-3512.
    • (2008) Biochemistry , vol.47 , pp. 3507-3512
    • Damager, I.1    Buchini, S.2    Amaya, M.F.3    Buschiazzo, A.4    Alzari, P.5    Frasch, A.C.6    Watts, A.7    Withers, S.G.8
  • 17
    • 0034234658 scopus 로고    scopus 로고
    • Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi
    • Frasch AC. 2000. Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi. Parasitol Today. 16:282-286.
    • (2000) Parasitol Today , vol.16 , pp. 282-286
    • Frasch, A.C.1
  • 18
    • 0037016699 scopus 로고    scopus 로고
    • The genetic bases for the variation in the lipo-oligosaccharide of the mucosal pathogen Campylobacter jejuni. Biosynthesis of sialylated ganglioside mimics in the core oligosaccharide
    • Gilbert M, Karwaski MF, Bernatchez S, Young NM, Taboada E, Michniewicz J, Cunningham AM, Wakarchuk WW. 2002. The genetic bases for the variation in the lipo-oligosaccharide of the mucosal pathogen, Campylobacter jejuni. Biosynthesis of sialylated ganglioside mimics in the core oligosaccharide. J Biol Chem. 277:327-337.
    • (2002) J Biol Chem , vol.277 , pp. 327-337
    • Gilbert, M.1    Karwaski, M.F.2    Bernatchez, S.3    Young, N.M.4    Taboada, E.5    Michniewicz, J.6    Cunningham, A.M.7    Wakarchuk, W.W.8
  • 19
    • 53049107996 scopus 로고    scopus 로고
    • Structural and functional studies of Strep-tococcus pneumoniae neuraminidase B: An intramolecular trans-sialidase
    • Gut H, King SJ, Walsh MA. 2008. Structural and functional studies of Strep-tococcus pneumoniae neuraminidase B: An intramolecular trans-sialidase. FEBS Lett. 582:3348-3352.
    • (2008) FEBS Lett , vol.582 , pp. 3348-3352
    • Gut, H.1    King, S.J.2    Walsh, M.A.3
  • 22
    • 2642558619 scopus 로고    scopus 로고
    • Synthesis of 2-[(2-pyridyl)amino]ethyl beta-D-lactosaminide and evaluation of its acceptor ability for sialyltransferase: A comparison with 4-methylumbelliferyl and dansyl beta-D-lactosaminide
    • Kajihara Y, Kamiyama D, Yamamoto N, Sakakibara T, Izumi M, Hashimoto H. 2004. Synthesis of 2-[(2-pyridyl)amino]ethyl beta-D-lactosaminide and evaluation of its acceptor ability for sialyltransferase: A comparison with 4-methylumbelliferyl and dansyl beta-D-lactosaminide. Carbohydr Res. 339:1545-1550.
    • (2004) Carbohydr Res , vol.339 , pp. 1545-1550
    • Kajihara, Y.1    Kamiyama, D.2    Yamamoto, N.3    Sakakibara, T.4    Izumi, M.5    Hashimoto, H.6
  • 23
    • 0000888809 scopus 로고    scopus 로고
    • A novel a-2,6-sialyltransferase: Transfer of sialic acid to fucosyl and sialyl trisaccharides
    • Kajihara Y, Yamamoto T, Nagae H, Nakashizuka M, Sakakibara T, Terada I. 1996. A novel a-2,6-sialyltransferase: Transfer of sialic acid to fucosyl and sialyl trisaccharides. J Org Chem. 61:8632-8635.
    • (1996) J Org Chem , vol.61 , pp. 8632-8635
    • Kajihara, Y.1    Yamamoto, T.2    Nagae, H.3    Nakashizuka, M.4    Sakakibara, T.5    Terada, I.6
  • 24
    • 37549044252 scopus 로고    scopus 로고
    • Crystal structure of Vibrionaceae Photobacterium sp. JT-ISH-224 alpha2,6-sialyltransferase in a ternary complex with donor product CMP and acceptor substrate lactose: Catalytic mechanism and substrate recognition
    • Kakuta Y, Okino N, Kajiwara H, Ichikawa M, Takakura Y, Ito M, Yamamoto T. 2008. Crystal structure of Vibrionaceae Photobacterium sp. JT-ISH-224 alpha2,6-sialyltransferase in a ternary complex with donor product CMP and acceptor substrate lactose: Catalytic mechanism and substrate recognition. Glycobiology. 18:66-73.
    • (2008) Glycobiology , vol.18 , pp. 66-73
    • Kakuta, Y.1    Okino, N.2    Kajiwara, H.3    Ichikawa, M.4    Takakura, Y.5    Ito, M.6    Yamamoto, T.7
  • 25
    • 33846225189 scopus 로고    scopus 로고
    • Alternative donor substrates for inverting and retaining glycosyltransferases
    • Lairson LL, Wakarchuk WW, Withers SG. 2007. Alternative donor substrates for inverting and retaining glycosyltransferases. Chem Commun. 4:365-367.
    • (2007) Chem Commun , vol.4 , pp. 365-367
    • Lairson, L.L.1    Wakarchuk, W.W.2    Withers, S.G.3
  • 27
    • 0031440882 scopus 로고    scopus 로고
    • Temperature differences for trans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Try-panosomacruzi trans-sialidase
    • Ribeirao M, Pereira-Chioccola VL, Eichinger D, Rodrigues MM, Schenkman S. 1997. Temperature differences for trans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Try-panosomacruzi trans-sialidase. Glycobiology. 7:1237-1246.
    • (1997) Glycobiology , vol.7 , pp. 1237-1246
    • Ribeirao, M.1    Pereira-Chioccola, V.L.2    Eichinger, D.3    Rodrigues, M.M.4    Schenkman, S.5
  • 28
    • 0025713971 scopus 로고
    • ′-one, a new substrate for neuraminidase assay
    • ′one, a new substrate for neuraminidase assay. Carbohydr Res. 196:29-40.
    • (1990) Carbohydr Res , vol.196 , pp. 29-40
    • Rothermel, J.1    Faillard, H.2
  • 29
    • 0034444960 scopus 로고    scopus 로고
    • Achievements and challenges of sialic acid research
    • Schauer R. 2000. Achievements and challenges of sialic acid research. Glycoconj J. 17:485-499.
    • (2000) Glycoconj J , vol.17 , pp. 485-499
    • Schauer, R.1
  • 30
    • 0025769326 scopus 로고
    • A novel cell surface trans-sialidase of Trypanosoma cruzi generates a stage-specific epitope required for invasion of mammalian cells
    • Schenkman S, Jiang MS, Hart GW, Nussenzweig V. 1991. A novel cell surface trans-sialidase of Trypanosoma cruzi generates a stage-specific epitope required for invasion of mammalian cells. Cell. 65:1117-1125.
    • (1991) Cell , vol.65 , pp. 1117-1125
    • Schenkman, S.1    Jiang, M.S.2    Hart, G.W.3    Nussenzweig, V.4
  • 31
    • 0027314040 scopus 로고
    • Enzymatic characterization of beta-D-galactoside alpha 23-trans-sialidase from Trypanosoma cruzi
    • Scudder P, Doom JP, Chuenkova M, Manger ID, Pereira ME. 1993. Enzymatic characterization of beta-D-galactoside alpha 2,3-trans-sialidase from Trypanosoma cruzi. J Biol Chem. 268:9886-9891.
    • (1993) J Biol Chem , vol.268 , pp. 9886-9891
    • Scudder, P.1    Doom, J.P.2    Chuenkova, M.3    Manger, I.D.4    Pereira, M.E.5
  • 32
    • 77949882540 scopus 로고
    • Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary persepective
    • Segel IH 1975. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems. New York: Wiley.
    • (1975) Chem Rev
    • Segel, I.H.1    Angata, T.2    Varki, A.3
  • 33
    • 0033520837 scopus 로고    scopus 로고
    • Expression of alpha2,8/2,9-polysialyltransferase from Escherichia coli K92. Characterization of the enzyme and its reaction products
    • Shen GJ, Datta AK, Izumi M, Koeller KM, Wong CH. 1999. Expression of alpha2,8/2,9-polysialyltransferase from Escherichia coli K92. Characterization of the enzyme and its reaction products. J Biol Chem. 274:35139-35146.
    • (1999) J Biol Chem. , vol.274 , pp. 35139-35146
    • Shen, G.J.1    Datta, A.K.2    Izumi, M.3    Koeller, K.M.4    Wong, C.H.5
  • 34
    • 43149109297 scopus 로고    scopus 로고
    • N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela alpha2,6-sialyltransferase
    • Sun M, Li Y, Chokhawala HA, Henning R, Chen X. 2008. N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela alpha2,6-sialyltransferase. Biotechnol Lett. 30:671-676.
    • (2008) Biotechnol Lett. , vol.30 , pp. 671-676
    • Sun, M.1    Li, Y.2    Chokhawala, H.A.3    Henning, R.4    Chen, X.5
  • 35
    • 20544463930 scopus 로고    scopus 로고
    • Synthesis of sialyl TN glycopeptides - Enzymatic sialylation by á2,6-sialyltransferase from Photobacterium damsela
    • Teo C, Hwang T, Chen P, Hung C, Gao H, Chang L, Lin C. 2005. Synthesis of sialyl TN glycopeptides - Enzymatic sialylation by á2,6-sialyltransferase from Photobacterium damsela. Adv Synth Catal. 347:967-972.
    • (2005) Adv Synth Catal. , vol.347 , pp. 967-972
    • Teo, C.1    Hwang, T.2    Chen, P.3    Hung, C.4    Gao, H.5    Chang, L.6    Lin, C.7
  • 36
    • 0029854379 scopus 로고    scopus 로고
    • Systematic nomenclature for sialyltransferases
    • Tsuji S, Datta AK, Paulson JC. 1996. Systematic nomenclature for sialyltransferases. Glycobiology. 6:v-vii.
    • (1996) Glycobiology , vol.6
    • Tsuji, S.1    Datta, A.K.2    Paulson, J.C.3
  • 37
    • 39049097535 scopus 로고    scopus 로고
    • Photobacterium sp. JTISH-224 produces two sialyltransferases, alpha-/beta-galactoside alpha2,3-sialyltransferase and beta-galactoside alpha2,6-sialyltransferase
    • Tsukamoto H, Takakura Y,Mine T, Yamamoto T. 2008. Photobacterium sp. JTISH-224 produces two sialyltransferases, alpha-/beta-galactoside alpha2,3-sialyltransferase and beta-galactoside alpha2,6-sialyltransferase. J Biochem. 143:187-197.
    • (2008) J Biochem. , vol.143 , pp. 187-197
    • Tsukamoto, H.1    Takakura, Y.2    Mine, T.3    Yamamoto, T.4
  • 38
    • 0031913180 scopus 로고    scopus 로고
    • Cloning and expression of a marine bacterial beta-galactoside alpha2,6-sialyltransferase gene from Photobacterium damsela JT0160
    • Yamamoto T, Nakashizuka M, Terada I. 1998. Cloning and expression of a marine bacterial beta-galactoside alpha2,6-sialyltransferase gene from Photobacterium damsela JT0160. J Biochem. 123:94-100.
    • (1998) J Biochem. , vol.123 , pp. 94-100
    • Yamamoto, T.1    Nakashizuka, M.2    Terada, I.3
  • 39
    • 0034673856 scopus 로고    scopus 로고
    • Primary 13C and beta-secondary 2H KIEs for trans-sialidase. A snapshot of nucleophilic participation during catalysis
    • Yang J, Schenkman S, Horenstein BA. 2000. Primary 13C and beta-secondary 2H KIEs for trans-sialidase. A snapshot of nucleophilic participation during catalysis. Biochemistry. 39:5902-5910.
    • (2000) Biochemistry , vol.39 , pp. 5902-5910
    • Yang, J.1    Schenkman, S.2    Horenstein, B.A.3
  • 40
    • 33847755495 scopus 로고    scopus 로고
    • Carbohydrate post-glycosylational modifications
    • Yu H, Chen X. 2007. Carbohydrate post-glycosylational modifications. Org Biomol Chem. 5:865-872.
    • (2007) Org Biomol Chem. , vol.5 , pp. 865-872
    • Yu, H.1    Chen, X.2
  • 41
    • 29344431622 scopus 로고    scopus 로고
    • A multifunctional Pasteurella multocida sialyltransferase: A powerful tool for the synthesis of sialoside libraries
    • Yu H, Chokhawala H, Karpel R, Yu H, Wu B, Zhang J, Zhang Y, Jia Q, Chen X. 2005. A multifunctional Pasteurella multocida sialyltransferase: A powerful tool for the synthesis of sialoside libraries. J Am Chem Soc. 127:17618-17619.
    • (2005) J Am Chem Soc. , vol.127 , pp. 17618-17619
    • Yu, H.1    Chokhawala, H.2    Karpel, R.3    Yu, H.4    Wu, B.5    Zhang, J.6    Zhang, Y.7    Jia, Q.8    Chen, X.9
  • 42
    • 33746302579 scopus 로고    scopus 로고
    • Highly efficient chemoenzymatic synthesis of naturally occurring and non-natural alpha-2,6-linked sialosides: A P. damsela alpha-2,6-sialyltransferase with extremely flexible donor-substrate specificity
    • Yu H, Huang S, Chokhawala H, Sun M, Zheng H, Chen X. 2006. Highly efficient chemoenzymatic synthesis of naturally occurring and non-natural alpha-2,6-linked sialosides: A P. damsela alpha-2,6-sialyltransferase with extremely flexible donor-substrate specificity. Angew Chem Int Ed Engl. 45:3938-3944.
    • (2006) Angew Chem Int Ed Engl. , vol.45 , pp. 3938-3944
    • Yu, H.1    Huang, S.2    Chokhawala, H.3    Sun, M.4    Zheng, H.5    Chen, X.6
  • 43
    • 33748302743 scopus 로고    scopus 로고
    • Exploiting the reversibility of natural product glycosyltransferase-catalyzed reactions
    • Science
    • Zhang C,Griffith BR, Fu Q, Albermann C, Fu X, Lee IK, Li L, Thorson JS. 2006. Exploiting the reversibility of natural product glycosyltransferase-catalyzed reactions. Science. 313:1291-1294.
    • (2006) , vol.313 , pp. 1291-1294
    • Zhang, C.1    Griffith, B.R.2    Fu, Q.3    Albermann, C.4    Fu, X.5    Lee, I.K.6    Li, L.7    Thorson, J.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.