메뉴 건너뛰기




Volumn 37, Issue 1, 1998, Pages 1-13

Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin

Author keywords

Catalytic residues; Mechanism based labelling; Multiple molecular forms; Retaining mechanism; Sequence similarity; Starch degradation

Indexed keywords

ALPHA GLUCOSIDASE; ISOENZYME; STARCH;

EID: 0031972297     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005925819741     Document Type: Review
Times cited : (124)

References (100)
  • 2
    • 0030915788 scopus 로고    scopus 로고
    • Identification of the CD45-associated 116-kDa and 80-kDa proteins as the α and β subunits of α-glucosidase II
    • Arendt CW, Ostergaard HL: Identification of the CD45-associated 116-kDa and 80-kDa proteins as the α and β subunits of α-glucosidase II. J Biol Chem 272: 13117-13125 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 13117-13125
    • Arendt, C.W.1    Ostergaard, H.L.2
  • 3
    • 0029916915 scopus 로고
    • The PROSITE database: Its status in 1995
    • Bairoch A, Bucher P, Hofmann K: The PROSITE database: its status in 1995. Nucl Acids Res 24: 189-196 (1995).
    • (1995) Nucl Acids Res , vol.24 , pp. 189-196
    • Bairoch, A.1    Bucher, P.2    Hofmann, K.3
  • 4
    • 0003341874 scopus 로고
    • Partial characterization and subcellular localization of three α-glucosidase isoforms in pea (Pisum sativum L.) seedlings
    • Beers EP, Duke SH, Henson CA: Partial characterization and subcellular localization of three α-glucosidase isoforms in pea (Pisum sativum L.) seedlings. Plant Physiol 94: 738-744 (1990).
    • (1990) Plant Physiol , vol.94 , pp. 738-744
    • Beers, E.P.1    Duke, S.H.2    Henson, C.A.3
  • 5
    • 0028860889 scopus 로고
    • Mechanism-based inhibition of yeast α-glucosidase and human pancreatic α-amylase by a new class of inhibitors
    • Braun C, Brayer GD, Withers SG: Mechanism-based inhibition of yeast α-glucosidase and human pancreatic α-amylase by a new class of inhibitors. J Biol Chem 270: 26778-26781 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 26778-26781
    • Braun, C.1    Brayer, G.D.2    Withers, S.G.3
  • 6
    • 0030760550 scopus 로고    scopus 로고
    • Structure of the Aspergillus oryzae α-amylase complexed with the inhibitor acarbose at 2.0 Å resolution
    • Brzozowski AM, Davies GJ: Structure of the Aspergillus oryzae α-amylase complexed with the inhibitor acarbose at 2.0 Å resolution. Biochemistry 36: 10837-10845 (1997).
    • (1997) Biochemistry , vol.36 , pp. 10837-10845
    • Brzozowski, A.M.1    Davies, G.J.2
  • 7
    • 0026674130 scopus 로고
    • Sequence of the complete cDNA and the 5 structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase
    • Chantret I, Lacasa M, Chevalier G, Ruf J, Islam I, Mantei N, Edwards Y, Swallow D, Rousset M: Sequence of the complete cDNA and the 5 structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase. Biochem J 285: 915-923 (1992).
    • (1992) Biochem J , vol.285 , pp. 915-923
    • Chantret, I.1    Lacasa, M.2    Chevalier, G.3    Ruf, J.4    Islam, I.5    Mantei, N.6    Edwards, Y.7    Swallow, D.8    Rousset, M.9
  • 8
    • 0002339053 scopus 로고
    • α-Glucosidases
    • The Amylase Research Society of Japan (ed) Pergamon Press, Oxford
    • Chiba S: α-Glucosidases. In: The Amylase Research Society of Japan (ed) Handbook of Amylases and Related Enzymes, pp. 104-105. Pergamon Press, Oxford (1988).
    • (1988) Handbook of Amylases and Related Enzymes , pp. 104-105
    • Chiba, S.1
  • 9
    • 0031201675 scopus 로고    scopus 로고
    • Molecular mechanism in α-glucosidase and glucoamylase
    • Chiba S: Molecular mechanism in α-glucosidase and glucoamylase. Biosci Biotechnol Biochem 61: 1233-1239 (1997).
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1233-1239
    • Chiba, S.1
  • 10
    • 84954960818 scopus 로고
    • Purification and some properties of flint corn α-glucosidase
    • Chiba S, Shimomura T: Purification and some properties of flint corn α-glucosidase. Agric Biol Chem 39: 1033-1040 (1975).
    • (1975) Agric Biol Chem , vol.39 , pp. 1033-1040
    • Chiba, S.1    Shimomura, T.2
  • 11
    • 0017821899 scopus 로고
    • Purification and properties of an α-glucosidase (glucoamylase) in sugar beet seeds
    • Chiba S, Inomata S, Matsui H, Shimomura T: Purification and properties of an α-glucosidase (glucoamylase) in sugar beet seeds. Agric Biol Chem 42: 241-245 (1978).
    • (1978) Agric Biol Chem , vol.42 , pp. 241-245
    • Chiba, S.1    Inomata, S.2    Matsui, H.3    Shimomura, T.4
  • 12
    • 0013686521 scopus 로고
    • Substrate specificity and subsite affinities of buckwheat α-glucosidase
    • Chiba S, Kanaya K, Hiromi K, Shimomura T: Substrate specificity and subsite affinities of buckwheat α-glucosidase. Agric Biol Chem 43: 237-242 (1979).
    • (1979) Agric Biol Chem , vol.43 , pp. 237-242
    • Chiba, S.1    Kanaya, K.2    Hiromi, K.3    Shimomura, T.4
  • 13
    • 0016774185 scopus 로고
    • A probable oxocarbonium ion in the reaction mechanism of small intestinal sucrase and isomaltase
    • Cogoli A, Semenza G: A probable oxocarbonium ion in the reaction mechanism of small intestinal sucrase and isomaltase. J Biol Chem 250: 7802-7809 (1975).
    • (1975) J Biol Chem , vol.250 , pp. 7802-7809
    • Cogoli, A.1    Semenza, G.2
  • 14
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies GJ, Henrissat B: Structures and mechanisms of glycosyl hydrolases. Structure 3: 853-859 (1995).
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.J.1    Henrissat, B.2
  • 15
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies GJ, Wilson KS, Henrissat B: Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J 321: 557-559 (1997).
    • (1997) Biochem J , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 16
    • 0025221711 scopus 로고
    • Cloning of the Schwanniomyces occidentalis glucoamylase gene (GAM1) and its expression in Saccharamyces cerevisiae
    • Dohmen JR, Strasser AWM, Dahlems UM, Hollenberg CP: Cloning of the Schwanniomyces occidentalis glucoamylase gene (GAM1) and its expression in Saccharamyces cerevisiae. Gene 95: 111-121 (1990).
    • (1990) Gene , vol.95 , pp. 111-121
    • Dohmen, J.R.1    Strasser, A.W.M.2    Dahlems, U.M.3    Hollenberg, C.P.4
  • 17
    • 0029900198 scopus 로고    scopus 로고
    • Mutational modulation of substrate bond-type specificity and thermostability of glucoamylase from Aspergillus awamori by replacement with short homologue active site sequences and thiol/disulfide engineering
    • Fierobe H-P, Stoffer BB, Frandsen TP, Svensson B: Mutational modulation of substrate bond-type specificity and thermostability of glucoamylase from Aspergillus awamori by replacement with short homologue active site sequences and thiol/disulfide engineering. Biochemistry 35: 8696-8704 (1996).
    • (1996) Biochemistry , vol.35 , pp. 8696-8704
    • Fierobe, H.-P.1    Stoffer, B.B.2    Frandsen, T.P.3    Svensson, B.4
  • 19
    • 0030592505 scopus 로고    scopus 로고
    • Structure and energetics of the glucoamylase-isomaltose transition-state complex probed by using modeling and deoxygenated substrates coupled with site-directed mutagenesis
    • Frandsen TP, Stoffer BB, Palcic MM, Hof S, Svensson, B: Structure and energetics of the glucoamylase-isomaltose transition-state complex probed by using modeling and deoxygenated substrates coupled with site-directed mutagenesis. J Mol Biol 263: 79-89 (1996).
    • (1996) J Mol Biol , vol.263 , pp. 79-89
    • Frandsen, T.P.1    Stoffer, B.B.2    Palcic, M.M.3    Hof, S.4    Svensson, B.5
  • 20
    • 0018786930 scopus 로고
    • Action of intestinal sucrase-isomaltase and its free monomers on an α-limit dextrin
    • Gray GM, Lally BC, Conklin KA: Action of intestinal sucrase-isomaltase and its free monomers on an α-limit dextrin. J Biol Chem 254: 6038-6043 (1979).
    • (1979) J Biol Chem , vol.254 , pp. 6038-6043
    • Gray, G.M.1    Lally, B.C.2    Conklin, K.A.3
  • 21
    • 0019332339 scopus 로고
    • Substrate specificity of rat liver microsomal glucosidases which process glycoproteins
    • Grinna LS, Robbins PW: Substrate specificity of rat liver microsomal glucosidases which process glycoproteins. J Biol Chem 255: 2255-2258 (1980).
    • (1980) J Biol Chem , vol.255 , pp. 2255-2258
    • Grinna, L.S.1    Robbins, P.W.2
  • 22
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarity
    • Henrissat B: A classification of glycosyl hydrolases based on amino acid sequence similarity. Biochem J 280: 309-316 (1991).
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 23
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid similarities
    • Henrissat B, Bairoch A: New families in the classification of glycosyl hydrolases based on amino acid similarities. Biochem J 293: 781-788 (1993).
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 24
    • 0343217744 scopus 로고
    • Barley seed α-glucosidases: Their characteristics and roles in starch degradation
    • Saddler JN, Penner, MH (eds) ACS, Washington, DC
    • Henson CA, Sun Z: Barley seed α-glucosidases: their characteristics and roles in starch degradation. In: Saddler JN, Penner, MH (eds) ACS Symposium Series 618, pp. 51-58. ACS, Washington, DC (1995).
    • (1995) ACS Symposium Series 618 , pp. 51-58
    • Henson, C.A.1    Sun, Z.2
  • 25
    • 0028557942 scopus 로고
    • The effect of a single base pair deletion (ΔT525) and a C1634T missense mutation (pro5451eu) on the expression of lysosomal α-glucosidase in patients with glycogen storage disease type II
    • Hermans MMP, de Graaff E, Kroos MA, Mohkamsing S, Eussen BJ, Joosse M, Willemsen R, Kleijer WJ, Oostra BA, Reuser AJJ: The effect of a single base pair deletion (ΔT525) and a C1634T missense mutation (pro5451eu) on the expression of lysosomal α-glucosidase in patients with glycogen storage disease type II. Hum Mol Genet 3: 2213-2218 (1994).
    • (1994) Hum Mol Genet , vol.3 , pp. 2213-2218
    • Hermans, M.M.P.1    De Graaff, E.2    Kroos, M.A.3    Mohkamsing, S.4    Eussen, B.J.5    Joosse, M.6    Willemsen, R.7    Kleijer, W.J.8    Oostra, B.A.9    Reuser, A.J.J.10
  • 27
    • 0027439832 scopus 로고
    • The conservative substitution Asp645→Glu in lysosomal α-glucosidase affects transport and phosphorylation of the enzyme in an adult patient with glycogen-storage disease type II
    • Hermans MMP, de Graaff E, Kroos MA, Wisselaar HA, Willemsen R, Oostra BA, Reuser AJJ: The conservative substitution Asp645→Glu in lysosomal α-glucosidase affects transport and phosphorylation of the enzyme in an adult patient with glycogen-storage disease type II. Biochem J 289: 687-693 (1993).
    • (1993) Biochem J , vol.289 , pp. 687-693
    • Hermans, M.M.P.1    De Graaff, E.2    Kroos, M.A.3    Wisselaar, H.A.4    Willemsen, R.5    Oostra, B.A.6    Reuser, A.J.J.7
  • 29
    • 0027304634 scopus 로고
    • Two mutations affecting the transport and maturation of lysosomal α-glucosidase in an adult case of glycogen storage disease type II
    • Hermans MMP, Kroos MA, de Graaff, E, Oostra BA, Reuser AJ: Two mutations affecting the transport and maturation of lysosomal α-glucosidase in an adult case of glycogen storage disease type II. Hum Mut 2: 268-273 (1993).
    • (1993) Hum Mut , vol.2 , pp. 268-273
    • Hermans, M.M.P.1    Kroos, M.A.2    De Graaff, E.3    Oostra, B.A.4    Reuser, A.J.5
  • 30
    • 0020687024 scopus 로고
    • Subsite structure and ligand binding mechanism of glucoamylase
    • Hiromi K, Ohnishi M, Tanaka A: Subsite structure and ligand binding mechanism of glucoamylase. Mol Cell Biochem 51: 79-95 (1983).
    • (1983) Mol Cell Biochem , vol.51 , pp. 79-95
    • Hiromi, K.1    Ohnishi, M.2    Tanaka, A.3
  • 31
    • 0024026526 scopus 로고
    • Primary structure and processing of lysosomal α-glucosidase; homology with the intestinal sucrase-isomaltase complex
    • Hoefsloot LH, Hoogeveen-Westerveld M, Kroos MA, van Beeumen J, Reuser AJ, Oostra BA: Primary structure and processing of lysosomal α-glucosidase; homology with the intestinal sucrase-isomaltase complex. EMBO J 7: 1697-1704 (1988).
    • (1988) EMBO J , vol.7 , pp. 1697-1704
    • Hoefsloot, L.H.1    Hoogeveen-Westerveld, M.2    Kroos, M.A.3    Van Beeumen, J.4    Reuser, A.J.5    Oostra, B.A.6
  • 32
    • 0028217853 scopus 로고
    • A de novo 13 nt deletion, a newly identified C647W missense mutation and a deletion of exon 18 in infantile onset glycogen storage disease type II (GSDII)
    • Huie ML, Chen AS, Brooks SS, Grix A, Hirschorn R: A de novo 13 nt deletion, a newly identified C647W missense mutation and a deletion of exon 18 in infantile onset glycogen storage disease type II (GSDII). Hum Mol Genet 3: 1081-1087 (1994).
    • (1994) Hum Mol Genet , vol.3 , pp. 1081-1087
    • Huie, M.L.1    Chen, A.S.2    Brooks, S.S.3    Grix, A.4    Hirschorn, R.5
  • 33
    • 0031047941 scopus 로고    scopus 로고
    • Characterization of the active site of Schwanniomyces occidentalis glucoamylase by in vitro mutagenesis
    • Hülseweh B, Dahlems UM, Dohmen J, Strasser AWM, Hollenberg CP: Characterization of the active site of Schwanniomyces occidentalis glucoamylase by in vitro mutagenesis. Eur J Biochem 244: 128-133 (1997).
    • (1997) Eur J Biochem , vol.244 , pp. 128-133
    • Hülseweh, B.1    Dahlems, U.M.2    Dohmen, J.3    Strasser, A.W.M.4    Hollenberg, C.P.5
  • 34
    • 0022504432 scopus 로고
    • The sucrase-isomaltase complex: Primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein
    • Hunziker W, Spiess M, Semenza G, Lodish HF: The sucrase-isomaltase complex: primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein. Cell 46: 227-234 (1986).
    • (1986) Cell , vol.46 , pp. 227-234
    • Hunziker, W.1    Spiess, M.2    Semenza, G.3    Lodish, H.F.4
  • 35
    • 0028886770 scopus 로고
    • Characterization of high pI α-glucosidase from germinated barley seeds: Substrate specificity, subsite affinities and active-site residues
    • Im H, Henson CA: Characterization of high pI α-glucosidase from germinated barley seeds: substrate specificity, subsite affinities and active-site residues. Carbohydr Res 277: 145-159. (1995).
    • (1995) Carbohydr Res , vol.277 , pp. 145-159
    • Im, H.1    Henson, C.A.2
  • 36
    • 0031026328 scopus 로고    scopus 로고
    • Altering substrate specificity of Bacillus sp. SAM1606 α-glucosidase by comparative site-specific mutagenesis
    • Inohara-Ochiai M, Nakayama T, Goto R, Nakao M, Ueda T, Shibano Y: Altering substrate specificity of Bacillus sp. SAM1606 α-glucosidase by comparative site-specific mutagenesis. J Biol Chem 272: 1601-1607 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 1601-1607
    • Inohara-Ochiai, M.1    Nakayama, T.2    Goto, R.3    Nakao, M.4    Ueda, T.5    Shibano, Y.6
  • 39
    • 0026040317 scopus 로고
    • Comparison of the domain-level organization of starch hydrolases and related enzymes
    • Jespersen HM, MacGregor EA, Sierks MR, Svensson B: Comparison of the domain-level organization of starch hydrolases and related enzymes. Biochem J 280: 51-55 (1991).
    • (1991) Biochem J , vol.280 , pp. 51-55
    • Jespersen, H.M.1    MacGregor, E.A.2    Sierks, M.R.3    Svensson, B.4
  • 42
    • 0343221074 scopus 로고
    • Improved method for purification of buckwheat α-glucosidase and some kinetic properties
    • Kanaya K-I, Chiba S, Shimomura T, Nishi K: Improved method for purification of buckwheat α-glucosidase and some kinetic properties. Agric Biol Chem 40: 1929-1936 (1976).
    • (1976) Agric Biol Chem , vol.40 , pp. 1929-1936
    • Kanaya, K.-I.1    Chiba, S.2    Shimomura, T.3    Nishi, K.4
  • 43
    • 0025130561 scopus 로고    scopus 로고
    • Purification to homogeneity and properties of glucosidase II from mung bean seedlings and suspension-cultured soybean cells
    • Kaushal GP, Pastuszak I, Hatanaka K, Elbein AD: Purification to homogeneity and properties of glucosidase II from mung bean seedlings and suspension-cultured soybean cells. J Biol Chem 265: 16271-16279.
    • J Biol Chem , vol.265 , pp. 16271-16279
    • Kaushal, G.P.1    Pastuszak, I.2    Hatanaka, K.3    Elbein, A.D.4
  • 44
    • 0001575206 scopus 로고
    • Properties of potato α-glucosidase
    • Killilea SD, Clancy MJ: Properties of potato α-glucosidase. Phytochemistry 17: 1429-1431 (1978).
    • (1978) Phytochemistry , vol.17 , pp. 1429-1431
    • Killilea, S.D.1    Clancy, M.J.2
  • 46
    • 0031180875 scopus 로고    scopus 로고
    • A catalytic amino acid and primary structure of active site in Aspergillus niger α-glucosidase
    • Kimura A, Takata M, Fukushi Y, Mori H, Matsui H, Chiba S: A catalytic amino acid and primary structure of active site in Aspergillus niger α-glucosidase. Biosci Biotechnol Biochem 61: 1091-1098 (1997).
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1091-1098
    • Kimura, A.1    Takata, M.2    Fukushi, Y.3    Mori, H.4    Matsui, H.5    Chiba, S.6
  • 47
    • 0026042790 scopus 로고
    • Primary structure and processing of the Candida tsukubaensis α-glucosidase. Homology with the rabbit intestinal sucraseisomaltase complex and human lysosomal α-glucosidase
    • Kinsella BT, Hogan S, Larkin A, Cantwell BA: Primary structure and processing of the Candida tsukubaensis α-glucosidase. Homology with the rabbit intestinal sucraseisomaltase complex and human lysosomal α-glucosidase. Eur J Biochem 202: 657-664 (1991).
    • (1991) Eur J Biochem , vol.202 , pp. 657-664
    • Kinsella, B.T.1    Hogan, S.2    Larkin, A.3    Cantwell, B.A.4
  • 48
    • 0010907005 scopus 로고
    • Partial purification and characterization of acid and neutral α-glucosidases from preclimacteric banana pulp tissues
    • Konishi Y, Kitazato S, Nakatani N: Partial purification and characterization of acid and neutral α-glucosidases from preclimacteric banana pulp tissues. Biosci Biotechnol Biochem 56: 2046-2051 (1992).
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 2046-2051
    • Konishi, Y.1    Kitazato, S.2    Nakatani, N.3
  • 49
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • Koshland DE: Stereochemistry and the mechanism of enzymatic reactions. Biol Rev 28: 416-436 (1953).
    • (1953) Biol Rev , vol.28 , pp. 416-436
    • Koshland, D.E.1
  • 50
    • 0030016344 scopus 로고    scopus 로고
    • Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center
    • Kuriki T, Kaneko H, Yanase M, Takata H, Shimada J, Handa S, Takada T, Umeyama H, Okada S: Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center. J Biol Chem 271: 17321-17329 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 17321-17329
    • Kuriki, T.1    Kaneko, H.2    Yanase, M.3    Takata, H.4    Shimada, J.5    Handa, S.6    Takada, T.7    Umeyama, H.8    Okada, S.9
  • 51
    • 0029759746 scopus 로고    scopus 로고
    • Effects of both shortening and lengthening the active site nucleophile of Bacillus circulans xylanase on catalytic activity
    • Lawson SL, Wakarchuk WW, Withers SG: Effects of both shortening and lengthening the active site nucleophile of Bacillus circulans xylanase on catalytic activity. Biochemistry 35: 10110-10118 (1996).
    • (1996) Biochemistry , vol.35 , pp. 10110-10118
    • Lawson, S.L.1    Wakarchuk, W.W.2    Withers, S.G.3
  • 52
    • 0025675652 scopus 로고
    • Glycoside hydrolases: Mechanistic information from studies with reversible and irreversible inhibitors
    • Legler G: Glycoside hydrolases: mechanistic information from studies with reversible and irreversible inhibitors. Adv Carb Chem Biochem 48: 319-385 (1990).
    • (1990) Adv Carb Chem Biochem , vol.48 , pp. 319-385
    • Legler, G.1
  • 53
    • 0343836701 scopus 로고
    • The hydrated polar-group 'gate' effect on the specificity and strength of the binding of oligosaccharides by protein receptor sites
    • Dahlbon R, Nilsson JLG (eds) Swedish Pharmaceutical Press, Stockholm
    • Lemieux RU: The hydrated polar-group 'gate' effect on the specificity and strength of the binding of oligosaccharides by protein receptor sites. In: Dahlbon R, Nilsson JLG (eds) Proceedings from the VIIIth International Symposium on Medical Chemistry 1, pp. 329-351. Swedish Pharmaceutical Press, Stockholm (1984).
    • (1984) Proceedings from the VIIIth International Symposium on Medical Chemistry , vol.1 , pp. 329-351
    • Lemieux, R.U.1
  • 55
    • 0028960133 scopus 로고
    • Identification of a de novo point mutation resulting in infantile form of Pompe's disease
    • Lin C-Y, Shieh JJ: Identification of a de novo point mutation resulting in infantile form of Pompe's disease. Biochem Biophys Res Commun 208: 886-893 (1995).
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 886-893
    • Lin, C.-Y.1    Shieh, J.J.2
  • 56
    • 0040020893 scopus 로고
    • a-Amylase, limit dextrinase, and α-glucosidase enzymes in barley and malt
    • MacGregor AW: a-Amylase, limit dextrinase, and α-glucosidase enzymes in barley and malt. CRC Crit Rev Biotechnol 5: 117-128 (1987).
    • (1987) CRC Crit Rev Biotechnol , vol.5 , pp. 117-128
    • MacGregor, A.W.1
  • 57
    • 0007553835 scopus 로고
    • Substrate specificity of an α-glucosidase in sugar beet seeds
    • Matsui H, Chiba S, Shimomura T: Substrate specificity of an α-glucosidase in sugar beet seeds. Agric Biol Chem 42: 1855-1860 (1978).
    • (1978) Agric Biol Chem , vol.42 , pp. 1855-1860
    • Matsui, H.1    Chiba, S.2    Shimomura, T.3
  • 58
    • 84969081579 scopus 로고
    • Low-molecular-activity α-glucosidase from ungerminated rice seeds
    • Matsui H, Ito H, Chiba S: Low-molecular-activity α-glucosidase from ungerminated rice seeds. Agric Biol Chem 52: 1859-1860 (1988).
    • (1988) Agric Biol Chem , vol.52 , pp. 1859-1860
    • Matsui, H.1    Ito, H.2    Chiba, S.3
  • 60
    • 0030883742 scopus 로고    scopus 로고
    • 8-barrel domain of barley α-amylase
    • 8-barrel domain of barley α-amylase. J Biol Chem 272: 22456-22463 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 22456-22463
    • Matsui, I.1    Svensson, B.2
  • 61
    • 0028098225 scopus 로고
    • Roles of the aromatic residues conserved in the active center of Saccharomycopsis α-amylase for transglycosylation and hydrolysis activity
    • Matsui I, Yoneda S, Ishikawa K, Miyairi S, Fukui S, Umeyama H, Honda K: Roles of the aromatic residues conserved in the active center of Saccharomycopsis α-amylase for transglycosylation and hydrolysis activity. Biochemistry 33: 451-458 (1994).
    • (1994) Biochemistry , vol.33 , pp. 451-458
    • Matsui, I.1    Yoneda, S.2    Ishikawa, K.3    Miyairi, S.4    Fukui, S.5    Umeyama, H.6    Honda, K.7
  • 62
    • 0028609166 scopus 로고
    • Mechanisms of enzymatic glycoside hydrolysis
    • McCarter JD, Withers SG: Mechanisms of enzymatic glycoside hydrolysis. Curr Opin Struct Biol 4: 885-892 (1994).
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 885-892
    • McCarter, J.D.1    Withers, S.G.2
  • 63
    • 0030031965 scopus 로고    scopus 로고
    • 5-Fluoro glucosides: A new class of mechanism-based inhibitors of both α- and β-glucosidases
    • McCarter JD, Withers SG: 5-Fluoro glucosides: a new class of mechanism-based inhibitors of both α- and β-glucosidases. J Am Chem Soc 118: 241-242 (1996).
    • (1996) J Am Chem Soc , vol.118 , pp. 241-242
    • McCarter, J.D.1    Withers, S.G.2
  • 64
    • 0029915713 scopus 로고    scopus 로고
    • Unequivocal identification of Asp-214 as the catalytic nucleophile of Saccharomyces cerevisiae α-glucosidase using 5-fluoro glycosyl fluorides
    • McCarter JD, Withers SG: Unequivocal identification of Asp-214 as the catalytic nucleophile of Saccharomyces cerevisiae α-glucosidase using 5-fluoro glycosyl fluorides. J Biol Chem 271: 6889-6894 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 6889-6894
    • McCarter, J.D.1    Withers, S.G.2
  • 66
    • 0342489012 scopus 로고
    • Mammalian a-glucosidases (Mammalian blood serum and human urine)
    • The Amylase Research Society of Japan (ed) Pergamon Press, Oxford
    • Minamiura N: Mammalian a-glucosidases (Mammalian blood serum and human urine). In: The Amylase Research Society of Japan (ed) Handbook of Amylases and Related Enzymes, pp. 105-109. Pergamon Press, Oxford (1988).
    • (1988) Handbook of Amylases and Related Enzymes , pp. 105-109
    • Minamiura, N.1
  • 67
    • 0029347189 scopus 로고
    • Nucleotide sequence and expression of α-glucosidase-encoding gene (agdA) from Aspergillus oryzae
    • Minetoki T, Gomi K, Kitamoto K, Kumagai C, Tamura G: Nucleotide sequence and expression of α-glucosidase-encoding gene (agdA) from Aspergillus oryzae. Biosci Biotechnol Biochem 59: 1516-1521 (1995).
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 1516-1521
    • Minetoki, T.1    Gomi, K.2    Kitamoto, K.3    Kumagai, C.4    Tamura, G.5
  • 68
    • 0028213490 scopus 로고
    • Glycosidases of the asparagine-linked oligosaccharide processing pathway
    • Moremen KW, Trimble RB, Herscovics A: Glycosidases of the asparagine-linked oligosaccharide processing pathway. Glycobiology 4: 113-125 (1994).
    • (1994) Glycobiology , vol.4 , pp. 113-125
    • Moremen, K.W.1    Trimble, R.B.2    Herscovics, A.3
  • 69
    • 0026041607 scopus 로고
    • Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal α-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene
    • Naim HY, Niermann T, Kleinhans U, Hollenberg CP, Strasser AWM: Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal α-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene. FEBS Lett 294: 109-112 (1991).
    • (1991) FEBS Lett , vol.294 , pp. 109-112
    • Naim, H.Y.1    Niermann, T.2    Kleinhans, U.3    Hollenberg, C.P.4    Strasser, A.W.M.5
  • 71
    • 0001454857 scopus 로고
    • Molecular recognition X. A novel procedure for the detection of the intermolecular hydrogen bonds present in a protein-oligosaccharide complex
    • Nikrad PV, Beierbeck H, Lemieux RU: Molecular recognition X. A novel procedure for the detection of the intermolecular hydrogen bonds present in a protein-oligosaccharide complex. Can J Chem 70: 241-253 (1992).
    • (1992) Can J Chem , vol.70 , pp. 241-253
    • Nikrad, P.V.1    Beierbeck, H.2    Lemieux, R.U.3
  • 72
    • 0342814062 scopus 로고
    • α-Glucosidase from grape berries: Partial purification and characterization
    • Peruffo ADB, Renosto F, Pallavicini C: α-Glucosidase from grape berries: partial purification and characterization. Planta 142: 195-201 (1978).
    • (1978) Planta , vol.142 , pp. 195-201
    • Peruffo, A.D.B.1    Renosto, F.2    Pallavicini, C.3
  • 73
    • 0028198814 scopus 로고
    • The active centre of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution
    • Qian M, Haser R, Buisson G, Duée E, Payan F: The active centre of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution. Biochemistry 33: 6284-6294 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duée, E.4    Payan, F.5
  • 74
    • 0017121125 scopus 로고
    • Partial amino acid sequences around the essential carboxylate in the active sites of the intestinal sucrase-isomaltase complex
    • Quaroni A, Semenza G: Partial amino acid sequences around the essential carboxylate in the active sites of the intestinal sucrase-isomaltase complex. J Biol Chem 251: 3250-3253 (1976).
    • (1976) J Biol Chem , vol.251 , pp. 3250-3253
    • Quaroni, A.1    Semenza, G.2
  • 75
    • 0027215304 scopus 로고
    • Probing the atomic interactions between proteins and carbohydrates
    • Quiocho FA: Probing the atomic interactions between proteins and carbohydrates. Biochem Soc Trans 21: 442-448 (1993).
    • (1993) Biochem Soc Trans , vol.21 , pp. 442-448
    • Quiocho, F.A.1
  • 76
    • 0026515012 scopus 로고
    • Kinetic identification of a hydrogen bonding pair in the glucoamylase/maltose transition state complex
    • Sierks MR, Svensson B: Kinetic identification of a hydrogen bonding pair in the glucoamylase/maltose transition state complex. Protein Eng 5: 185-188 (1992).
    • (1992) Protein Eng , vol.5 , pp. 185-188
    • Sierks, M.R.1    Svensson, B.2
  • 77
    • 0026705218 scopus 로고
    • Active site similarities of glucose dehydrogenase, glucose oxidase and glueoamylase probed by deoxygenated substrates
    • Sierks MR, Bock K, Refn S, Svensson B: Active site similarities of glucose dehydrogenase, glucose oxidase and glueoamylase probed by deoxygenated substrates. Biochemistry 31: 8972-8977 (1992).
    • (1992) Biochemistry , vol.31 , pp. 8972-8977
    • Sierks, M.R.1    Bock, K.2    Refn, S.3    Svensson, B.4
  • 78
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnott ML: Catalytic mechanisms of enzymic glycosyl transfer. Chem Rev 90: 1171-1202 (1990).
    • (1990) Chem Rev , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 79
    • 0004670366 scopus 로고
    • Hydrolysis of barley starch granules by α-glucosidases from malt
    • Sissons, MJ, MacGregor AW: Hydrolysis of barley starch granules by α-glucosidases from malt. J Cereal Sci 19: 161-169 (1994).
    • (1994) J Cereal Sci , vol.19 , pp. 161-169
    • Sissons, M.J.1    MacGregor, A.W.2
  • 80
    • 0028961637 scopus 로고
    • X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases
    • Strokopytov B, Penninga D, Rozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW: X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases. Biochemistry 34: 2234-2240 (1995).
    • (1995) Biochemistry , vol.34 , pp. 2234-2240
    • Strokopytov, B.1    Penninga, D.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkhuizen, L.5    Dijkstra, B.W.6
  • 81
    • 0029931070 scopus 로고    scopus 로고
    • Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 Å resolution. Implications for product specificity
    • Strokopytov B, Knegtel RMA, Penninga D, Rozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW: Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 Å resolution. Implications for product specificity. Biochemistry 35: 4241-4249 (1996).
    • (1996) Biochemistry , vol.35 , pp. 4241-4249
    • Strokopytov, B.1    Knegtel, R.M.A.2    Penninga, D.3    Rozeboom, H.J.4    Kalk, K.H.5    Dijkhuizen, L.6    Dijkstra, B.W.7
  • 82
    • 0029972508 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and expression of a cDNA encoding a-glucosidase from Mucor javanicus
    • Sugimoto M, Suzuki Y: Molecular cloning, sequencing, and expression of a cDNA encoding a-glucosidase from Mucor javanicus. J Biochem 119: 500-505 (1996).
    • (1996) J Biochem , vol.119 , pp. 500-505
    • Sugimoto, M.1    Suzuki, Y.2
  • 83
    • 0028890556 scopus 로고
    • Multiple molecular forms of a-glucosidase from spinach seeds, Spinacia oleracea L
    • Sugimoto M, Furui S, Suzuki Y: Multiple molecular forms of a-glucosidase from spinach seeds, Spinacia oleracea L. Biosci Biotechnol Biochem 59: 673-677 (1995).
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 673-677
    • Sugimoto, M.1    Furui, S.2    Suzuki, Y.3
  • 84
    • 0031106232 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA encoding α-glucosidase from spinach
    • Sugimoto M, Furui S, Suzuki Y: Molecular cloning and characterization of a cDNA encoding α-glucosidase from spinach. Plant Mol Biol 33: 765-768 (1997).
    • (1997) Plant Mol Biol , vol.33 , pp. 765-768
    • Sugimoto, M.1    Furui, S.2    Suzuki, Y.3
  • 85
    • 0000112493 scopus 로고
    • Degradation of native starch granules by barley α-glucosidases
    • Sun Z, Henson CA: Degradation of native starch granules by barley α-glucosidases. Plant Physiol 94: 320-327 (1990).
    • (1990) Plant Physiol , vol.94 , pp. 320-327
    • Sun, Z.1    Henson, C.A.2
  • 86
    • 0028843003 scopus 로고
    • The role of pea chloroplast a-glucosidase in transitory starch degradation
    • Sun Z, Duke SH, Henson CA: The role of pea chloroplast a-glucosidase in transitory starch degradation. Plant Physiol 108: 211-217 (1995).
    • (1995) Plant Physiol , vol.108 , pp. 211-217
    • Sun, Z.1    Duke, S.H.2    Henson, C.A.3
  • 87
    • 0342923148 scopus 로고
    • Three forms of α-glucosidase from welsh onion (Allium fistulosum L.)
    • Suzuki Y, Uchida K: Three forms of α-glucosidase from welsh onion (Allium fistulosum L.). Agric Biol Chem 48: 1343-1345 (1984).
    • (1984) Agric Biol Chem , vol.48 , pp. 1343-1345
    • Suzuki, Y.1    Uchida, K.2
  • 88
    • 0028429952 scopus 로고
    • Protein engineering in the a-amylase family: Catalytic mechanism, substrate specificity, and stability
    • Svensson B: Protein engineering in the a-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol Biol 25: 141-157 (1994).
    • (1994) Plant Mol Biol , vol.25 , pp. 141-157
    • Svensson, B.1
  • 89
    • 0027299062 scopus 로고
    • Mutational analysis of glycosylase function
    • Svensson B, Søgaard M: Mutational analysis of glycosylase function. J Biotechnol 29: 1-37 (1993).
    • (1993) J Biotechnol , vol.29 , pp. 1-37
    • Svensson, B.1    Søgaard, M.2
  • 90
    • 0022726639 scopus 로고
    • Purification and properties of glucosidase I from mung bean seedlings
    • Szumilo T, Kaushal GP, Elbein AD: Purification and properties of glucosidase I from mung bean seedlings. Arch Biochem Biophys 247: 261-271 (1986).
    • (1986) Arch Biochem Biophys , vol.247 , pp. 261-271
    • Szumilo, T.1    Kaushal, G.P.2    Elbein, A.D.3
  • 91
    • 0000433250 scopus 로고
    • Studies on α-glucosidase in rice. Part I. Isolation and some properties of α-glucosidase I and α-glucosidase II
    • Takahashi N, Shimomura T, Chiba S: Studies on α-glucosidase in rice. Part I. Isolation and some properties of α-glucosidase I and α-glucosidase II. Agric Biol Chem 35: 2015-2024 (1971).
    • (1971) Agric Biol Chem , vol.35 , pp. 2015-2024
    • Takahashi, N.1    Shimomura, T.2    Chiba, S.3
  • 92
    • 0028595690 scopus 로고
    • Transition state structures for the hydrolysis of α-D-glucopyranosyl fluoride by retaining and inverting reactions of glycosylases
    • Tanaka Y, Tao W, Blanchard JS, Hehre EJ: Transition state structures for the hydrolysis of α-D-glucopyranosyl fluoride by retaining and inverting reactions of glycosylases. J Biol Chem 269: 32306-32312 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 32306-32312
    • Tanaka, Y.1    Tao, W.2    Blanchard, J.S.3    Hehre, E.J.4
  • 94
    • 0030050498 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a gibberellin-inducible, putative a-glucosidase gene from barley
    • Tibbot BK, Skadsen RW: Molecular cloning and characterization of a gibberellin-inducible, putative a-glucosidase gene from barley. Plant Mol Biol 30: 229-241 (1996).
    • (1996) Plant Mol Biol , vol.30 , pp. 229-241
    • Tibbot, B.K.1    Skadsen, R.W.2
  • 95
    • 0031591389 scopus 로고    scopus 로고
    • The refined structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: Structural characterization of proline-substitution sites for protein thermostabilization
    • Watanabe K, Hata Y, Kizaki H, Katsube Y, Suzuki Y: The refined structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: structural characterization of proline-substitution sites for protein thermostabilization. J Mol Biol 269: 142-153 (1997).
    • (1997) J Mol Biol , vol.269 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5
  • 96
    • 0028943508 scopus 로고
    • Approaches to labelling and identification of active site residues in glycosidases
    • Withers SG, Aebersold R: Approaches to labelling and identification of active site residues in glycosidases. Protein Sci 4: 361-372 (1995).
    • (1995) Protein Sci , vol.4 , pp. 361-372
    • Withers, S.G.1    Aebersold, R.2
  • 97
    • 0342489007 scopus 로고
    • Purification and properties of three forms of a-glucosidase from germinated green gram (Phaseolus vidissimus Ten.)
    • Yamasaki Y, Suzuki Y: Purification and properties of three forms of a-glucosidase from germinated green gram (Phaseolus vidissimus Ten.). Agric Biol Chem 43: 481-489 (1979).
    • (1979) Agric Biol Chem , vol.43 , pp. 481-489
    • Yamasaki, Y.1    Suzuki, Y.2
  • 98
    • 0343358332 scopus 로고
    • Two forms of α-glucosidase from sugar-beet seeds
    • Yamasaki Y, Suzuki Y: Two forms of α-glucosidase from sugar-beet seeds. Planta 148: 354-361 (1980).
    • (1980) Planta , vol.148 , pp. 354-361
    • Yamasaki, Y.1    Suzuki, Y.2
  • 99
    • 0345189669 scopus 로고
    • Two forms of α-glucosidase from soybean callus
    • Yamasaki Y, Konno H: Two forms of α-glucosidase from soybean callus. Agric Biol Chem 49: 849-850 (1985).
    • (1985) Agric Biol Chem , vol.49 , pp. 849-850
    • Yamasaki, Y.1    Konno, H.2
  • 100
    • 0030823127 scopus 로고    scopus 로고
    • Crystal structures of a mutant maltotetraose-forming exoamylase cocrystallized with maltopentaose
    • Yoshioka Y, Hasegawa K, Matsuura Y, Katsube Y, Kubota M: Crystal structures of a mutant maltotetraose-forming exoamylase cocrystallized with maltopentaose. J Mol Biol 271: 619-628 (1997).
    • (1997) J Mol Biol , vol.271 , pp. 619-628
    • Yoshioka, Y.1    Hasegawa, K.2    Matsuura, Y.3    Katsube, Y.4    Kubota, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.