메뉴 건너뛰기




Volumn 194, Issue 16, 2012, Pages 4260-4271

Synthesis of long-chain chitooligosaccharides by a hypertransglycosylating processive endochitinase of Serratia proteamaculans 568

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CHITIN; CHITINASE; CHITOBIOSE; LONG CHAIN CHITOOLIGOSACCHARIDE; N ACETYLGLUCOSAMINE; OLIGOSACCHARIDE; SPCHID PROTEIN; UNCLASSIFIED DRUG;

EID: 84866334862     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06473-11     Document Type: Article
Times cited : (64)

References (50)
  • 1
    • 17044455396 scopus 로고    scopus 로고
    • Transglycosidase activity of chitotriosidase: improved enzymatic assay for the human macrophage chitinase
    • Aguilera B, et al. 2003. Transglycosidase activity of chitotriosidase: improved enzymatic assay for the human macrophage chitinase. J. Biol. Chem. 278:40911-40916.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40911-40916
    • Aguilera, B.1
  • 3
    • 49749153849 scopus 로고
    • The chitinase system of a strain of Streptomyces griseus
    • Berger LR, Reynolds DM. 1958. The chitinase system of a strain of Streptomyces griseus. Biochim. Biophys. Acta 29:522-534.
    • (1958) Biochim. Biophys. Acta , vol.29 , pp. 522-534
    • Berger, L.R.1    Reynolds, D.M.2
  • 5
    • 3543091560 scopus 로고    scopus 로고
    • Two-step purification of Bacillus circulans chitinase A1 expressed in Escherichia coli periplasm
    • Chen CT, Huang CJ, Wang YH, Chen CY. 2004. Two-step purification of Bacillus circulans chitinase A1 expressed in Escherichia coli periplasm. Protein Expr. Purif. 37:27-31.
    • (2004) Protein Expr. Purif. , vol.37 , pp. 27-31
    • Chen, C.T.1    Huang, C.J.2    Wang, Y.H.3    Chen, C.Y.4
  • 7
    • 0027968302 scopus 로고
    • The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei
    • Divne C, et al. 1994. The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science 265:524-528.
    • (1994) Science , vol.265 , pp. 524-528
    • Divne, C.1
  • 8
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50 å long tunnel of cellobiohydrolase I from Trichoderma reesei
    • Divne C, Ståhlberg J, Teeri TT, Jones TA. 1998. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 å long tunnel of cellobiohydrolase I from Trichoderma reesei. J. Mol. Biol. 275:309-325.
    • (1998) J. Mol. Biol. , vol.275 , pp. 309-325
    • Divne, C.1    Ståhlberg, J.2    Teeri, T.T.3    Jones, T.A.4
  • 9
    • 84856845043 scopus 로고    scopus 로고
    • Human chitotriosidase-catalyzed hydrolysis of chitosan
    • Eide KB, et al. 2012. Human chitotriosidase-catalyzed hydrolysis of chitosan. Biochemistry 51:487-495.
    • (2012) Biochemistry , vol.51 , pp. 487-495
    • Eide, K.B.1
  • 10
    • 80053134490 scopus 로고    scopus 로고
    • Chitinases from Autographa californica multiplepolyhedranvirus: rapid purification from SF-9 medium and mode of action
    • Fukamizo T, et al. 2011. Chitinases from Autographa californica multiplepolyhedranvirus: rapid purification from SF-9 medium and mode of action. Biosci. Biotechnol. Biochem. 75:1763-1769.
    • (2011) Biosci. Biotechnol. Biochem. , vol.75 , pp. 1763-1769
    • Fukamizo, T.1
  • 11
    • 0037067670 scopus 로고    scopus 로고
    • Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins
    • Fusetti F, et al. 2002. Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins. J. Biol. Chem. 277:25537-25544.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25537-25544
    • Fusetti, F.1
  • 12
    • 77955841193 scopus 로고    scopus 로고
    • Chitooligosaccharide sensing and downstream signaling: contrasted outcomes in pathogenic and beneficial plantmicrobe interactions
    • Hamel LP, Beaudoin N. 2010. Chitooligosaccharide sensing and downstream signaling: contrasted outcomes in pathogenic and beneficial plantmicrobe interactions. Planta 232:787-806.
    • (2010) Planta , vol.232 , pp. 787-806
    • Hamel, L.P.1    Beaudoin, N.2
  • 13
    • 2542475295 scopus 로고    scopus 로고
    • Mutation of active site residues in the chitinbinding domain ChBDChiA1 from chitinase A1 of Bacillus circulans alters substrate specificity: use of a green fluorescent protein binding assay
    • Hardt M, Laine RA. 2004. Mutation of active site residues in the chitinbinding domain ChBDChiA1 from chitinase A1 of Bacillus circulans alters substrate specificity: use of a green fluorescent protein binding assay. Arch. Biochem. Biophys. 426:286-297.
    • (2004) Arch. Biochem. Biophys. , vol.426 , pp. 286-297
    • Hardt, M.1    Laine, R.A.2
  • 14
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat B, Davies G. 1997. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7:637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 15
    • 33644935876 scopus 로고    scopus 로고
    • Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens
    • Horn SJ, et al. 2006. Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens. FEBS J. 273:491-503.
    • (2006) FEBS J. , vol.273 , pp. 491-503
    • Horn, S.J.1
  • 16
    • 11144238616 scopus 로고    scopus 로고
    • High-level expression and characterization of two chitinases, ChiCH and ChiCW, of Bacillus cereus 28-9 in Escherichia coli
    • Huang CJ, Chen CY. 2005. High-level expression and characterization of two chitinases, ChiCH and ChiCW, of Bacillus cereus 28-9 in Escherichia coli. Biochem. Biophys. Res. Commun. 327:8-17.
    • (2005) Biochem. Biophys. Res. Commun. , vol.327 , pp. 8-17
    • Huang, C.J.1    Chen, C.Y.2
  • 17
    • 0001251702 scopus 로고
    • Synthesis of 4-methylcoumarin-7-yloxy tetra-N-acetyl-β-chitotetraoside, a novel synthetic substrate for the fluorometric assay of lysozyme
    • Inaba T, Ohgusi T, Iga Y, Hasegawa E. 1984. Synthesis of 4-methylcoumarin-7-yloxy tetra-N-acetyl-β-chitotetraoside, a novel synthetic substrate for the fluorometric assay of lysozyme. Chem. Pharm. Bull. 32:1597-1603.
    • (1984) Chem. Pharm. Bull. , vol.32 , pp. 1597-1603
    • Inaba, T.1    Ohgusi, T.2    Iga, Y.3    Hasegawa, E.4
  • 18
    • 1842813472 scopus 로고    scopus 로고
    • Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding
    • Johansson P, et al. 2004. Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding. Plant Cell 16:874-886.
    • (2004) Plant Cell , vol.16 , pp. 874-886
    • Johansson, P.1
  • 19
    • 33645090163 scopus 로고    scopus 로고
    • Three-dimensional crystal structure and enzymatic characterization of β-mannanase Man5A from blue mussel Mytilus edulis
    • Larsson AM, et al. 2006. Three-dimensional crystal structure and enzymatic characterization of β-mannanase Man5A from blue mussel Mytilus edulis. J. Mol. Biol. 357:1500-1510.
    • (2006) J. Mol. Biol. , vol.357 , pp. 1500-1510
    • Larsson, A.M.1
  • 20
    • 0038070162 scopus 로고    scopus 로고
    • Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: the role of alanine 230 in acceptor subsite +1
    • Leemhuis H, et al. 2003. Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: the role of alanine 230 in acceptor subsite +1. Biochemistry 42:7518-7526.
    • (2003) Biochemistry , vol.42 , pp. 7518-7526
    • Leemhuis, H.1
  • 21
    • 0036684594 scopus 로고    scopus 로고
    • Simulation of hyaluronidase reaction involving hydrolysis, transglycosylation and condensation
    • Nakatani H, Monte C. 2002. Simulation of hyaluronidase reaction involving hydrolysis, transglycosylation and condensation. Biochem. J. 365:701-705.
    • (2002) Biochem. J. , vol.365 , pp. 701-705
    • Nakatani, H.1    Monte, C.2
  • 22
    • 77956067561 scopus 로고    scopus 로고
    • Biotechnological approaches to develop bacterial chitinases as a bioshield against fungal diseases of plants
    • Neeraja C, et al. 2010. Biotechnological approaches to develop bacterial chitinases as a bioshield against fungal diseases of plants. Crit. Rev. Biotechnol. 30:231-241.
    • (2010) Crit. Rev. Biotechnol. , vol.30 , pp. 231-241
    • Neeraja, C.1
  • 23
    • 76049087800 scopus 로고    scopus 로고
    • Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13
    • Neeraja C, Moerschbacher B, Podile AR. 2010. Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13. Bioresour. Technol. 101:3635-3641.
    • (2010) Bioresour. Technol. , vol.101 , pp. 3635-3641
    • Neeraja, C.1    Moerschbacher, B.2    Podile, A.R.3
  • 24
    • 77954569121 scopus 로고    scopus 로고
    • Swapping the chitin-binding domain in Bacillus chitinases improves the substrate binding affinity and conformational stability
    • Neeraja C, Subramanyam R, Moerschbacher B, Podile AR. 2010. Swapping the chitin-binding domain in Bacillus chitinases improves the substrate binding affinity and conformational stability. Mol. Biosyst. 6:1492-1502.
    • (2010) Mol. Biosyst. , vol.6 , pp. 1492-1502
    • Neeraja, C.1    Subramanyam, R.2    Moerschbacher, B.3    Podile, A.R.4
  • 25
    • 17444406353 scopus 로고    scopus 로고
    • Roles of four chitinases (ChiA, ChiB, ChiC, and ChiD) in the chitin degradation system of marine bacterium Alteromonas sp. strain O-7
    • Orikoshi H, et al. 2005. Roles of four chitinases (ChiA, ChiB, ChiC, and ChiD) in the chitin degradation system of marine bacterium Alteromonas sp. strain O-7. Appl. Environ. Microbiol. 71:1811-1815.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1811-1815
    • Orikoshi, H.1
  • 26
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein?
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. 1995. How to measure and predict the molar absorption coefficient of a protein? Protein Sci. 4:2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 27
    • 84860733560 scopus 로고    scopus 로고
    • Chitin binding proteins act synergistically with chitinases in Serratia proteamaculans 568
    • doi:10.1371/journal.pone.0036714
    • Purushotham P, Arun PVPS, Prakash JSS, Podile AR. 2012. Chitin binding proteins act synergistically with chitinases in Serratia proteamaculans 568. PLoS One 7:e36714. doi:10.1371/journal.pone.0036714.
    • (2012) PLoS One , vol.7
    • Purushotham, P.1    Arun, P.V.P.S.2    Prakash, J.S.S.3    Podile, A.R.4
  • 28
    • 84859218754 scopus 로고    scopus 로고
    • Multiple chitinases of an endophytic Serratia proteamaculans 568 generate chitin oligomers
    • Purushotham P, Sarma PVSRN, Podile AR. 2012. Multiple chitinases of an endophytic Serratia proteamaculans 568 generate chitin oligomers. Bioresour. Technol. 112:261-269.
    • (2012) Bioresour. Technol. , vol.112 , pp. 261-269
    • Purushotham, P.1    Sarma, P.V.S.R.N.2    Podile, A.R.3
  • 29
    • 0025182502 scopus 로고
    • Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei
    • Rouvinen J, Bergfors T, Teeri T, Knowles JK, Jones TA. 1990. Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science 249:380-386.
    • (1990) Science , vol.249 , pp. 380-386
    • Rouvinen, J.1    Bergfors, T.2    Teeri, T.3    Knowles, J.K.4    Jones, T.A.5
  • 30
    • 84873725307 scopus 로고    scopus 로고
    • Production of oligosaccharides in microbes
    • In J. P. Kamerling (ed), Elsevier, Philadelphia, PA
    • Samain, E. 2007. Production of oligosaccharides in microbes, p. 923. In J. P. Kamerling (ed), Comprehensive glycoscience, vol. 1. Elsevier, Philadelphia, PA.
    • (2007) Comprehensive glycoscience , vol.1 , pp. 923
    • Samain, E.1
  • 32
    • 77952314594 scopus 로고    scopus 로고
    • Glycoconjugates as elicitors or suppressors of plant innate immunity
    • Silipo A, et al. 2010. Glycoconjugates as elicitors or suppressors of plant innate immunity. Glycobiology 20:406-419.
    • (2010) Glycobiology , vol.20 , pp. 406-419
    • Silipo, A.1
  • 33
    • 22144480668 scopus 로고    scopus 로고
    • Enzymatic properties of wild-type and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MS
    • Suginta W, Vongsuwan A, Songsiriritthigul C, Svasti J, Prinz H. 2005. Enzymatic properties of wild-type and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MS. FEBS J. 272:3376-3386.
    • (2005) FEBS J. , vol.272 , pp. 3376-3386
    • Suginta, W.1    Vongsuwan, A.2    Songsiriritthigul, C.3    Svasti, J.4    Prinz, H.5
  • 34
    • 0036562588 scopus 로고    scopus 로고
    • Chitinases A. B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: enzymatic properties and synergism on chitin degradation
    • Suzuki K, et al. 2002. Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: enzymatic properties and synergism on chitin degradation. Biosci. Biotechnol. Biochem. 66:1075-1083.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1075-1083
    • Suzuki, K.1
  • 35
    • 1642521614 scopus 로고    scopus 로고
    • Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase
    • Synstad B, et al. 2004. Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase. FEBS J. 271:253-262.
    • (2004) FEBS J. , vol.271 , pp. 253-262
    • Synstad, B.1
  • 36
    • 59649090302 scopus 로고    scopus 로고
    • Genome survey and characterization of endophytic bacteria exhibiting a beneficial effect on growth and development of poplar trees
    • Taghavi S, et al. 2009. Genome survey and characterization of endophytic bacteria exhibiting a beneficial effect on growth and development of poplar trees. Appl. Environ. Microbiol. 75:748-757.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 748-757
    • Taghavi, S.1
  • 37
    • 0028774705 scopus 로고
    • Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor
    • Terwisscha van Scheltinga AC, Kalk KH, Beintema JJ, Dijkstra BW. 1994. Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure 2:1181-1189.
    • (1994) Structure , vol.2 , pp. 1181-1189
    • Terwisscha van Scheltinga, A.C.1    Kalk, K.H.2    Beintema, J.J.3    Dijkstra, B.W.4
  • 38
    • 0035798612 scopus 로고    scopus 로고
    • Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170
    • Uchiyama T, et al. 2001. Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170. J. Biol. Chem. 276:41343-41349.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41343-41349
    • Uchiyama, T.1
  • 39
    • 41949130819 scopus 로고    scopus 로고
    • Mutants of Mucor hiemalis endo-β-Nacetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities
    • Umekawa M, et al. 2008. Mutants of Mucor hiemalis endo-β-Nacetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities. J. Biol. Chem. 283:4469-4479.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4469-4479
    • Umekawa, M.1
  • 40
    • 63049086705 scopus 로고    scopus 로고
    • The chitinolytic system of Lactococcus lactis ssp. lactis comprises a nonprocessive chitinase and a chitin-binding protein that promotes the degradation of α- and β-chitin
    • Vaaje-Kolstad G, Bunaes AC, Mathiesen G, Eijsink VGH. 2009. The chitinolytic system of Lactococcus lactis ssp. lactis comprises a nonprocessive chitinase and a chitin-binding protein that promotes the degradation of α- and β-chitin. FEBS J. 276:2402-2415.
    • (2009) FEBS J. , vol.276 , pp. 2402-2415
    • Vaaje-Kolstad, G.1    Bunaes, A.C.2    Mathiesen, G.3    Eijsink, V.G.H.4
  • 41
    • 23344446196 scopus 로고    scopus 로고
    • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation
    • Vaaje-Kolstad G, Horn SJ, van Aalten DM, Synstad B, Eijsink VG. 2005. The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J. Bio. Chem. 280:28492-28497.
    • (2005) J. Bio. Chem. , vol.280 , pp. 28492-28497
    • Vaaje-Kolstad, G.1    Horn, S.J.2    van Aalten, D.M.3    Synstad, B.4    Eijsink, V.G.5
  • 42
    • 0035979240 scopus 로고    scopus 로고
    • Structural insights into the catalytic mechanism of a family 18 exo-chitinase
    • van Aalten DMF, et al. 2001. Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc. Natl. Acad. Sci. U. S. A. 98:8979-8984.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8979-8984
    • van Aalten, D.M.F.1
  • 43
    • 0034705193 scopus 로고    scopus 로고
    • Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-å resolution
    • van Aalten DMF, et al. 2000. Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-å resolution. Proc. Natl. Acad. Sci. U. S. A. 97:5842-5847.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5842-5847
    • van Aalten, D.M.F.1
  • 44
    • 0037478704 scopus 로고    scopus 로고
    • Structural basis for ligand binding and processivity in cellobiohydrolase cel6a from Humicola insolens
    • Varrot A, et al. 2003. Structural basis for ligand binding and processivity in cellobiohydrolase cel6a from Humicola insolens. Structure 11:855-864.
    • (2003) Structure , vol.11 , pp. 855-864
    • Varrot, A.1
  • 45
    • 0037051496 scopus 로고    scopus 로고
    • Purification and characterization of two antifungal chitinases extracellularly produced by Bacillus amyloliquefaciens V656 in a shrimp and crab shell powder medium
    • Wang SL, Shih IL, Liang TW, Wang CH. 2002. Purification and characterization of two antifungal chitinases extracellularly produced by Bacillus amyloliquefaciens V656 in a shrimp and crab shell powder medium. J. Agric. Food Chem. 50:2241-2248.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 2241-2248
    • Wang, S.L.1    Shih, I.L.2    Liang, T.W.3    Wang, C.H.4
  • 46
    • 0034631781 scopus 로고    scopus 로고
    • Glycosyl fluorides in enzymatic reactions
    • Williams SJ, Withers SG. 2000. Glycosyl fluorides in enzymatic reactions. Carbohydr. Res. 327:27-46.
    • (2000) Carbohydr. Res. , vol.327 , pp. 27-46
    • Williams, S.J.1    Withers, S.G.2
  • 47
    • 0019883721 scopus 로고
    • A convenient synthesis of glycolchitin, a substrate of lysozyme
    • Yamada H, Imoto T. 1981. A convenient synthesis of glycolchitin, a substrate of lysozyme. Carbohydr. Res. 92:160-162.
    • (1981) Carbohydr. Res. , vol.92 , pp. 160-162
    • Yamada, H.1    Imoto, T.2
  • 48
    • 77953914238 scopus 로고    scopus 로고
    • Oligochitosan: a plant diseases vaccine-a review
    • Yin H, Zhao X, Du Y. 2010. Oligochitosan: a plant diseases vaccine-a review. Carbohydr. Polym. 82:1-8.
    • (2010) Carbohydr. Polym. , vol.82 , pp. 1-8
    • Yin, H.1    Zhao, X.2    Du, Y.3
  • 49
    • 67449088829 scopus 로고    scopus 로고
    • Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency
    • Zakariassen H, et al. 2009. Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency. J. Biol. Chem. 284:10610-10617.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10610-10617
    • Zakariassen, H.1
  • 50
    • 79959457508 scopus 로고    scopus 로고
    • Mutational effects on transglycosylating activity of family 18 chitinases and construction of a hypertransglycosylating mutant
    • Zakariassen H, Hansen MC, Jøranli Eijsink MGVH, Sørlie M. 2011. Mutational effects on transglycosylating activity of family 18 chitinases and construction of a hypertransglycosylating mutant. Biochemistry 50:5693-5703.
    • (2011) Biochemistry , vol.50 , pp. 5693-5703
    • Zakariassen, H.1    Hansen, M.C.2    Jøranli Eijsink, M.G.V.H.3    Sørlie, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.