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Volumn 240, Issue 3, 1996, Pages 692-698

Two subsites on the active center of pig kidney trehalase

Author keywords

Active center; Kinetic analysis; Multiple inhibition; Trehalase; Two subsites

Indexed keywords

1 DEOXYMANNONOJIRIMYCIN; 1 DEOXYNOJIRIMYCIN; ALPHA METHYL MANNOSIDE; ALPHA METHYLGLUCOSIDE; ENZYME INHIBITOR; FAGOMINE; METHYL MANNOSIDE; METHYLGLUCOSIDE; TREHALASE; VALIDOXYLAMINE A;

EID: 0029742701     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0692h.x     Document Type: Article
Times cited : (24)

References (30)
  • 1
    • 0023198415 scopus 로고
    • Effect of validamycins on glycohydrolases of Rhizoctonia solani
    • Asano, N., Yamaguchi, T., Kameda, Y. & Matsui, K. (1987) Effect of validamycins on glycohydrolases of Rhizoctonia solani, J. Antibiot. (Tokyo) 40, 526-532.
    • (1987) J. Antibiot. (Tokyo) , vol.40 , pp. 526-532
    • Asano, N.1    Yamaguchi, T.2    Kameda, Y.3    Matsui, K.4
  • 2
    • 0025297124 scopus 로고
    • Trehalase inhibitors, validoxylamine A and related compounds as insecticides
    • Asano, N., Takeuchi, M., Kameda, Y., Matsui, K. & Kono, Y. (1990) Trehalase inhibitors, validoxylamine A and related compounds as insecticides, J. Antibiot. (Tokyo) 43, 722-726.
    • (1990) J. Antibiot. (Tokyo) , vol.43 , pp. 722-726
    • Asano, N.1    Takeuchi, M.2    Kameda, Y.3    Matsui, K.4    Kono, Y.5
  • 3
    • 0028127346 scopus 로고
    • Nitrogen-in-the-ring pyranoses and furanoses: Structural basis of inhibition of mammalian glycosidases
    • Asano, N., Oseki, K., Kizu, H. & Matsui, K. (1994) Nitrogen-in-the-ring pyranoses and furanoses: Structural basis of inhibition of mammalian glycosidases. J. Med. Chem. 37, 3701-3706.
    • (1994) J. Med. Chem. , vol.37 , pp. 3701-3706
    • Asano, N.1    Oseki, K.2    Kizu, H.3    Matsui, K.4
  • 4
    • 0021095302 scopus 로고
    • Conformations in solution of α,α-trehalose, α-D-glucopyranosyl α-D-mannopyranoside, and their 1-thioglycosyl analogs, and a tentative correlation of their behaviour with respect to the enzyme trehalase
    • Bock, K., Defaye, J., Driguez, H. & Bar-Guilloux, E. (1983) Conformations in solution of α,α-trehalose, α-D-glucopyranosyl α-D-mannopyranoside, and their 1-thioglycosyl analogs, and a tentative correlation of their behaviour with respect to the enzyme trehalase, Eur. J. Biochem. 131, 595-600.
    • (1983) Eur. J. Biochem. , vol.131 , pp. 595-600
    • Bock, K.1    Defaye, J.2    Driguez, H.3    Bar-Guilloux, E.4
  • 5
    • 0019017880 scopus 로고
    • Stereochemistry of the hydrolysis of trehalose by the enzyme trehalase prepared from the fresh fly Sarcophaga barbata
    • Clifford, K. H. (1980) Stereochemistry of the hydrolysis of trehalose by the enzyme trehalase prepared from the fresh fly Sarcophaga barbata, Eur. J. Biochem. 106, 337-340.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 337-340
    • Clifford, K.H.1
  • 6
    • 78651114973 scopus 로고
    • Determination of maltase and isomaltase activities with a glucose-oxidase reagent
    • Dahlqvist, A. (1961) Determination of maltase and isomaltase activities with a glucose-oxidase reagent. Biochem. J. 80, 547-551.
    • (1961) Biochem. J. , vol.80 , pp. 547-551
    • Dahlqvist, A.1
  • 9
    • 0346956065 scopus 로고
    • Study of the specificity and mechanism of action of trehalase by using substrate analogs. Symmetrical and unsymmetrical 2-deoxy and 2-deuterated derivatives of α,α-trehalose
    • Defaye, J., Driguez, H., Henrissat, B. & Bar-Guilloux, E. (1980b) Study of the specificity and mechanism of action of trehalase by using substrate analogs. Symmetrical and unsymmetrical 2-deoxy and 2-deuterated derivatives of α,α-trehalose. Nouv. J. Chim. 4, 59-67.
    • (1980) Nouv. J. Chim. , vol.4 , pp. 59-67
    • Defaye, J.1    Driguez, H.2    Henrissat, B.3    Bar-Guilloux, E.4
  • 10
    • 0043109159 scopus 로고
    • Stereochemistry of hydrolysis of α,α-trehalose by trehalase, determined by using a labelled substrate
    • Defaye, J., Driguez, H., Henrissat, B. & Bar-Guilloux, E. (1983) Stereochemistry of hydrolysis of α,α-trehalose by trehalase, determined by using a labelled substrate. Carbohydr. Res. 124, 265-273.
    • (1983) Carbohydr. Res. , vol.124 , pp. 265-273
    • Defaye, J.1    Driguez, H.2    Henrissat, B.3    Bar-Guilloux, E.4
  • 11
    • 0016305880 scopus 로고
    • The metabolism of α,α-trehalose
    • Elbein, A. D. (1974) The metabolism of α,α-trehalose, Adv. Carbohydr. Chem. 30, 227-254.
    • (1974) Adv. Carbohydr. Chem. , vol.30 , pp. 227-254
    • Elbein, A.D.1
  • 12
    • 0014242319 scopus 로고
    • Rat intestinal microvillus membranes. Purification and biochemical characterization
    • Forstner, G. G., Sabesin, S. M. & Isselbacher, K. J. (1968) Rat intestinal microvillus membranes. Purification and biochemical characterization, Biochem. J. 106, 381-390.
    • (1968) Biochem. J. , vol.106 , pp. 381-390
    • Forstner, G.G.1    Sabesin, S.M.2    Isselbacher, K.J.3
  • 13
    • 0015906848 scopus 로고
    • Studies on the enzymology of purified preparations of brush border from rabbit kidmey
    • George, S. G. & Kenny, A. J. (1973) Studies on the enzymology of purified preparations of brush border from rabbit kidmey. Biochem. J. 134, 43-57.
    • (1973) Biochem. J. , vol.134 , pp. 43-57
    • George, S.G.1    Kenny, A.J.2
  • 14
    • 0020488855 scopus 로고
    • Trehalase: Stereocomplementary hydrolytic and glucosyl transfer reactions with α- and β-D-glucosyl fluoride
    • Hehre, E. J., Sawai, T., Brewer, C. F., Nakano, M. & Kanda, T. (1982) Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with α- and β-D-glucosyl fluoride, Biochemistry 21, 3090-3097.
    • (1982) Biochemistry , vol.21 , pp. 3090-3097
    • Hehre, E.J.1    Sawai, T.2    Brewer, C.F.3    Nakano, M.4    Kanda, T.5
  • 15
    • 0015262372 scopus 로고
    • Studies on validamycins, new antibiotics. VIII Isolation and characterization of validamycins C, D, E and F
    • Horii, S., Kameda, Y. & Kawahara, K. (1972) Studies on validamycins, new antibiotics. VIII Isolation and characterization of validamycins C, D, E and F, J. Antibiot. (Tokyo) 25, 48-53.
    • (1972) J. Antibiot. (Tokyo) , vol.25 , pp. 48-53
    • Horii, S.1    Kameda, Y.2    Kawahara, K.3
  • 16
    • 0022455206 scopus 로고
    • Synthesis and α-D-glucosidase inhibitory activity of N-substituted valiolamine derivatives as potential oral antidiabetic agents
    • Horri, S., Fukase, H., Matsuo, T., Kameda, Y., Asano, N. & Matsui, K. (1986) Synthesis and α-D-glucosidase inhibitory activity of N-substituted valiolamine derivatives as potential oral antidiabetic agents. J. Med. Chem. 29, 1038-1046.
    • (1986) J. Med. Chem. , vol.29 , pp. 1038-1046
    • Horri, S.1    Fukase, H.2    Matsuo, T.3    Kameda, Y.4    Asano, N.5    Matsui, K.6
  • 20
    • 0015822219 scopus 로고
    • 1-Aminoglycosides, a new class of specific inhibitors of glycosidases
    • Lai, H.-Y. & Axelrod, B. (1973) 1-Aminoglycosides, a new class of specific inhibitors of glycosidases, Biochem. Biophys. Res. Commun. 54, 463-468.
    • (1973) Biochem. Biophys. Res. Commun. , vol.54 , pp. 463-468
    • Lai, H.-Y.1    Axelrod, B.2
  • 21
    • 0019215333 scopus 로고
    • Isolation and characterization of a new trehalase inhibitor, S - GI
    • Murao, S. & Miyata, S. (1980) Isolation and characterization of a new trehalase inhibitor, S - GI, Agric. Biol. Chem. 44, 219-221.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 219-221
    • Murao, S.1    Miyata, S.2
  • 22
    • 0021769576 scopus 로고
    • Renal trehalase: Two subsites at the substrate-binding site
    • Nakano, M. & Sacktor, B. (1984) Renal trehalase: two subsites at the substrate-binding site, Biochim. Biophys. Acta 791, 45-49.
    • (1984) Biochim. Biophys. Acta , vol.791 , pp. 45-49
    • Nakano, M.1    Sacktor, B.2
  • 23
    • 0025208211 scopus 로고
    • Time-dependent inhibition of porcine kidney trehalase by aminosugars
    • Salleh, H. M. & Honek, J. F. (1990) Time-dependent inhibition of porcine kidney trehalase by aminosugars. FEBS Lett. 262, 359-362.
    • (1990) FEBS Lett. , vol.262 , pp. 359-362
    • Salleh, H.M.1    Honek, J.F.2
  • 24
    • 0015987113 scopus 로고
    • + activation, inhibition by tris(hydroxymethyl)aminomethane at the glucose subsite
    • + activation, inhibition by tris(hydroxymethyl)aminomethane at the glucose subsite, Eur. J. Biochem. 41, 149-162.
    • (1974) Eur. J. Biochem. , vol.41 , pp. 149-162
    • Semenza, G.1    Von Balthasar, A.-K.2
  • 25
    • 0002809819 scopus 로고
    • Glycosyl group transfer
    • Page, M. I. & Williams, A., eds The Royal Society of Chemistry, London
    • Sinnot, M. L. (1987) Glycosyl group transfer, in Enzyme mechanisms (Page, M. I. & Williams, A., eds) pp. 259-297. The Royal Society of Chemistry, London.
    • (1987) Enzyme Mechanisms , pp. 259-297
    • Sinnot, M.L.1
  • 26
    • 0025168621 scopus 로고
    • Inhibitory effect of validamine, valienamine and valiolamine on activities of carbohydrases in rat small intestinal brush border membranes
    • Takeuchi, M., Takai, N., Asano, N., Kameda, Y. & Matsui, K. (1990) Inhibitory effect of validamine, valienamine and valiolamine on activities of carbohydrases in rat small intestinal brush border membranes. Chem. Pharm. Bull. 38, 1970-1972.
    • (1990) Chem. Pharm. Bull. , vol.38 , pp. 1970-1972
    • Takeuchi, M.1    Takai, N.2    Asano, N.3    Kameda, Y.4    Matsui, K.5
  • 28
    • 0000957077 scopus 로고
    • Studies on liver alcohol dehydrogenase complexs. III. Multiple inhibition kinetics in the presence of two competitive inhibitors
    • Yonetani, T. & Theorell, H. (1964) Studies on liver alcohol dehydrogenase complexs. III. Multiple inhibition kinetics in the presence of two competitive inhibitors. Arch. Biochem. Biophys. 106, 243-251.
    • (1964) Arch. Biochem. Biophys. , vol.106 , pp. 243-251
    • Yonetani, T.1    Theorell, H.2
  • 29
    • 0001458216 scopus 로고
    • General principles of inhibition
    • Academic Press, London
    • Webb, J. L. (1963) General principles of inhibition, in Enzyme and metabolic inhibitory, vol. 1, pp. 488-490, Academic Press, London.
    • (1963) Enzyme and Metabolic Inhibitory , vol.1 , pp. 488-490
    • Webb, J.L.1
  • 30
    • 0024433743 scopus 로고
    • Design of potential anti-HIV agents 1. Mannosidase inhibitors
    • Winkler, D. A. & Holan, G. (1989) Design of potential anti-HIV agents 1. Mannosidase inhibitors. J. Med. Chem. 32, 2084-2089.
    • (1989) J. Med. Chem. , vol.32 , pp. 2084-2089
    • Winkler, D.A.1    Holan, G.2


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