메뉴 건너뛰기




Volumn 70, Issue 11, 2006, Pages 2662-2668

In vivo expression of UDP-N-acetylglucosamine: α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I (GnT-1) in Aspergillus oryzae and effects on the sugar chain of α-amylase

Author keywords

amylase; Aspergillus oryzae; Fungi; Glycosylation; N acetylglucosaminyltransferase I

Indexed keywords

AMINES; BIOCONVERSION; FLUORESCENCE; FUNGI; GENES; LIQUID CHROMATOGRAPHY; SUGAR (SUCROSE);

EID: 33751418445     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60265     Document Type: Article
Times cited : (20)

References (20)
  • 1
    • 0037137488 scopus 로고    scopus 로고
    • UDP-N-acetylglucosamine:α-3-D-mannoside β-1,2-N- acetylglucosaminyltransferase I and UDPN-acetylglucosamine: α-6-D- mannoside β-1,2-N-acetylglucosaminyltransferase II in Caenorhabditis elegans
    • Chen, S., Tan, J., Reinhold, V. N., Spence, A. M., and Schachter, H., UDP-N-acetylglucosamine:α-3-D-mannoside β-1,2-N- acetylglucosaminyltransferase I and UDPN-acetylglucosamine: α-6-D- mannoside β-1,2-N-acetylglucosaminyltransferase II in Caenorhabditis elegans. Biochim. Biophys. Acta, 19, 271-279 (2002).
    • (2002) Biochim. Biophys. Acta , vol.19 , pp. 271-279
    • Chen, S.1    Tan, J.2    Reinhold, V.N.3    Spence, A.M.4    Schachter, H.5
  • 2
    • 0026750626 scopus 로고
    • Control of glycoprotein synthesis: Substrate specificity of rat liver UDP-GlcNAc: Man α3R β2-N-acetylglucosaminyltransferase I using synthetic substrate analogues
    • Moller, G., Reck, F., Paulsen, H., Kaur, K. J., Sarkar, M., Schachter, H., and Brockhausen, I., Control of glycoprotein synthesis: substrate specificity of rat liver UDP-GlcNAc: Man α3R β2-N- acetylglucosaminyltransferase I using synthetic substrate analogues. Glycoconj. J., 9, 180-190 (1992).
    • (1992) Glycoconj. J. , vol.9 , pp. 180-190
    • Moller, G.1    Reck, F.2    Paulsen, H.3    Kaur, K.J.4    Sarkar, M.5    Schachter, H.6    Brockhausen, I.7
  • 4
  • 7
    • 33344464428 scopus 로고    scopus 로고
    • Cloning and expression of 1,2-α-mannosidase gene (fmanIB) from filamentous fungus Aspergillus oryzae: In vivo visualization of the Fman-IBp-GFP fusion protein
    • Akao, T., Yamaguchi, M., Yahara, A., Yoshiuchi, K., Fujita, H., Yamada, O., Akita, O., Ohmachi, T., Asada, Y., and Yoshida, T., Cloning and expression of 1,2-α-mannosidase gene (fmanIB) from filamentous fungus Aspergillus oryzae: in vivo visualization of the Fman-IBp-GFP fusion protein. Biosci. Biotechnol. Biochem., 70, 471-479 (2006).
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 471-479
    • Akao, T.1    Yamaguchi, M.2    Yahara, A.3    Yoshiuchi, K.4    Fujita, H.5    Yamada, O.6    Akita, O.7    Ohmachi, T.8    Asada, Y.9    Yoshida, T.10
  • 8
    • 0029010002 scopus 로고
    • Insertion into Aspergillus nidulans of functional UDP-GlcNAc: α3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I, the enzyme catalysing the first committed step from oligomannose to hybrid and complex N-glycans
    • Kalsner, I., Hintz, W., Reid, L. S., and Schachter, H., Insertion into Aspergillus nidulans of functional UDP-GlcNAc: α3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I, the enzyme catalysing the first committed step from oligomannose to hybrid and complex N-glycans. Glycoconj. J., 12, 360-370 (1995).
    • (1995) Glycoconj. J. , vol.12 , pp. 360-370
    • Kalsner, I.1    Hintz, W.2    Reid, L.S.3    Schachter, H.4
  • 9
    • 0015137704 scopus 로고
    • The complete sequence of a glycopeptide obtained from Taka-amylase A
    • (Tokyo)
    • Yamaguchi, H., Ikenaka, T., and Matsushima, Y., The complete sequence of a glycopeptide obtained from Taka-amylase A. J. Biochem. (Tokyo), 70, 587-594 (1971).
    • (1971) J. Biochem. , vol.70 , pp. 587-594
    • Yamaguchi, H.1    Ikenaka, T.2    Matsushima, Y.3
  • 10
    • 0026688912 scopus 로고
    • Functional elements of the promoter region of the Aspergillus oryzae glaA gene encoding glucoamylase
    • Hata, Y., Kitamoto, K., Gomi, K., Kumagai, C., and Tamura, G., Functional elements of the promoter region of the Aspergillus oryzae glaA gene encoding glucoamylase. Curr. Genet., 22, 85-91 (1992).
    • (1992) Curr. Genet. , vol.22 , pp. 85-91
    • Hata, Y.1    Kitamoto, K.2    Gomi, K.3    Kumagai, C.4    Tamura, G.5
  • 11
    • 0035407325 scopus 로고    scopus 로고
    • Visualization of nuclei in Aspergillus oryzae with EGFP and analysis of the number of nuclei in each conidium by FACS
    • Maruyama, J., Nakajima, H., and Kitamoto, K., Visualization of nuclei in Aspergillus oryzae with EGFP and analysis of the number of nuclei in each conidium by FACS. Biosci. Biotechnol. Biochem., 65, 1504-1510 (2001).
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 1504-1510
    • Maruyama, J.1    Nakajima, H.2    Kitamoto, K.3
  • 12
    • 33751399930 scopus 로고
    • Chromatography of Taka-amylase A on diethylaminoethyl-cellulose column
    • (Tokyo)
    • Toda, H., and Akabori, S., Chromatography of Taka-amylase A on diethylaminoethyl-cellulose column. J. Biochem. (Tokyo), 53, 102-110 (1963).
    • (1963) J. Biochem. , vol.53 , pp. 102-110
    • Toda, H.1    Akabori, S.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 277, 680-685 (1970).
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0021308647 scopus 로고
    • Re-examination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins
    • Hase, S., Ibuki, T., and Ikenaka, T., Re-examination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins. J. Biochem., 95, 197-203 (1984).
    • (1984) J. Biochem. , vol.95 , pp. 197-203
    • Hase, S.1    Ibuki, T.2    Ikenaka, T.3
  • 16
    • 0031983578 scopus 로고    scopus 로고
    • Plant-adapted green fluorescent protein is a versatile vital reporter for gene expression, protein localization and mitosis in the filamentous fungus, Aspergillus nidulans
    • Fernandez-Abalos, J. M., Fox, H., Pitt, C., Wells, B., and Doonan, J. H., Plant-adapted green fluorescent protein is a versatile vital reporter for gene expression, protein localization and mitosis in the filamentous fungus, Aspergillus nidulans. Mol. Microbiol., 27, 121-130 (1998).
    • (1998) Mol. Microbiol. , vol.27 , pp. 121-130
    • Fernandez-Abalos, J.M.1    Fox, H.2    Pitt, C.3    Wells, B.4    Doonan, J.H.5
  • 17
    • 0037005893 scopus 로고    scopus 로고
    • Observation of EGFP-visualized nuclei and distribution of vacuoles in Aspergillus oryzae arpA null mutant
    • Maruyama, J., Nakajima, H., and Kitamoto, K., Observation of EGFP-visualized nuclei and distribution of vacuoles in Aspergillus oryzae arpA null mutant. FEMS Microbiol. Lett., 206, 57-61 (2002).
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 57-61
    • Maruyama, J.1    Nakajima, H.2    Kitamoto, K.3
  • 18
    • 0036196575 scopus 로고    scopus 로고
    • Dynein supports motility of endoplasmic reticulum in the fungus Ustilago maydis
    • Wedlich-Soldner, R., Schulz, I., Straube, A., and Steinberg, G., Dynein supports motility of endoplasmic reticulum in the fungus Ustilago maydis. Mol. Biol. Cell, 13, 965-977 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 965-977
    • Wedlich-Soldner, R.1    Schulz, I.2    Straube, A.3    Steinberg, G.4
  • 19
    • 0035983848 scopus 로고    scopus 로고
    • Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: Evidence from selective photobleaching
    • Brandizzi, F., Snapp, E. L., Roberts, A. G., Lippincott-Schwartz, J., and Hawes, C., Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching. Plant Cell, 14, 1293-1309 (2002).
    • (2002) Plant Cell , vol.14 , pp. 1293-1309
    • Brandizzi, F.1    Snapp, E.L.2    Roberts, A.G.3    Lippincott-Schwartz, J.4    Hawes, C.5
  • 20
    • 0023881383 scopus 로고
    • The effect of the protein matrix on glycan processing in glycoproteins: Kinetic analysis of three rat liver Golgi enzymes
    • Shao, M. C., and Wold, F., The effect of the protein matrix on glycan processing in glycoproteins: kinetic analysis of three rat liver Golgi enzymes. J. Biol. Chem., 263, 5771-5774 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 5771-5774
    • Shao, M.C.1    Wold, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.