메뉴 건너뛰기




Volumn 46, Issue 3, 2007, Pages 792-798

Kinetic and structural analysis of enzyme sliding on a substrate: Multiple attack in β-amylase

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; HYDROGEN BONDS; MOLECULAR STRUCTURE; MONTE CARLO METHODS; MUTAGENESIS; OLIGOMERS; STARCH;

EID: 33846355772     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061605w     Document Type: Article
Times cited : (21)

References (38)
  • 1
    • 0006322177 scopus 로고
    • The significance of multiple reactions in enzyme polymer systems
    • Bailey, J. M., and French, D. (1957). The significance of multiple reactions in enzyme polymer systems, J. Biol. Chem. 226, 1-14.
    • (1957) J. Biol. Chem , vol.226 , pp. 1-14
    • Bailey, J.M.1    French, D.2
  • 2
    • 84979316189 scopus 로고
    • Die Wirkungsweise von beta-amylase auf Starkeoligosaccharide
    • French, D., and Youngquist, R. W. (1963). Die Wirkungsweise von beta-amylase auf Starkeoligosaccharide, Starke 12, 425-431.
    • (1963) Starke , vol.12 , pp. 425-431
    • French, D.1    Youngquist, R.W.2
  • 3
    • 0014140609 scopus 로고
    • Multiple attach hypothesis of alpha-amylase action: Action of porcine pancreatic, human salivary, and Aspergillus Oryzae alpha-amylases
    • Robyt, J. F., and French, D. (1967). Multiple attach hypothesis of alpha-amylase action: action of porcine pancreatic, human salivary, and Aspergillus Oryzae alpha-amylases, Arch. Biochem. Biophys. 122, 8-16.
    • (1967) Arch. Biochem. Biophys , vol.122 , pp. 8-16
    • Robyt, J.F.1    French, D.2
  • 4
    • 0014944762 scopus 로고
    • Subsite mapping of enzymes. Studies on Bacillus subtilis amylase
    • Thoma, J. A., Brothers, C., and Spradlin, J. (1970). Subsite mapping of enzymes. Studies on Bacillus subtilis amylase, Biochemistry 9, 1768-1775.
    • (1970) Biochemistry , vol.9 , pp. 1768-1775
    • Thoma, J.A.1    Brothers, C.2    Spradlin, J.3
  • 5
    • 0015240182 scopus 로고
    • Subsite mapping of enzymes. Correlation of product patterns with Michaelis parameters and substrate-induced strain
    • Thoma, J. A., Rao, G. V., Brothers, C., Spradlin, J., and Li, L. H. (1971). Subsite mapping of enzymes. Correlation of product patterns with Michaelis parameters and substrate-induced strain, J. Biol. Chem. 246, 5621-5635.
    • (1971) J. Biol. Chem , vol.246 , pp. 5621-5635
    • Thoma, J.A.1    Rao, G.V.2    Brothers, C.3    Spradlin, J.4    Li, L.H.5
  • 6
    • 0016960327 scopus 로고
    • Models for depolymerizing enzymes: Criteria for discrimination of models
    • Thoma, J. A. (1976). Models for depolymerizing enzymes: criteria for discrimination of models, Carbohydr. Res. 48, 85-103.
    • (1976) Carbohydr. Res , vol.48 , pp. 85-103
    • Thoma, J.A.1
  • 7
    • 0027372602 scopus 로고
    • Multiple attack mechanism in the porcine pancreatic alpha-amylase hydrolysis of amylose and amylopectin
    • Mazur, A. K., and Nakatani, H. (1993). Multiple attack mechanism in the porcine pancreatic alpha-amylase hydrolysis of amylose and amylopectin, Arch. Biochem. Biophys. 306, 29-38.
    • (1993) Arch. Biochem. Biophys , vol.306 , pp. 29-38
    • Mazur, A.K.1    Nakatani, H.2
  • 8
    • 0029743877 scopus 로고    scopus 로고
    • The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size
    • Kleman-Leyer, K. M., Siika-Aho, M., Teeri, T. T., and Kirk, T. K. (1996). The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size, Appl. Environ. Microbiol. 62, 2883-2887.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 2883-2887
    • Kleman-Leyer, K.M.1    Siika-Aho, M.2    Teeri, T.T.3    Kirk, T.K.4
  • 9
    • 0037226350 scopus 로고    scopus 로고
    • Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: Importance of the CBM to cellulose hydrolysis
    • Arai, T., Araki, R., Tanaka, A., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K. (2003). Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: importance of the CBM to cellulose hydrolysis, J. Bacteriol. 185, 504-512.
    • (2003) J. Bacteriol , vol.185 , pp. 504-512
    • Arai, T.1    Araki, R.2    Tanaka, A.3    Karita, S.4    Kimura, T.5    Sakka, K.6    Ohmiya, K.7
  • 10
    • 0035798612 scopus 로고    scopus 로고
    • Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170
    • Uchiyama, T., Katouno, F., Nikaidou, N., Nonaka, T., Sugiyama, J., and Watanabe, T. (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    Katouno, F.2    Nikaidou, N.3    Nonaka, T.4    Sugiyama, J.5    Watanabe, T.6
  • 11
    • 0344825227 scopus 로고    scopus 로고
    • Aromatic residues within the substrate-binding cleft of Bacillus circulans chtinase A1 are essential for hydrolysis of crystalline chitin
    • Watanabe, T., Ariga, Y., Sato, U., Toratani, T., Hashimoto, M., Nikaidou, N., Kezuka, Y., Nonaka, T., and Sugiyama, J. (2003). Aromatic residues within the substrate-binding cleft of Bacillus circulans chtinase A1 are essential for hydrolysis of crystalline chitin, Biochem. J. 376, 237-244.
    • (2003) Biochem. J , vol.376 , pp. 237-244
    • Watanabe, T.1    Ariga, Y.2    Sato, U.3    Toratani, T.4    Hashimoto, M.5    Nikaidou, N.6    Kezuka, Y.7    Nonaka, T.8    Sugiyama, J.9
  • 13
    • 0029790522 scopus 로고    scopus 로고
    • Linear diffusion of the restriction endonuclease EcoRV on DNA is essential for the in vivo function of the enzyme
    • Jeltsch, A., Wenz, C., Stahl, F., and Pingoud, A. (1996). Linear diffusion of the restriction endonuclease EcoRV on DNA is essential for the in vivo function of the enzyme, EMBO J. 15, 5104-5111.
    • (1996) EMBO J , vol.15 , pp. 5104-5111
    • Jeltsch, A.1    Wenz, C.2    Stahl, F.3    Pingoud, A.4
  • 15
    • 0022731844 scopus 로고
    • Affinity labeling of soybean beta-amylase with 2′,3′-epoxypropyl alpha-D-glucopyranoside
    • Isoda, Y., and Nitta, Y. (1986). Affinity labeling of soybean beta-amylase with 2′,3′-epoxypropyl alpha-D-glucopyranoside, J. Biochem. (Tokyo) 99, 1631-1637.
    • (1986) J. Biochem. (Tokyo) , vol.99 , pp. 1631-1637
    • Isoda, Y.1    Nitta, Y.2
  • 16
    • 0027338121 scopus 로고
    • The 2.0-Å resolution structure of soybean beta-amylase complexed with alpha-cyclodextrin
    • Mikami, B., Hehre, E. J., Sato, M., Katsube, Y., Hirose, M., Morita, Y., and Sacchettini, J. C. (1993). The 2.0-Å resolution structure of soybean beta-amylase complexed with alpha-cyclodextrin, Biochemistry 32, 6836-6845.
    • (1993) Biochemistry , vol.32 , pp. 6836-6845
    • Mikami, B.1    Hehre, E.J.2    Sato, M.3    Katsube, Y.4    Hirose, M.5    Morita, Y.6    Sacchettini, J.C.7
  • 17
    • 0028181134 scopus 로고
    • Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: Active site components and their apparent roles in catalysis
    • Mikami, B., Degano, M., Hehre, E. J., and Sacchettini, J. C. (1994). Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis, Biochemistry 33, 7779-7787.
    • (1994) Biochemistry , vol.33 , pp. 7779-7787
    • Mikami, B.1    Degano, M.2    Hehre, E.J.3    Sacchettini, J.C.4
  • 18
    • 0027464862 scopus 로고
    • Cloning of the beta-amylase gene from Bacillus cereus and characteristics of the primary structure of the enzyme
    • Nanmori, T., Nagai, M., Shimizu, Y., Shinke, R., and Mikami, B. (1993). Cloning of the beta-amylase gene from Bacillus cereus and characteristics of the primary structure of the enzyme, Appl. Environ. Microbiol. 59, 623-627.
    • (1993) Appl. Environ. Microbiol , vol.59 , pp. 623-627
    • Nanmori, T.1    Nagai, M.2    Shimizu, Y.3    Shinke, R.4    Mikami, B.5
  • 19
    • 0029839527 scopus 로고    scopus 로고
    • Evolution of beta-amylase: Patterns of variation and conservation in subfamily sequences in relation to parsimony mechanisms
    • Pujadas, G., Ramirez, F. M., Valero, R., and Palau, J. (1996). Evolution of beta-amylase: patterns of variation and conservation in subfamily sequences in relation to parsimony mechanisms, Proteins 25, 456-472.
    • (1996) Proteins , vol.25 , pp. 456-472
    • Pujadas, G.1    Ramirez, F.M.2    Valero, R.3    Palau, J.4
  • 20
    • 0032806644 scopus 로고    scopus 로고
    • Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 Å resolution
    • Oyama, T., Kusunoki, M., Kishimoto, Y., Takasaki, Y., and Nitta, Y. (1999). Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 Å resolution, J. Biochem. (Tokyo) 125, 1120-1130.
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 1120-1130
    • Oyama, T.1    Kusunoki, M.2    Kishimoto, Y.3    Takasaki, Y.4    Nitta, Y.5
  • 21
    • 0033593468 scopus 로고    scopus 로고
    • The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 Å resolution
    • Mikami, B., Yoon, H. J., and Yoshigi, N. (1999). The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 Å resolution, J. Mol. Biol. 285, 1235-1243.
    • (1999) J. Mol. Biol , vol.285 , pp. 1235-1243
    • Mikami, B.1    Yoon, H.J.2    Yoshigi, N.3
  • 23
    • 0030298071 scopus 로고    scopus 로고
    • Monte Carlo simulation of multiple attack mechanism of alpha-amylase
    • Nakatani, H. (1996). Monte Carlo simulation of multiple attack mechanism of alpha-amylase, Biopolymers 39, 665-669.
    • (1996) Biopolymers , vol.39 , pp. 665-669
    • Nakatani, H.1
  • 24
    • 0031540792 scopus 로고    scopus 로고
    • Monte Carlo simulation of multiple attack mechanism of beta-amylase-catalyzed reaction
    • Nakatani, H. (1997). Monte Carlo simulation of multiple attack mechanism of beta-amylase-catalyzed reaction, Biopolymers 42, 831-836.
    • (1997) Biopolymers , vol.42 , pp. 831-836
    • Nakatani, H.1
  • 25
    • 0027263490 scopus 로고
    • Expression and mutation of soybean beta-amylase in Escherichia coli
    • Totsuka, A., and Fukazawa, C. (1993). Expression and mutation of soybean beta-amylase in Escherichia coli, Eur. J. Biochem. 214, 787-794.
    • (1993) Eur. J. Biochem , vol.214 , pp. 787-794
    • Totsuka, A.1    Fukazawa, C.2
  • 26
    • 0013670636 scopus 로고    scopus 로고
    • An isoelectric separation of soybean beta-amylase isoforms and their enzymatic characteristics
    • Wang, Y., Arahira, M., and Fukazawa, C. (1999). An isoelectric separation of soybean beta-amylase isoforms and their enzymatic characteristics, Biosci. Biotechnol. Biochem. 63, 726-730.
    • (1999) Biosci. Biotechnol. Biochem , vol.63 , pp. 726-730
    • Wang, Y.1    Arahira, M.2    Fukazawa, C.3
  • 29
    • 0032584737 scopus 로고    scopus 로고
    • Crystal structure of recombinant soybean beta-amylaser complexed with beta-cyclodextrin
    • Adachi, M., Mikami, B., Katsube, T., and Utsumi, S. (1998). Crystal structure of recombinant soybean beta-amylaser complexed with beta-cyclodextrin, J. Biol. Chem. 273, 19859-19865.
    • (1998) J. Biol. Chem , vol.273 , pp. 19859-19865
    • Adachi, M.1    Mikami, B.2    Katsube, T.3    Utsumi, S.4
  • 30
    • 16344376742 scopus 로고    scopus 로고
    • Structural analysis of threonine 342 mutants of soybean beta-amylase: Role of a conformational change of the inner loop in the catalytic mechanism
    • Kang, Y. N., Tanabe, A., Adachi, M., Utsumi, S., and Mikami, B. (2005). Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism, Biochemistry 44, 5106-5116.
    • (2005) Biochemistry , vol.44 , pp. 5106-5116
    • Kang, Y.N.1    Tanabe, A.2    Adachi, M.3    Utsumi, S.4    Mikami, B.5
  • 31
    • 0029772366 scopus 로고    scopus 로고
    • Functional analysis of Glu380 and Leu383 of soybean beta-amylase. A proposed action mechanism
    • Totsuka, A., and Fukazawa, C. (1996). Functional analysis of Glu380 and Leu383 of soybean beta-amylase. A proposed action mechanism, Eur. J. Biochem. 240, 655-659.
    • (1996) Eur. J. Biochem , vol.240 , pp. 655-659
    • Totsuka, A.1    Fukazawa, C.2
  • 32
    • 0019036695 scopus 로고
    • Studies of the action pattern of an alpha-amylase from Streptomyces praecox NA-273
    • Suganuma, T., Mizukami, T., Moori, K., Ohnishi, M., and Hiromi, K. (1980). Studies of the action pattern of an alpha-amylase from Streptomyces praecox NA-273, J. Biochem. (Tokyo) 88, 131-138.
    • (1980) J. Biochem. (Tokyo) , vol.88 , pp. 131-138
    • Suganuma, T.1    Mizukami, T.2    Moori, K.3    Ohnishi, M.4    Hiromi, K.5
  • 33
    • 0028861775 scopus 로고
    • Crystallization, molecular replacement solution, and refinement of tetrameric beta-amylase from sweet potato
    • Cheong, C. G., Eom, S. H., Chang, C., Shin, D. H., Song, H. K., Min, K., Moon, J. H., Kim, K. K., Hwang, K. Y., and Suh, S. W. (1995). Crystallization, molecular replacement solution, and refinement of tetrameric beta-amylase from sweet potato, Proteins 21, 105-117.
    • (1995) Proteins , vol.21 , pp. 105-117
    • Cheong, C.G.1    Eom, S.H.2    Chang, C.3    Shin, D.H.4    Song, H.K.5    Min, K.6    Moon, J.H.7    Kim, K.K.8    Hwang, K.Y.9    Suh, S.W.10
  • 35
    • 0015197268 scopus 로고
    • Studies on starch-degrading enzymes. XIV. The multiple forms of procine, pancreatic alpha-amylase
    • Banks, W., Greenwood, C. T., and Khan, K. M. (1971). Studies on starch-degrading enzymes. XIV. The multiple forms of procine, pancreatic alpha-amylase, Carbohydr. Res. 20, 233-242.
    • (1971) Carbohydr. Res , vol.20 , pp. 233-242
    • Banks, W.1    Greenwood, C.T.2    Khan, K.M.3
  • 36
    • 0016302334 scopus 로고
    • Diffusion controlled reaction rates in spheroidal geometry. Application to repressor-operator association and membrane bound enzymes
    • Richter, P. H., and Eigen, M. (1974). Diffusion controlled reaction rates in spheroidal geometry. Application to repressor-operator association and membrane bound enzymes, Biophys. Chem. 2, 255-263.
    • (1974) Biophys. Chem , vol.2 , pp. 255-263
    • Richter, P.H.1    Eigen, M.2
  • 37
    • 0032716849 scopus 로고    scopus 로고
    • Automatic docking of maltose, 2-deoxymaltose, and maltotetraose into the soybean beta-amylase active site
    • Laederach, A., Dowd, M. K., Coutinho, P. M., and Reilly, P. J. (1999). Automatic docking of maltose, 2-deoxymaltose, and maltotetraose into the soybean beta-amylase active site, Proteins 37, 166-175.
    • (1999) Proteins , vol.37 , pp. 166-175
    • Laederach, A.1    Dowd, M.K.2    Coutinho, P.M.3    Reilly, P.J.4
  • 38
    • 0034922579 scopus 로고    scopus 로고
    • Molecular mimicry of substrate oxygen atoms by water molecules in the beta-amylase active site
    • Pujadas, G., and Palau, J. (2001). Molecular mimicry of substrate oxygen atoms by water molecules in the beta-amylase active site, Protein Sci. 10, 1645-1657.
    • (2001) Protein Sci , vol.10 , pp. 1645-1657
    • Pujadas, G.1    Palau, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.