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Volumn 78, Issue 12, 2014, Pages 2064-2068

Production of 1,5-anhydro-D-fructose by an α-glucosidase belonging to glycoside hydrolase family 31

Author keywords

1,5 anhydro D fructose; Elimination mechanism; GH31 glucosidase

Indexed keywords

ASPERGILLUS; CHEMICAL REACTIONS; HYDROLASES; SUGARS;

EID: 84924607581     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1080/09168451.2014.943651     Document Type: Article
Times cited : (1)

References (26)
  • 1
    • 1342283939 scopus 로고    scopus 로고
    • α-1,4-Glucan lyase, a new starch processing enzyme for production of 1,5-anhydro-D-fructose
    • Yu S. α-1,4-Glucan lyase, a new starch processing enzyme for production of 1,5-anhydro-D-fructose. Zuckerindustrie. 2004;129: 26-30.
    • (2004) Zuckerindustrie. , vol.129 , pp. 26-30
    • Yu, S.1
  • 2
    • 0027499832 scopus 로고
    • α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. I. Efficient purification and characterization from red seaweeds
    • Yu S, Kenne L, Peders̈en M. α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. I. Efficient purification and characterization from red seaweeds. Biochim. Biophys. Acta. 1993;1156:313-320.
    • (1993) Biochim. Biophys. Acta. , vol.1156 , pp. 313-320
    • Yu, S.1    Kenne, L.2    Peders̈en, M.3
  • 3
    • 0027492818 scopus 로고
    • α-1,4-Glucan lyase, a new class of starch/gly-cogen-degrading enzyme. II. Subcellular localization and partial amino acid sequence
    • Yu S, Peders̈en M. α-1,4-Glucan lyase, a new class of starch/gly-cogen-degrading enzyme. II. Subcellular localization and partial amino acid sequence. Planta. 1993;191:137-142.
    • (1993) Planta. , vol.191 , pp. 137-142
    • Yu, S.1    Peders̈en, M.2
  • 4
    • 0032753606 scopus 로고    scopus 로고
    • Characterization of exo-(1,4)-α glucan lyase from red alga Gracilaria chorda. Activation, inactivation and the kinetic properties of the enzyme
    • Yoshinaga K, Fujisue M, Abe J, Hanashiro I, Takeda Y, Muroya K, Hizukuri S. Characterization of exo-(1,4)-α glucan lyase from red alga Gracilaria chorda. Activation, inactivation and the kinetic properties of the enzyme. Biochim. Biophys. Acta. 1999;1472:447-454.
    • (1999) Biochim. Biophys. Acta. , vol.1472 , pp. 447-454
    • Yoshinaga, K.1    Fujisue, M.2    Abe, J.3    Hanashiro, I.4    Takeda, Y.5    Muroya, K.6    Hizukuri, S.7
  • 6
    • 0030432418 scopus 로고    scopus 로고
    • Hepatic production of 1,5-anhydrofructose and 1,5-anhydroglucitol in rat by the third glycogenolytic pathway
    • Kametani S, Shiga Y, Akanuma H. Hepatic production of 1,5-anhydrofructose and 1,5-anhydroglucitol in rat by the third glycogenolytic pathway. Eur. J. Biochem. 1996;242:832-838.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 832-838
    • Kametani, S.1    Shiga, Y.2    Akanuma, H.3
  • 7
    • 0030965769 scopus 로고    scopus 로고
    • Efficient purification, characterization and partial amino acid sequencing of two α-1,4-glucan lyases from fungi
    • Yu S, Christensen TMIE, Kragh KM, Bojsen K, Marcussen J. Efficient purification, characterization and partial amino acid sequencing of two α-1,4-glucan lyases from fungi. Biochim. Biophys. Acta. 1997;1339:311-320.
    • (1997) Biochim. Biophys. Acta. , vol.1339 , pp. 311-320
    • Yu, S.1    Christensen, T.M.I.E.2    Kragh, K.M.3    Bojsen, K.4    Marcussen, J.5
  • 8
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1991;280:309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 9
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1993;293:781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 10
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat B, Bairoch A. Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 1996;316:695-696.
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 11
    • 72649094480 scopus 로고    scopus 로고
    • The first α-1,3-glucosidase from bacterial origin belonging to glycoside hydrolase family 31
    • Kang MS, Okuyama M, Mori H, Kimura A. The first α-1,3-glucosidase from bacterial origin belonging to glycoside hydrolase family 31. Biochimie. 2009;91:1434-1442.
    • (2009) Biochimie. , vol.91 , pp. 1434-1442
    • Kang, M.S.1    Okuyama, M.2    Mori, H.3    Kimura, A.4
  • 12
    • 33745048293 scopus 로고    scopus 로고
    • Structure of the Sulfolobus solfataricus α-glucosidase: Implications for domain conservation and substrate recognition in GH31
    • Ernst HA, Lo Leggio L, Willemoës M, Leonard G, Blum P, Larsen S. Structure of the Sulfolobus solfataricus α-glucosidase: Implications for domain conservation and substrate recognition in GH31. J. Mol. Biol. 2006;358:1106-1124.
    • (2006) J. Mol. Biol. , vol.358 , pp. 1106-1124
    • Ernst, H.A.1    Lo Leggio, L.2    Willemoës, M.3    Leonard, G.4    Blum, P.5    Larsen, S.6
  • 13
    • 12544256784 scopus 로고    scopus 로고
    • Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate
    • Lovering AL, Lee SS, Kim YW, Withers SG, Strynadka NC. Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate. J. Biol. Chem. 2005;280:2105-2115.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2105-2115
    • Lovering, A.L.1    Lee, S.S.2    Kim, Y.W.3    Withers, S.G.4    Strynadka, N.C.5
  • 14
    • 0035006850 scopus 로고    scopus 로고
    • Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe
    • Okuyama M, Okuno A, Shimizu N, Mori H, Kimura A, Chiba S. Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe. Eur. J. Biochem. 2001;268:2270-2280.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2270-2280
    • Okuyama, M.1    Okuno, A.2    Shimizu, N.3    Mori, H.4    Kimura, A.5    Chiba, S.6
  • 15
    • 0032797473 scopus 로고    scopus 로고
    • α-1,4-Glucan lyases producing 1,5-anhydro-D -fructose from starch and glycogen have sequence similarity to α-glucosidases
    • Yu S, Bojsen K, Svensson B, Marcussen J. α-1,4-Glucan lyases producing 1,5-anhydro-D -fructose from starch and glycogen have sequence similarity to α-glucosidases. Biochim. Biophys. Acta. 1999;1433:1-15.
    • (1999) Biochim. Biophys. Acta. , vol.1433 , pp. 1-15
    • Yu, S.1    Bojsen, K.2    Svensson, B.3    Marcussen, J.4
  • 16
    • 0242675935 scopus 로고    scopus 로고
    • Detailed dissection of a new mechanism for glycoside cleavage: α-1,4-glucan lyase
    • Lee SS, Yu S, Withers SG. Detailed dissection of a new mechanism for glycoside cleavage: α-1,4-glucan lyase. Biochemistry. 2003;42:13081-13090.
    • (2003) Biochemistry. , vol.42 , pp. 13081-13090
    • Lee, S.S.1    Yu, S.2    Withers, S.G.3
  • 17
    • 84954871548 scopus 로고
    • Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger
    • Kita A, Matsui H, Somoto A, Kimura A, Takata M, Chiba S. Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger. Agric. Biol. Chem. 1991;55:2327-2335.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 2327-2335
    • Kita, A.1    Matsui, H.2    Somoto, A.3    Kimura, A.4    Takata, M.5    Chiba, S.6
  • 18
    • 84871716252 scopus 로고    scopus 로고
    • Key aromatic residues, at subsites +2 and +3 of glycoside hydrolase family 31 α glucosidase contribute to recognition on long-chain substrates
    • Tagami T, Okuyama M, Nakai H, Kim YM, Mori H, Taguchi K, Svensson B, Kimura A. Key aromatic residues, at subsites +2 and +3 of glycoside hydrolase family 31 α glucosidase contribute to recognition on long-chain substrates. Biochim. Biophys. Acta. 2013;1834:329-335.
    • (2013) Biochim. Biophys. Acta. , vol.1834 , pp. 329-335
    • Tagami, T.1    Okuyama, M.2    Nakai, H.3    Kim, Y.M.4    Mori, H.5    Taguchi, K.6    Svensson, B.7    Kimura, A.8
  • 19
    • 0031393884 scopus 로고    scopus 로고
    • Methods for the assay of 1,5-anhydro-D -fructose and α-1,4-glucan lyase
    • Yu S, Olsen CE, Marcussen J. Methods for the assay of 1,5-anhydro-D -fructose and α-1,4-glucan lyase. Carbohydr. Res. 1997;305:73-82.
    • (1997) Carbohydr. Res. , vol.305 , pp. 73-82
    • Yu, S.1    Olsen, C.E.2    Marcussen, J.3
  • 20
    • 0028989882 scopus 로고
    • α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism
    • Yu S, Ahmad T, Kenne L, Peders̈en M. α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism. Biochim. Biophys. Acta. 1995;1244:1-9.
    • (1995) Biochim. Biophys. Acta. , vol.1244 , pp. 1-9
    • Yu, S.1    Ahmad, T.2    Kenne, L.3    Peders̈en, M.4
  • 21
    • 0015305643 scopus 로고
    • Mutarotase effect on colorimetric determination of blood glucose with β-D-glucose oxidase
    • Miwa I, Okuda J, Maeda K, Okuda G. Mutarotase effect on colorimetric determination of blood glucose with β-D-glucose oxidase. Clin. Chim. Acta. 1972;37:538-540.
    • (1972) Clin. Chim. Acta. , vol.37 , pp. 538-540
    • Miwa, I.1    Okuda, J.2    Maeda, K.3    Okuda, G.4
  • 22
    • 0030066741 scopus 로고    scopus 로고
    • NMR of all-carbon-13 sugars: An application in development of an analytical method for a novel natural sugar, 1,5-anhydrofructose
    • Kametani S, Mizuno H, Shiga Y, Akanuma H. NMR of all-carbon-13 sugars: An application in development of an analytical method for a novel natural sugar, 1,5-anhydrofructose. J. Biochem. 1996;119:180-185.
    • (1996) J. Biochem. , vol.119 , pp. 180-185
    • Kametani, S.1    Mizuno, H.2    Shiga, Y.3    Akanuma, H.4
  • 23
    • 33144471137 scopus 로고    scopus 로고
    • Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: Discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis
    • Kühn A, Yu S, Giffhorn F. Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: Discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis. Appl. Environ. Microbiol. 2006;72:1248-1257.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1248-1257
    • Kühn, A.1    Yu, S.2    Giffhorn, F.3
  • 26
    • 84857825776 scopus 로고    scopus 로고
    • A historical perspective for the catalytic reaction mechanism of glycosidase; so as to bring about breakthrough in confusing situation
    • Chiba S. A historical perspective for the catalytic reaction mechanism of glycosidase; so as to bring about breakthrough in confusing situation. Biosci. Biotechnol. Biochem. 2012;76:215-231.
    • (2012) Biosci. Biotechnol. Biochem. , vol.76 , pp. 215-231
    • Chiba, S.1


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