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Volumn 68, Issue 6, 2005, Pages 757-765

α-Glucosidase from a strain of deep-sea Geobacillus: A potential enzyme for the biosynthesis of complex carbohydrates

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; GENES; IONIC STRENGTH; SEDIMENTS;

EID: 27644570786     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-005-1977-3     Document Type: Article
Times cited : (47)

References (31)
  • 1
    • 0018287541 scopus 로고
    • Polyethylene glycol induced protoplast transformation of Bacillus subtilis
    • Chang S, Cohen SN (1979) Polyethylene glycol induced protoplast transformation of Bacillus subtilis. Mol Gen Genet 168:111-115
    • (1979) Mol Gen Genet , vol.168 , pp. 111-115
    • Chang, S.1    Cohen, S.N.2
  • 2
    • 0031201675 scopus 로고    scopus 로고
    • Molecular mechanism in α-glucosidase and glucoamylase
    • Chiba S (1997) Molecular mechanism in α-glucosidase and glucoamylase. Biosci Biotechnol Biochem 61:1233-1239
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1233-1239
    • Chiba, S.1
  • 3
    • 33746129272 scopus 로고    scopus 로고
    • Application of glycosylases in the synthesis of complex carbohydrates
    • Gilbert HJ, Davies GJ, Henrissat B, Svensson B (eds). The Royal Society of Chemistry, Cambridge
    • Crout DHC, Critchley P, Muller D, Scigelova M, Singh S, Vic G (1999) Application of glycosylases in the synthesis of complex carbohydrates. In: Gilbert HJ, Davies GJ, Henrissat B, Svensson B (eds) Recent advances in carbohydrate bioengineering. The Royal Society of Chemistry, Cambridge, pp 15-23
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 15-23
    • Crout, D.H.C.1    Critchley, P.2    Muller, D.3    Scigelova, M.4    Singh, S.5    Vic, G.6
  • 4
    • 0029150144 scopus 로고
    • Transglucosylation of a fungal alpha-glucosidase. The enzyme properties and correlation of isomaltooligosaccharide production
    • Duan KJ, Sheu DC, Lin CT (1995) Transglucosylation of a fungal alpha-glucosidase. The enzyme properties and correlation of isomaltooligosaccharide production. Ann N Y Acad Sci 750:325-328
    • (1995) Ann N Y Acad Sci , vol.750 , pp. 325-328
    • Duan, K.J.1    Sheu, D.C.2    Lin, C.T.3
  • 5
    • 0031888036 scopus 로고    scopus 로고
    • High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry
    • Ducret A, Van Oostveen I, Eng JK, Yates JR III, Aebersold R (1998) High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry. Protein Sci 7:706-719
    • (1998) Protein Sci , vol.7 , pp. 706-719
    • Ducret, A.1    Van Oostveen, I.2    Eng, J.K.3    Yates III, J.R.4    Aebersold, R.5
  • 6
    • 0032717219 scopus 로고    scopus 로고
    • Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complex mutants of a maltotetraose-forming amylase
    • Hasegawa K, Kubota M, Matsuura Y (1999) Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complex mutants of a maltotetraose-forming amylase. Protein Eng 12(10):819-824
    • (1999) Protein Eng , vol.12 , Issue.10 , pp. 819-824
    • Hasegawa, K.1    Kubota, M.2    Matsuura, Y.3
  • 7
    • 0022473663 scopus 로고
    • Primary structure of the maltase gene of the MAL6 locus of Saccharomyces carlsbergensis
    • Hong SH, Marmur J (1986) Primary structure of the maltase gene of the MAL6 locus of Saccharomyces carlsbergensis. J Gene 41:75-84
    • (1986) J Gene , vol.41 , pp. 75-84
    • Hong, S.H.1    Marmur, J.2
  • 8
    • 0020080769 scopus 로고
    • Modification of a glucoamylase from Aspergillus saitoi with 1-cyclohexyl-3-(2-morpholinyl-(4)-ethyl)carbodiimide
    • Tokyo
    • Inokuchi N, Iwama M, Takahashi T, Irie M (1982) Modification of a glucoamylase from Aspergillus saitoi with 1-cyclohexyl-3-(2-morpholinyl-(4)- ethyl)carbodiimide. J Biochem (Tokyo) 91:125-133
    • (1982) J Biochem , vol.91 , pp. 125-133
    • Inokuchi, N.1    Iwama, M.2    Takahashi, T.3    Irie, M.4
  • 9
    • 0026094827 scopus 로고
    • Synthesis of maltotriose by maltase purified from rabbit kidney
    • Itoh K, Hara T, Shibata N (1991) Synthesis of maltotriose by maltase purified from rabbit kidney. Biochem Int 24:969-979
    • (1991) Biochem Int , vol.24 , pp. 969-979
    • Itoh, K.1    Hara, T.2    Shibata, N.3
  • 10
    • 0034213129 scopus 로고    scopus 로고
    • The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism
    • Izard T, Ellis J (2000) The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism. EMBO J 19:2690-2700
    • (2000) EMBO J , vol.19 , pp. 2690-2700
    • Izard, T.1    Ellis, J.2
  • 11
    • 0024585544 scopus 로고
    • Substrate specificities of exo- and endo-type cellulases in the hydrolysis of β-1,3- and β-1,4-mixed D-glucans
    • Kanda T, Yatomi H, Makishima S, Amano Y, Nisizawa K (1989) Substrate specificities of exo- and endo-type cellulases in the hydrolysis of β-1,3- and β-1,4-mixed D-glucans. J Biochem 150:127-132
    • (1989) J Biochem , vol.150 , pp. 127-132
    • Kanda, T.1    Yatomi, H.2    Makishima, S.3    Amano, Y.4    Nisizawa, K.5
  • 13
    • 0042352394 scopus 로고    scopus 로고
    • Purification and characterization of a new type of alpha-glucosidase from Paecilomyces lilacinus that has transglucosylation activity to produce alpha-1,3- and alpha-1,2-linked oligosaccharides
    • Kobayashi I, Tokuda M, Hashimoto H, Konda T, Nakano H, Kitahata S (2003) Purification and characterization of a new type of alpha-glucosidase from Paecilomyces lilacinus that has transglucosylation activity to produce alpha-1,3- and alpha-1,2-linked oligosaccharides. Biosci Biotechnol Biochem 67:29-35
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 29-35
    • Kobayashi, I.1    Tokuda, M.2    Hashimoto, H.3    Konda, T.4    Nakano, H.5    Kitahata, S.6
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 17344386610 scopus 로고    scopus 로고
    • Towards regio-selective synthesis of oligosaccharides by use of α-glucosidases with different substrate specificity
    • Mala S, Dvorakova H, Hrabal R, Kralova B (1999) Towards regio-selective synthesis of oligosaccharides by use of α-glucosidases with different substrate specificity. Carbohydr Res 322: 209-218
    • (1999) Carbohydr Res , vol.322 , pp. 209-218
    • Mala, S.1    Dvorakova, H.2    Hrabal, R.3    Kralova, B.4
  • 17
    • 0007553835 scopus 로고
    • Substrate specificity of an α-glucosidase in sugar beet seed
    • Matsui H, Chiba S, Shimomura T (1978) Substrate specificity of an α-glucosidase in sugar beet seed. Agric Biol Chem 42:1855-1860
    • (1978) Agric Biol Chem , vol.42 , pp. 1855-1860
    • Matsui, H.1    Chiba, S.2    Shimomura, T.3
  • 18
    • 0028360856 scopus 로고
    • Purification and characterization of a Bacillus sp. SAM1606 thermostable alpha-glucosidase with transglycosylation activity
    • Nakao M, Nakayama T, Harada M, Kakudo A, Ikemoto H, Kobayashi S, Shibano Y (1994) Purification and characterization of a Bacillus sp. SAM1606 thermostable alpha-glucosidase with transglycosylation activity. Appl Microbiol Biotechnol 41:337-343
    • (1994) Appl Microbiol Biotechnol , vol.41 , pp. 337-343
    • Nakao, M.1    Nakayama, T.2    Harada, M.3    Kakudo, A.4    Ikemoto, H.5    Kobayashi, S.6    Shibano, Y.7
  • 19
    • 0035064602 scopus 로고    scopus 로고
    • Taxonomic study of aerobic thermophilic bacilli: Descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus
    • G. thermocatenulatus, G. thermoleovorans, G. kaustophilus, G. thermoglucosideasius and G. thermodenitrificans
    • Nazina TN, Tourova TP, Poltaraus AB, Novikova EV, Grigoryan AA, Ivanova AE, Lysenko AM, Petrunyaka VV, Osipov GA, Belyaev SS, Ivanov MV (2001) Taxonomic study of aerobic thermophilic bacilli: descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus, G. thermocatenulatus, G. thermoleovorans, G. kaustophilus, G. thermoglucosideasius and G. thermodenitrificans. Int J Syst Evol Microbiol 51:433-446
    • (2001) Int J Syst Evol Microbiol , vol.51 , pp. 433-446
    • Nazina, T.N.1    Tourova, T.P.2    Poltaraus, A.B.3    Novikova, E.V.4    Grigoryan, A.A.5    Ivanova, A.E.6    Lysenko, A.M.7    Petrunyaka, V.V.8    Osipov, G.A.9    Belyaev, S.S.10    Ivanov, M.V.11
  • 20
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68:850-858
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 22
    • 0038116509 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray study of α-glucosidase from Geobacillus sp. strain HTA-462, one of the deepest sea bacteria
    • Shirai T, Hung VS, Akita M, Hatada Y, Ito S, Horikoshi K (2003) Crystallization and preliminary X-ray study of α-glucosidase from Geobacillus sp. strain HTA-462, one of the deepest sea bacteria. Acta Crystallogr, D Biol Crystallogr 59:1278-1279
    • (2003) Acta Crystallogr, D Biol Crystallogr , vol.59 , pp. 1278-1279
    • Shirai, T.1    Hung, V.S.2    Akita, M.3    Hatada, Y.4    Ito, S.5    Horikoshi, K.6
  • 23
    • 27644546247 scopus 로고    scopus 로고
    • Evidence of intramolecular transglycosylation catalyzed by an α-glucosidase
    • Son M, Mori H, Okuyama M, Kimura A, Chiba S (2003) Evidence of intramolecular transglycosylation catalyzed by an α-glucosidase. J Appl Glycosci 50:41-43
    • (2003) J Appl Glycosci , vol.50 , pp. 41-43
    • Son, M.1    Mori, H.2    Okuyama, M.3    Kimura, A.4    Chiba, S.5
  • 24
    • 0029400980 scopus 로고
    • Application of upstream region of a Bacillus endoglucanase gene to high-level expression of foreign gene in Bacillus substilis
    • Sumitomo N, Ozaki K, Hitomi J, Kawaminami S, Kobayashi T, Kawai S, Ito S (1995) Application of upstream region of a Bacillus endoglucanase gene to high-level expression of foreign gene in Bacillus substilis. Biosci Biotechnol Biochem 59:2172-2175
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 2172-2175
    • Sumitomo, N.1    Ozaki, K.2    Hitomi, J.3    Kawaminami, S.4    Kobayashi, T.5    Kawai, S.6    Ito, S.7
  • 25
    • 0031001295 scopus 로고    scopus 로고
    • Bacillus thermoamyloliquefaciens KP1071 alpha-glucosidase II is a thermostable M(r) 540,000 homohexameric alpha-glucosidase with both exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities
    • Suzuki Y, Nobiki M, Matsuda M, Sawai T (1997) Bacillus thermoamyloliquefaciens KP1071 alpha-glucosidase II is a thermostable M(r) 540,000 homohexameric alpha-glucosidase with both exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Eur J Biochem 245:129-136
    • (1997) Eur J Biochem , vol.245 , pp. 129-136
    • Suzuki, Y.1    Nobiki, M.2    Matsuda, M.3    Sawai, T.4
  • 26
    • 0030745477 scopus 로고    scopus 로고
    • Microbial flora in the deepest sea mud of Mariana Trench
    • Takami H, Inoue A, Fuji F, Horikoshi K (1997) Microbial flora in the deepest sea mud of Mariana Trench. FEBS Microbiol Lett 152:279-285
    • (1997) FEBS Microbiol Lett , vol.152 , pp. 279-285
    • Takami, H.1    Inoue, A.2    Fuji, F.3    Horikoshi, K.4
  • 28
    • 0026439111 scopus 로고
    • Cloning and expression of a thermostable exo-α-1,4-glucosidase gene from Bacillus stearothermophilus ATCC12016 in Escherichia coli
    • Takii Y, Daimon K, Suzuki Y (1992) Cloning and expression of a thermostable exo-α-1,4-glucosidase gene from Bacillus stearothermophilus ATCC12016 in Escherichia coli. Appl Microbiol Biotechnol 38:243-247
    • (1992) Appl Microbiol Biotechnol , vol.38 , pp. 243-247
    • Takii, Y.1    Daimon, K.2    Suzuki, Y.3
  • 29
    • 0030019468 scopus 로고    scopus 로고
    • Bacillus stearothermophilus ATCC12016 a-glucosidase specific for α-1,4 bonds of maltosaccharides and α-glucans shows high amino acid sequence similarities to seven α-D-glucohydrolases with different substrate specificity
    • Takii Y, Takahashi K, Yamamoto K, Sogabe Y, Suzuki Y (1996) Bacillus stearothermophilus ATCC12016 a-glucosidase specific for α-1,4 bonds of maltosaccharides and α-glucans shows high amino acid sequence similarities to seven α-D-glucohydrolases with different substrate specificity. Appl Microbiol Biotechnol 44:629-634
    • (1996) Appl Microbiol Biotechnol , vol.44 , pp. 629-634
    • Takii, Y.1    Takahashi, K.2    Yamamoto, K.3    Sogabe, Y.4    Suzuki, Y.5
  • 31
    • 0035465317 scopus 로고    scopus 로고
    • Identification of catalytic and substrate-binding site residues in Bacillus cereus ATCC7064 oligo-1,6-glucosidase
    • Watanabe K, Miyake K, Suzuki Y (2001) Identification of catalytic and substrate-binding site residues in Bacillus cereus ATCC7064 oligo-1,6- glucosidase. Biosci Biotechnol Biochem 65:2058-2064
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 2058-2064
    • Watanabe, K.1    Miyake, K.2    Suzuki, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.