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Volumn 10, Issue 4, 2007, Pages 233-243

Hydration of vinyl ether groups by unsaturated glycoside hydrolases and their role in bacterial pathogenesis

Author keywords

Bacterial hydrolases; Bacterial lyases; Glycosaminoglycan; Glycoside hydrolase family; Pathogenic saprophytic bacteria

Indexed keywords

BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 38949129725     PISSN: 11396709     EISSN: 16181905     Source Type: Journal    
DOI: 10.2436/20.1501.01.32     Document Type: Article
Times cited : (6)

References (55)
  • 1
    • 0037436378 scopus 로고    scopus 로고
    • Crystal structure and evolution of a prokaryotic glucoamylase
    • Aleshin AE, Feng PH, Honzatko RB, Reilly PJ (2003) Crystal structure and evolution of a prokaryotic glucoamylase. J Mol Biol 327:61-73
    • (2003) J Mol Biol , vol.327 , pp. 61-73
    • Aleshin, A.E.1    Feng, P.H.2    Honzatko, R.B.3    Reilly, P.J.4
  • 2
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • Carpita NC, Gibeaut DM (1993) Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Plant J 3:1-30
    • (1993) Plant J , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 3
    • 27944434246 scopus 로고    scopus 로고
    • Recent structural insights into the expanding world of carbohydrate-active enzymes
    • Davies GJ, Gloster TM, Henrissat B (2005) Recent structural insights into the expanding world of carbohydrate-active enzymes. Curr Opin Struct Biol 15:637-645
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 637-645
    • Davies, G.J.1    Gloster, T.M.2    Henrissat, B.3
  • 4
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G, Henrissat B (1995) Structures and mechanisms of glycosyl hydrolases. Structure 3:853-859
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 5
    • 0032754629 scopus 로고    scopus 로고
    • Hyaluronan synthases: Fascinating glycosyltransferases from vertebrates, bacterial pathogens, and algal viruses
    • DeAngelis PL (1999) Hyaluronan synthases: fascinating glycosyltransferases from vertebrates, bacterial pathogens, and algal viruses. Cell Mol Life Sci 56:670-682
    • (1999) Cell Mol Life Sci , vol.56 , pp. 670-682
    • DeAngelis, P.L.1
  • 7
    • 0029597839 scopus 로고
    • Purification, characterization and specificity of chondroitin lyases and glycuronidase from Flavobacterium heparinum
    • Gu K, Linhardt RJ, Laliberté M, Gu K, Zimmermann J (1995) Purification, characterization and specificity of chondroitin lyases and glycuronidase from Flavobacterium heparinum. Biochem J 312:569-577
    • (1995) Biochem J , vol.312 , pp. 569-577
    • Gu, K.1    Linhardt, R.J.2    Laliberté, M.3    Gu, K.4    Zimmermann, J.5
  • 8
    • 0031106252 scopus 로고    scopus 로고
    • Microbial system for polysaccharide depolymerization: Enzymatic route for gellan depolymerization by Bacillus sp. GL1
    • Hashimoto W, Maesaka K, Sato N, Kimura S, Yamamoto K, Kumagai H, Murata K (1997) Microbial system for polysaccharide depolymerization: enzymatic route for gellan depolymerization by Bacillus sp. GL1. Arch Biochem Biophys 339:17-23
    • (1997) Arch Biochem Biophys , vol.339 , pp. 17-23
    • Hashimoto, W.1    Maesaka, K.2    Sato, N.3    Kimura, S.4    Yamamoto, K.5    Kumagai, H.6    Murata, K.7
  • 9
    • 0031664395 scopus 로고    scopus 로고
    • Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains
    • Hashimoto W, Miki H, Tsuchiya N, Nankai H, Murata K (1998) Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains. Appl Environ Microbiol 64:3765-3768
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3765-3768
    • Hashimoto, W.1    Miki, H.2    Tsuchiya, N.3    Nankai, H.4    Murata, K.5
  • 10
    • 0031858250 scopus 로고    scopus 로고
    • Polysaccharide lyase: Molecular cloning of gellan lyase gene and formation of the lyase from a huge precursor protein in Bacillus sp. GL1
    • Hashimoto W, Sato N, Kimura S, Murata K (1998) Polysaccharide lyase: molecular cloning of gellan lyase gene and formation of the lyase from a huge precursor protein in Bacillus sp. GL1. Arch Biochem Biophys 354:31-39
    • (1998) Arch Biochem Biophys , vol.354 , pp. 31-39
    • Hashimoto, W.1    Sato, N.2    Kimura, S.3    Murata, K.4
  • 11
    • 0033567244 scopus 로고    scopus 로고
    • Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: Novel enzyme prerequisite for metabolism of unsaturated oligosaccharides produced by polysaccharide lyases
    • Hashimoto W, Kobayashi E, Nankai H, Sato N, Miya T, Kawai S, Murata K (1999) Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme prerequisite for metabolism of unsaturated oligosaccharides produced by polysaccharide lyases. Arch Biochem Biophys 368:367-374
    • (1999) Arch Biochem Biophys , vol.368 , pp. 367-374
    • Hashimoto, W.1    Kobayashi, E.2    Nankai, H.3    Sato, N.4    Miya, T.5    Kawai, S.6    Murata, K.7
  • 12
    • 0033905713 scopus 로고    scopus 로고
    • Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate
    • Hashimoto W, Miyake O, Momma K, Kawai S, Murata K (2000) Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate. J Bacteriol 182:4572-4577
    • (2000) J Bacteriol , vol.182 , pp. 4572-4577
    • Hashimoto, W.1    Miyake, O.2    Momma, K.3    Kawai, S.4    Murata, K.5
  • 13
    • 0033579524 scopus 로고    scopus 로고
    • Crystal structure of chondroitinase B from Flavobacterium heparinum and its complex with a disaccharide product at 1.7 Å resolution
    • Huang W, Matte A, Li Y, Kim YS, Linhardt RJ, Su H, Cygler M (1999) Crystal structure of chondroitinase B from Flavobacterium heparinum and its complex with a disaccharide product at 1.7 Å resolution. J Mol Biol 294:1257-1269
    • (1999) J Mol Biol , vol.294 , pp. 1257-1269
    • Huang, W.1    Matte, A.2    Li, Y.3    Kim, Y.S.4    Linhardt, R.J.5    Su, H.6    Cygler, M.7
  • 14
    • 1542511814 scopus 로고    scopus 로고
    • The RhaS activator controls the Erwinia chrysanthemi 3937 genes rhiN, rhiT and rhiE involved in rhamnogalacturonan catabolism
    • Hugouvieux-Cotte-Pattat N (2004) The RhaS activator controls the Erwinia chrysanthemi 3937 genes rhiN, rhiT and rhiE involved in rhamnogalacturonan catabolism. Mol Microbiol 51:1361-1374
    • (2004) Mol Microbiol , vol.51 , pp. 1361-1374
    • Hugouvieux-Cotte-Pattat, N.1
  • 15
    • 0031657808 scopus 로고    scopus 로고
    • Matrix proteoglycans: From molecular design to cellular function
    • Iozzo RV (1998) Matrix proteoglycans: from molecular design to cellular function. Annu Rev Biochem 67:609-652
    • (1998) Annu Rev Biochem , vol.67 , pp. 609-652
    • Iozzo, R.V.1
  • 16
    • 3843119941 scopus 로고    scopus 로고
    • Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 Å resolution
    • Itoh T, Akao S, Hashimoto W, Mikami B, Murata K (2004) Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 Å resolution. J Biol Chem 279:31804-31812
    • (2004) J Biol Chem , vol.279 , pp. 31804-31812
    • Itoh, T.1    Akao, S.2    Hashimoto, W.3    Mikami, B.4    Murata, K.5
  • 17
    • 33749564034 scopus 로고    scopus 로고
    • Crystal structure of unsaturated glucuronyl hydrolase complexed with substrate: Molecular insights into its catalytic reaction mechanism
    • Itoh T, Hashimoto W, Mikami B, Murata K (2006) Crystal structure of unsaturated glucuronyl hydrolase complexed with substrate: molecular insights into its catalytic reaction mechanism. J Biol Chem 281:29807-29816
    • (2006) J Biol Chem , vol.281 , pp. 29807-29816
    • Itoh, T.1    Hashimoto, W.2    Mikami, B.3    Murata, K.4
  • 18
    • 33646033148 scopus 로고    scopus 로고
    • Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1
    • Itoh T, Hashimoto W, Mikami B, Murata K (2006) Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1. Biochem Biophys Res Commun 344:253-262
    • (2006) Biochem Biophys Res Commun , vol.344 , pp. 253-262
    • Itoh, T.1    Hashimoto, W.2    Mikami, B.3    Murata, K.4
  • 19
    • 0034634335 scopus 로고    scopus 로고
    • Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 Å resolution
    • Itoh T, Mikami B, Maru I, Ohta Y, Hashimoto W, Murata K (2000) Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 Å resolution. J Mol Biol 303:733-744
    • (2000) J Mol Biol , vol.303 , pp. 733-744
    • Itoh, T.1    Mikami, B.2    Maru, I.3    Ohta, Y.4    Hashimoto, W.5    Murata, K.6
  • 20
    • 33745670608 scopus 로고    scopus 로고
    • A novel glycoside hydrolase family 105: The structure of family 105 unsaturated rhamnogalacturonyl hydrolase complexed with a disaccharide in comparison with family 88 enzyme complexed with the disaccharide
    • Itoh T, Ochiai A, Mikami B, Hashimoto W, Murata K (2006) A novel glycoside hydrolase family 105: the structure of family 105 unsaturated rhamnogalacturonyl hydrolase complexed with a disaccharide in comparison with family 88 enzyme complexed with the disaccharide. J Mol Biol 360:573-585
    • (2006) J Mol Biol , vol.360 , pp. 573-585
    • Itoh, T.1    Ochiai, A.2    Mikami, B.3    Hashimoto, W.4    Murata, K.5
  • 21
  • 22
    • 0016624572 scopus 로고
    • Structure of the extracellular polysaccharide from Xanthomonas campestris
    • Jansson PE, Kenne L, Lindberg B (1975) Structure of the extracellular polysaccharide from Xanthomonas campestris. Carbohydr Res 45:275-282
    • (1975) Carbohydr Res , vol.45 , pp. 275-282
    • Jansson, P.E.1    Kenne, L.2    Lindberg, B.3
  • 23
    • 0000282135 scopus 로고
    • Structural studies of gellan gum, an extracellular polysaccharide elaborated by Pseudomonas elodea
    • Jansson PE, Lindberg B, Sandford PA (1983) Structural studies of gellan gum, an extracellular polysaccharide elaborated by Pseudomonas elodea. Carbohydr Res 124:135-139
    • (1983) Carbohydr Res , vol.124 , pp. 135-139
    • Jansson, P.E.1    Lindberg, B.2    Sandford, P.A.3
  • 24
    • 0034971094 scopus 로고    scopus 로고
    • Pneumococcal virulence factors: Structure and function
    • Jedrzejas MJ (2001) Pneumococcal virulence factors: structure and function. Microbiol Mol Biol Rev 65:187-207
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 187-207
    • Jedrzejas, M.J.1
  • 26
    • 0035798695 scopus 로고    scopus 로고
    • Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase
    • Li S, Jedrzejas MJ (2001) Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase. J Biol Chem 276:41407-41416
    • (2001) J Biol Chem , vol.276 , pp. 41407-41416
    • Li, S.1    Jedrzejas, M.J.2
  • 27
    • 0002946411 scopus 로고
    • The formation of unsaturated disacharides from mucopolysaccharides and their cleavage to α-keto acid by bacterial enzymes
    • Linker A, Hoffman P, Meyer K, Sampson P, Korn ED (1960) The formation of unsaturated disacharides from mucopolysaccharides and their cleavage to α-keto acid by bacterial enzymes. J Biol Chem 235:3061-3065
    • (1960) J Biol Chem , vol.235 , pp. 3061-3065
    • Linker, A.1    Hoffman, P.2    Meyer, K.3    Sampson, P.4    Korn, E.D.5
  • 28
    • 2442695616 scopus 로고    scopus 로고
    • Extracellular virulence factors of group B Streptococci
    • Liu GY, Nizet V (2004) Extracellular virulence factors of group B Streptococci. Front Biosci 9:1794-1802
    • (2004) Front Biosci , vol.9 , pp. 1794-1802
    • Liu, G.Y.1    Nizet, V.2
  • 29
    • 0035469635 scopus 로고    scopus 로고
    • Genetic bases and medical relevance of capsular polysaccharide biosynthesis in pathogenic streptococci
    • Llull D, Lopez R, Garcia E (2001) Genetic bases and medical relevance of capsular polysaccharide biosynthesis in pathogenic streptococci. Curr Mol Med 1:475-491
    • (2001) Curr Mol Med , vol.1 , pp. 475-491
    • Llull, D.1    Lopez, R.2    Garcia, E.3
  • 30
    • 0026460982 scopus 로고
    • Purification and characterization of heparin lyases from Flavobacterium heparinum
    • Lohse DL, Linhardt RJ (1992) Purification and characterization of heparin lyases from Flavobacterium heparinum. J Biol Chem 267:24347-24355
    • (1992) J Biol Chem , vol.267 , pp. 24347-24355
    • Lohse, D.L.1    Linhardt, R.J.2
  • 32
    • 21744444127 scopus 로고    scopus 로고
    • Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: Insights into the enzyme reaction mechanism
    • Maruyama Y, Hashimoto W, Mikami B, Murata K (2005) Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: insights into the enzyme reaction mechanism. J Mol Biol 350:974-986
    • (2005) J Mol Biol , vol.350 , pp. 974-986
    • Maruyama, Y.1    Hashimoto, W.2    Mikami, B.3    Murata, K.4
  • 33
    • 0031570284 scopus 로고    scopus 로고
    • Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases
    • Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J, Pickersgill R, Jenkins J (1997) Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. Structure 5:677-689
    • (1997) Structure , vol.5 , pp. 677-689
    • Mayans, O.1    Scott, M.2    Connerton, I.3    Gravesen, T.4    Benen, J.5    Visser, J.6    Pickersgill, R.7    Jenkins, J.8
  • 34
    • 2342602908 scopus 로고    scopus 로고
    • Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4
    • McDonough MA, Kadirvelraj R, Harris P, Poulsen JC, Larsen S (2004) Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4. FEBS Lett 565:188-194
    • (2004) FEBS Lett , vol.565 , pp. 188-194
    • McDonough, M.A.1    Kadirvelraj, R.2    Harris, P.3    Poulsen, J.C.4    Larsen, S.5
  • 35
    • 0000054384 scopus 로고
    • Structure of plant cell walls: X. Rhamnogalacturonan I, a structurally complex pectic polysaccharide in the walls of suspension-cultured sycamore cells
    • McNeil M, Darvill AG, Albersheim P (1980) Structure of plant cell walls: X. Rhamnogalacturonan I, a structurally complex pectic polysaccharide in the walls of suspension-cultured sycamore cells. Plant Physiol 66:1128-1134
    • (1980) Plant Physiol , vol.66 , pp. 1128-1134
    • McNeil, M.1    Darvill, A.G.2    Albersheim, P.3
  • 36
    • 1842456932 scopus 로고    scopus 로고
    • The pathogenesis of streptococcal infections: From tooth decay to meningitis
    • Mitchell TJ (2003) The pathogenesis of streptococcal infections: from tooth decay to meningitis. Nat Rev Microbiol 1:219-230
    • (2003) Nat Rev Microbiol , vol.1 , pp. 219-230
    • Mitchell, T.J.1
  • 37
    • 0038193700 scopus 로고    scopus 로고
    • A novel member of glycoside hydrolase family 88: Overexpression, purification, and characterization of unsaturated β-glucuronyl hydrolase of Bacillus sp. GL1
    • Mori S, Akao S, Nankai H, Hashimoto W, Mikami B, Murata K (2003) A novel member of glycoside hydrolase family 88: overexpression, purification, and characterization of unsaturated β-glucuronyl hydrolase of Bacillus sp. GL1. Protein Expr Purif 29:77-84
    • (2003) Protein Expr Purif , vol.29 , pp. 77-84
    • Mori, S.1    Akao, S.2    Nankai, H.3    Hashimoto, W.4    Mikami, B.5    Murata, K.6
  • 38
    • 33646243578 scopus 로고    scopus 로고
    • Beneficial biofilm formation by industrial bacteria Bacillus subtilis and related species
    • Morikawa M (2006) Beneficial biofilm formation by industrial bacteria Bacillus subtilis and related species. J Biosci Bioeng 101:1-8
    • (2006) J Biosci Bioeng , vol.101 , pp. 1-8
    • Morikawa, M.1
  • 39
    • 0037809268 scopus 로고    scopus 로고
    • The heparin/heparan sulfate 2-O-sulfatase from Flavobacterium heparinum. Molecular cloning, recombinant expression, and biochemical characterization
    • Myette JR, Shriver Z, Claycamp C, McLean MW, Venkataraman G, Sasisekharan R (2003) The heparin/heparan sulfate 2-O-sulfatase from Flavobacterium heparinum. Molecular cloning, recombinant expression, and biochemical characterization. J Biol Chem 278:12157-12166
    • (2003) J Biol Chem , vol.278 , pp. 12157-12166
    • Myette, J.R.1    Shriver, Z.2    Claycamp, C.3    McLean, M.W.4    Venkataraman, G.5    Sasisekharan, R.6
  • 40
    • 0037062622 scopus 로고    scopus 로고
    • Molecular cloning of the heparin/heparan sulfate Δ4,5 unsaturated glycuronidase from Flavobacterium heparinum, its recombinant expression in Escherichia coli, and biochemical determination of its unique substrate specificity
    • Myette JR, Shriver Z, Kiziltepe T, McLean MW, Venkataraman G, Sasisekharan R (2002) Molecular cloning of the heparin/heparan sulfate Δ4,5 unsaturated glycuronidase from Flavobacterium heparinum, its recombinant expression in Escherichia coli, and biochemical determination of its unique substrate specificity. Biochemistry 41:7424-7434
    • (2002) Biochemistry , vol.41 , pp. 7424-7434
    • Myette, J.R.1    Shriver, Z.2    Kiziltepe, T.3    McLean, M.W.4    Venkataraman, G.5    Sasisekharan, R.6
  • 41
    • 0032975847 scopus 로고    scopus 로고
    • Microbial system for polysaccharide depolymerization: Enzymatic route for xanthan depolymerization by Bacillus sp. strain GL1
    • Nankai H, Hashimoto W, Miki H, Kawai S, Murata K (1999) Microbial system for polysaccharide depolymerization: enzymatic route for xanthan depolymerization by Bacillus sp. strain GL1. Appl Environ Microbiol 65:2520-2526
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2520-2526
    • Nankai, H.1    Hashimoto, W.2    Miki, H.3    Kawai, S.4    Murata, K.5
  • 42
    • 34250877831 scopus 로고    scopus 로고
    • Plant cell wall degradation by saprophytic Bacillus subtilis strains: Gene clusters responsible for rhamnogalacturonan depolymerization
    • Ochiai A, Itoh T, Kawamata A, Hashimoto W, Murata K (2007) Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene clusters responsible for rhamnogalacturonan depolymerization. Appl Environ Microbiol 73:3803-3813
    • (2007) Appl Environ Microbiol , vol.73 , pp. 3803-3813
    • Ochiai, A.1    Itoh, T.2    Kawamata, A.3    Hashimoto, W.4    Murata, K.5
  • 43
    • 0029788024 scopus 로고    scopus 로고
    • Rhamnogalacturonan-II, a pectic polysaccharide in the walls of growing plant cell, forms a dimer that is covalently cross-linked by a borate ester. In vitro conditions for the formation and hydrolysis of the dimer
    • O'Neill MA, Warrenfeltz D, Kates K, Pellerin P, Doco T, Darvill AG, Albersheim P (1996) Rhamnogalacturonan-II, a pectic polysaccharide in the walls of growing plant cell, forms a dimer that is covalently cross-linked by a borate ester. In vitro conditions for the formation and hydrolysis of the dimer. J Biol Chem 271:22923-22930
    • (1996) J Biol Chem , vol.271 , pp. 22923-22930
    • O'Neill, M.A.1    Warrenfeltz, D.2    Kates, K.3    Pellerin, P.4    Doco, T.5    Darvill, A.G.6    Albersheim, P.7
  • 44
    • 2442549670 scopus 로고    scopus 로고
    • Interactions of heparin/heparan sulfate with proteins: Appraisal of structural factors and experimental approaches
    • Powell AK, Yates EA, Fernig DG, Turnbull JE (2004) Interactions of heparin/heparan sulfate with proteins: appraisal of structural factors and experimental approaches. Glycobiology 14:17R-30R
    • (2004) Glycobiology , vol.14
    • Powell, A.K.1    Yates, E.A.2    Fernig, D.G.3    Turnbull, J.E.4
  • 46
    • 0037151621 scopus 로고    scopus 로고
    • Elucidation of the mechanism of polysaccharide cleavage by chondroitin AC lyase from Flavobacterium heparinum
    • Rye CS, Withers SG (2002) Elucidation of the mechanism of polysaccharide cleavage by chondroitin AC lyase from Flavobacterium heparinum. J Am Chem Soc 124:9756-9767
    • (2002) J Am Chem Soc , vol.124 , pp. 9756-9767
    • Rye, C.S.1    Withers, S.G.2
  • 47
    • 0029549804 scopus 로고    scopus 로고
    • Protein-glycosaminoglycan interactions: Infectiological aspects
    • Sawitzky D (1996) Protein-glycosaminoglycan interactions: infectiological aspects. Med Microbiol Immunol 184:155-161
    • (1996) Med Microbiol Immunol , vol.184 , pp. 155-161
    • Sawitzky, D.1
  • 48
    • 0032988009 scopus 로고    scopus 로고
    • The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937
    • Shevchik VE, Condemine G, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N (1999) The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. J Bacteriol 181:3912-3919
    • (1999) J Bacteriol , vol.181 , pp. 3912-3919
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudouy, J.3    Hugouvieux-Cotte-Pattat, N.4
  • 49
    • 0029777326 scopus 로고    scopus 로고
    • Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum
    • Su H, Blain F, Musil RA, Zimmermann JJ, Gu K, Bennett DC (1996) Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum. Appl Environ Microbiol 62:2723-2734
    • (1996) Appl Environ Microbiol , vol.62 , pp. 2723-2734
    • Su, H.1    Blain, F.2    Musil, R.A.3    Zimmermann, J.J.4    Gu, K.5    Bennett, D.C.6
  • 51
    • 0033986003 scopus 로고    scopus 로고
    • Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium heparinum
    • Tkalec AL, Fink D, Blain F, Zhang-Sun G, Laliberte M, Bennett DC, Gu K, Zimmermann JJ, Su H (2000) Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium heparinum. Appl Environ Microbiol 66:29-35
    • (2000) Appl Environ Microbiol , vol.66 , pp. 29-35
    • Tkalec, A.L.1    Fink, D.2    Blain, F.3    Zhang-Sun, G.4    Laliberte, M.5    Bennett, D.C.6    Gu, K.7    Zimmermann, J.J.8    Su, H.9
  • 52
    • 0015507407 scopus 로고
    • Purification of an unusual α-glycuronidase from flavobacteria
    • Warnick CT, Linker A (1972) Purification of an unusual α-glycuronidase from flavobacteria. Biochemistry 11:568-572
    • (1972) Biochemistry , vol.11 , pp. 568-572
    • Warnick, C.T.1    Linker, A.2
  • 53
    • 0027918655 scopus 로고
    • Unusual structural features in the parallel β-helix in pectate lyases
    • Yoder MD, Lietzke SE, Jurnak F (1993) Unusual structural features in the parallel β-helix in pectate lyases. Structure 1:241-251
    • (1993) Structure , vol.1 , pp. 241-251
    • Yoder, M.D.1    Lietzke, S.E.2    Jurnak, F.3
  • 54
    • 0033538420 scopus 로고    scopus 로고
    • Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 Å resolution
    • Yoon H-J, Mikami B, Hashimoto W, Murata K (1999) Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 Å resolution. J Mol Biol 290:505-514
    • (1999) J Mol Biol , vol.290 , pp. 505-514
    • Yoon, H.-J.1    Mikami, B.2    Hashimoto, W.3    Murata, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.