메뉴 건너뛰기




Volumn 57, Issue SUPPL. 11, 2002, Pages 171-180

Action pattern of α-amylases on modified maltooligosaccharides

Author keywords

maltooligosaccharide glycosides; Action patterns; Bacillus licheniformis amylase; Chemoenzymatic syntheses; Human salivary amylase; Porcine pancreatic amylase

Indexed keywords

BACILLUS LICHENIFORMIS; ORYCTOLAGUS CUNICULUS; SUIDAE;

EID: 0347628155     PISSN: 13356399     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (14)

References (22)
  • 1
    • 0032520085 scopus 로고    scopus 로고
    • The mechanism of porcine pancreatic α-amylase. Inhibition of maltopentaose hydrolysis by acarbose, maltose and maltotriose
    • AL KAZAZ, M., DESSEAUX, V., MARCHIS-MOUREN, G., PRODANOV, E. & SANTIMONE, M. 1998. The mechanism of porcine pancreatic α-amylase. Inhibition of maltopentaose hydrolysis by acarbose, maltose and maltotriose. Eur. J. Biochem. 252: 100-107.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 100-107
    • Al Kazaz, M.1    Desseaux, V.2    Marchis-Mouren, G.3    Prodanov, E.4    Santimone, M.5
  • 2
    • 0034712653 scopus 로고    scopus 로고
    • Subsite mapping of the human pancreatic α-amylase active site through structural, kinetic, and mutagenesis techniques
    • BRAVER, G. D., SIDHU, G., MAURUS, R., RYDBERG, E. H., BRAUN, C., WANG, Y., NGUYEN, N. T., OVERALL, C. M. & WITHERS, G. S. 2000. Subsite mapping of the human pancreatic α-amylase active site through structural, kinetic, and mutagenesis techniques. Biochemistry 39: 4778-4791.
    • (2000) Biochemistry , vol.39 , pp. 4778-4791
    • Braver, G.D.1    Sidhu, G.2    Maurus, R.3    Rydberg, E.H.4    Braun, C.5    Wang, Y.6    Nguyen, N.T.7    Overall, C.M.8    Withers, G.S.9
  • 3
    • 0034605567 scopus 로고    scopus 로고
    • Oligosaccharide synthesis by reversed catalysis using α-amylase from Bacillus licheniformis
    • CHITRADON, L., MAHAKHAN, P. & BUCKE, C. 2000. Oligosaccharide synthesis by reversed catalysis using α-amylase from Bacillus licheniformis. J. Mol. Catal. B10: 273-280.
    • (2000) J. Mol. Catal. , vol.B10 , pp. 273-280
    • Chitradon, L.1    Mahakhan, P.2    Bucke, C.3
  • 4
    • 0034714134 scopus 로고    scopus 로고
    • Probing structural determinants specifying high thermostability in Bacillus licheniformis α-amylase
    • DECLERCK, N., MACHIUS, M., WIEGAND, G., HUBER, R. & GAILLARDIN, C. 2000. Probing structural determinants specifying high thermostability in Bacillus licheniformis α-amylase. J. Mol. Biol. 301: 1041-1057.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1041-1057
    • Declerck, N.1    Machius, M.2    Wiegand, G.3    Huber, R.4    Gaillardin, C.5
  • 5
    • 0343487716 scopus 로고    scopus 로고
    • Synthesis of chromogenic substrates of α-amylases on a cyclodextrin basis
    • FARKAS, E., JÁNOSSY, L. HARANGI, J., KANDRA, L. & LIPTAK, A. 1997. Synthesis of chromogenic substrates of α-amylases on a cyclodextrin basis. Carbohydr. Res. 303: 407-415.
    • (1997) Carbohydr. Res. , vol.303 , pp. 407-415
    • Farkas, E.1    Jánossy, L.2    Harangi, J.3    Kandra, L.4    Liptak, A.5
  • 6
    • 0002051360 scopus 로고
    • FOGARTY, W.M. (ed.) Applied Science Publishers Ltd., London
    • FOGARTY, W.M. 1983. Microbiol enzymes and biotechnology, pp. 1-92. In: FOGARTY, W.M. (ed.) Applied Science Publishers Ltd., London.
    • (1983) Microbiol Enzymes and Biotechnology , pp. 1-92
    • Fogarty, W.M.1
  • 7
    • 0034680692 scopus 로고    scopus 로고
    • Examination of the active sites of human salivary α-amylase (HSA)
    • KANDRA, L. & GYÉMÁNT, G. 2000. Examination of the active sites of human salivary α-amylase (HSA). Carbohydr. Res. 329: 579-585.
    • (2000) Carbohydr. Res. , vol.329 , pp. 579-585
    • Kandra, L.1    Gyémánt, G.2
  • 8
    • 0342940771 scopus 로고    scopus 로고
    • Action pattern of porcine pancreatic α-amylase on three different series of β-maltooligosaccharide glycosides
    • KANDRA, L., GYÉMÁNT, G. & LIPTÁK, A. 1997. Action pattern of porcine pancreatic α-amylase on three different series of β-maltooligosaccharide glycosides. Carbohydr. Res. 298: 237-242.
    • (1997) Carbohydr. Res. , vol.298 , pp. 237-242
    • Kandra, L.1    Gyémánt, G.2    Lipták, A.3
  • 9
    • 0344348934 scopus 로고    scopus 로고
    • Chemoenzymatic preparation of 2-chloro-4-nitrophenyl β-maltooligosaccharide glycosides using glycogen phosphorylase b
    • KANDRA, L., GYÉMÁNT, G. & LIPTAK, A. 1999. Chemoenzymatic preparation of 2-chloro-4-nitrophenyl β-maltooligosaccharide glycosides using glycogen phosphorylase b. Carbohydr. Res. 315: 180-186.
    • (1999) Carbohydr. Res. , vol.315 , pp. 180-186
    • Kandra, L.1    Gyémánt, G.2    Liptak, A.3
  • 10
    • 0035800113 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of 2-chloro-4-nitrophenyl β-maltoheptaoside acceptor-products using glycogen phosphorylase b
    • KANDRA, L., GYÉMÁNT, G., PAL, M., PETRÓ, M., REMENYIK, J. & LIPTÁK, A. 2001. Chemoenzymatic synthesis of 2-chloro-4-nitrophenyl β-maltoheptaoside acceptor-products using glycogen phosphorylase b. Carbohydr. Res. 333: 129-136.
    • (2001) Carbohydr. Res. , vol.333 , pp. 129-136
    • Kandra, L.1    Gyémánt, G.2    Pal, M.3    Petró, M.4    Remenyik, J.5    Lipták, A.6
  • 11
    • 0032976301 scopus 로고    scopus 로고
    • The concept of the α-amylase family: Structural similarity and common catalytic mechanism
    • KURIKI, T. & IMANAKA, T. 1999. The concept of the α-amylase family: structural similarity and common catalytic mechanism. J. Biosci. Bioeng. 87: 557-565.
    • (1999) J. Biosci. Bioeng. , vol.87 , pp. 557-565
    • Kuriki, T.1    Imanaka, T.2
  • 12
    • 84941610417 scopus 로고
    • Evaluation of α-amylase assays with 4-nitrophenyl-α-oligosaccharides as substrates
    • LORENTZ, K. 1983. Evaluation of α-amylase assays with 4-nitrophenyl-α-oligosaccharides as substrates. J. Clin. Chem. Clin. Biochem. 7: 463-471.
    • (1983) J. Clin. Chem. Clin. Biochem. , vol.7 , pp. 463-471
    • Lorentz, K.1
  • 13
    • 0028933531 scopus 로고
    • Crystal structure of Ca-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution
    • MACHIUS, M., WIEGAND, G. & HUBER, R. 1995. Crystal structure of Ca-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. J. Mol. Biol. 246: 545-559.
    • (1995) J. Mol. Biol. , vol.246 , pp. 545-559
    • Machius, M.1    Wiegand, G.2    Huber, R.3
  • 14
    • 13144305048 scopus 로고    scopus 로고
    • Activation of Bacillus licheniformis α-amylase through a disorder-order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad
    • MACHIUS, M., DECLERCK, N., HUBER, R. && WIEGAND, G. 1998. Activation of Bacillus licheniformis α-amylase through a disorder-order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure 15: 281-292.
    • (1998) Structure , vol.15 , pp. 281-292
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 16
    • 0001283165 scopus 로고
    • Action patterns of various exo-amylases and the anomeric configurations of their products
    • NAKAKUKI, T., AZUMA, K. & KAINUMA, K. 1984. Action patterns of various exo-amylases and the anomeric configurations of their products. Carbohydr. Res. 128: 297-310.
    • (1984) Carbohydr. Res. , vol.128 , pp. 297-310
    • Nakakuki, T.1    Azuma, K.2    Kainuma, K.3
  • 17
    • 0030725286 scopus 로고    scopus 로고
    • Structure of a pancreatic α-amylase bound to a substrate analogue at 2.03 Å resolution
    • QIAN, M., SPINELLI, S., DRIGUEZ, H. & PAYAN, F. 1997. Structure of a pancreatic α-amylase bound to a substrate analogue at 2.03 Å resolution. Protein Sci. 6: 2285-2296.
    • (1997) Protein Sci. , vol.6 , pp. 2285-2296
    • Qian, M.1    Spinelli, S.2    Driguez, H.3    Payan, F.4
  • 18
    • 0001631469 scopus 로고    scopus 로고
    • Structure of human salivary α-amylase at 1.6 Å resolution: Implications for its role in the oral cavity
    • RAMASUBBU, N., PALOTH, V., LUO, Y., BRAYER, G. D. & LEVINE, M. J. 1996. Structure of human salivary α-amylase at 1.6 Å resolution: implications for its role in the oral cavity. Acta Cryst. D52: 435-446.
    • (1996) Acta Cryst. , vol.D52 , pp. 435-446
    • Ramasubbu, N.1    Paloth, V.2    Luo, Y.3    Brayer, G.D.4    Levine, M.J.5
  • 19
    • 0014803288 scopus 로고
    • Multiple attack and polarity of action of porcine pancreatic α-amylase
    • ROBYT, J. F. & FRENCH, D. 1970. Multiple attack and polarity of action of porcine pancreatic α-amylase. Arch. Biochem Biophys. 138: 662-670.
    • (1970) Arch. Biochem Biophys. , vol.138 , pp. 662-670
    • Robyt, J.F.1    French, D.2
  • 20
    • 0008660998 scopus 로고
    • WHISTLER, R. L. & PASCHALL, E. F. (eds) Academic Press, New York
    • SHILDNECK, P. & SMITH, C. E. 1967. Starch: chemistry and technology, pp. 217-235. In: WHISTLER, R. L. & PASCHALL, E. F. (eds) Academic Press, New York.
    • (1967) Starch: Chemistry and Technology , pp. 217-235
    • Shildneck, P.1    Smith, C.E.2
  • 21
    • 0024469173 scopus 로고
    • Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylase
    • VIOLET, M. & MEUNIER, J.-C. 1989. Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylase. Biochem. J. 263: 665-670.
    • (1989) Biochem. J. , vol.263 , pp. 665-670
    • Violet, M.1    Meunier, J.-C.2
  • 22
    • 0023764706 scopus 로고
    • Development of a direct assay for α-amylase
    • WINN-DEEN, E. S., DAVID, H., SIGLER, G. & PHAVEZ, R. 1988. Development of a direct assay for α-amylase. Clin. Chem. 10: 2005-2008.
    • (1988) Clin. Chem. , vol.10 , pp. 2005-2008
    • Winn-Deen, E.S.1    David, H.2    Sigler, G.3    Phavez, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.