메뉴 건너뛰기




Volumn 6, Issue 5, 1996, Pages 527-536

Purification, biochemistry and molecular cloning of an insect glycosylasparaginase from Spodoptera frugiperda

Author keywords

Degradation; Glycoprotein; Glycosylasparaginase; Insect; Lysosomal hydrolase

Indexed keywords

N4 (BETA N ACETYLGLUCOSAMINYL)ASPARAGINASE;

EID: 0029837611     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/6.5.527     Document Type: Article
Times cited : (26)

References (23)
  • 1
    • 0024850749 scopus 로고
    • Lysosomal degradation of Asn-linked glycoproteins
    • Aronson, N.N ,Jr. and Koranda, M.J. (1989) Lysosomal degradation of Asn-linked glycoproteins. FASEB J., 3, 2615-2622.
    • (1989) FASEB J. , vol.3 , pp. 2615-2622
    • Aronson Jr., N.N.1    Koranda, M.J.2
  • 3
    • 0025063817 scopus 로고
    • Cloning and sequence analysis of a cDNA for human glycosylasparaginase: A single gene encodes the subunits of this lysosomal amidase
    • Fisher, K.J., Tollersrud, O.K. and Aronson, N.N., Jr. (1990) Cloning and sequence analysis of a cDNA for human glycosylasparaginase: a single gene encodes the subunits of this lysosomal amidase FEBS Lett., 269, 440-444.
    • (1990) FEBS Lett. , vol.269 , pp. 440-444
    • Fisher, K.J.1    Tollersrud, O.K.2    Aronson Jr., N.N.3
  • 4
    • 0025992759 scopus 로고
    • Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients
    • Fisher, K.J and Aronson, N.N., Jr. (1991) Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. J. Biol. Chem., 266, 12105-12113.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12105-12113
    • Fisher, K.J.1    Aronson Jr., N.N.2
  • 5
    • 0027166702 scopus 로고
    • Post-translational processing and Thr-206 are required for glycosylasparaginase activity
    • Fisher, K.J., Klein, M., Park, H., Vettese, M.B. and Aronson, N.N., Jr. (1993) Post-translational processing and Thr-206 are required for glycosylasparaginase activity. FEBS Lett., 323, 271-275.
    • (1993) FEBS Lett. , vol.323 , pp. 271-275
    • Fisher, K.J.1    Klein, M.2    Park, H.3    Vettese, M.B.4    Aronson Jr., N.N.5
  • 6
    • 0030051163 scopus 로고    scopus 로고
    • Activation of glycosylasparaginase: Formation of active N-terminal threonine by intramolecular autoproteolysis
    • Guan, C., Cui, T., Rao, V., Liao, W., Benner, J., Lin, C.-L. and Combs, D. (1996) Activation of glycosylasparaginase: formation of active N-terminal threonine by intramolecular autoproteolysis. J. Biol. Chem., 271, 1732-1737.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1732-1737
    • Guan, C.1    Cui, T.2    Rao, V.3    Liao, W.4    Benner, J.5    Lin, C.-L.6    Combs, D.7
  • 7
    • 0026089364 scopus 로고
    • Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease
    • Ikonen, E., Baumann, M. Grön, K., Syvanen, A.C., Enomaa, N., Halila, R., Aula, P. and Peltonen, L. (1991) Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease. EMBO J., 10, 51-58.
    • (1991) EMBO J. , vol.10 , pp. 51-58
    • Ikonen, E.1    Baumann, M.2    Grön, K.3    Syvanen, A.C.4    Enomaa, N.5    Halila, R.6    Aula, P.7    Peltonen, L.8
  • 8
    • 0027389271 scopus 로고
    • Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum
    • Ikonen, E., Julkunen, I., Tollersrud, O.K., Kakkinen, N. and Peltonen, L. (1993) Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum. EMBO J., 12, 295-302.
    • (1993) EMBO J. , vol.12 , pp. 295-302
    • Ikonen, E.1    Julkunen, I.2    Tollersrud, O.K.3    Kakkinen, N.4    Peltonen, L.5
  • 9
    • 0026095291 scopus 로고
    • Glycoasparaginase from human leukocytes: Inactivation and covalent modification with diazo-oxonorvaline
    • Kaartinen, V., Williams, J.C., Tomoch, J., Yates, J.R., III, Hood, L.E. and Mononen, I. (1991) Glycoasparaginase from human leukocytes: inactivation and covalent modification with diazo-oxonorvaline. J Biol. Chem., 266, 5860-5869.
    • (1991) J Biol. Chem. , vol.266 , pp. 5860-5869
    • Kaartinen, V.1    Williams, J.C.2    Tomoch, J.3    Yates III, J.R.4    Hood, L.E.5    Mononen, I.6
  • 10
    • 0028797941 scopus 로고
    • Localization of the disulfide bond involved in post-translational processing of glycosylasparaginase and disrupted by a mutation in the Finnish-type aspartylglucosaminuria
    • McCormack, A.L., Mononen, I., Kaartinen, V. and Yates, J.R., III (1995) Localization of the disulfide bond involved in post-translational processing of glycosylasparaginase and disrupted by a mutation in the Finnish-type aspartylglucosaminuria, J. Biol. Chem., 270, 3212-3215.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3212-3215
    • McCormack, A.L.1    Mononen, I.2    Kaartinen, V.3    Yates III, J.R.4
  • 12
    • 0027358558 scopus 로고
    • Aspartylglycosaminuria: Protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation
    • Mononen, I., Fisher, K.J., Kaartinen, V. and Aronson, N.N., Jr. (1993) Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation. FASEB J., 7, 1247-1256.
    • (1993) FASEB J. , vol.7 , pp. 1247-1256
    • Mononen, I.1    Fisher, K.J.2    Kaartinen, V.3    Aronson Jr., N.N.4
  • 13
    • 0028786346 scopus 로고
    • Three-dimensional structure of human lysosomal aspartylglucosaminidase
    • Oinonen, C., Tikkanen, R , Rouvinen, J. and Peltonen, L. (1995) Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nature Struc. Biol. 12, 1102-1108.
    • (1995) Nature Struc. Biol. , vol.12 , pp. 1102-1108
    • Oinonen, C.1    Tikkanen, R.2    Rouvinen, J.3    Peltonen, L.4
  • 14
    • 0029913160 scopus 로고    scopus 로고
    • Glycosylation and phosphorylation of lysosomal glycoasparaginase
    • Park, H. and Aronson, N.N., Jr. (1996) Glycosylation and phosphorylation of lysosomal glycoasparaginase Arch. Biochem. Biophys., 328, 73-77.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 73-77
    • Park, H.1    Aronson Jr., N.N.2
  • 15
    • 0028086586 scopus 로고
    • Dissection of the molecular consequences of a double mutation causing a human lysosomal disease
    • Riikonen, A., Ikonen, E., Sormunen, R., Lehto, V.-P., Peltonen, L. and Jalanko, A. (1994) Dissection of the molecular consequences of a double mutation causing a human lysosomal disease. DNA Cell Biol., 13, 257-264.
    • (1994) DNA Cell Biol. , vol.13 , pp. 257-264
    • Riikonen, A.1    Ikonen, E.2    Sormunen, R.3    Lehto, V.-P.4    Peltonen, L.5    Jalanko, A.6
  • 17
    • 0014481842 scopus 로고
    • The purification and properties of a β-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct
    • Tarentino, A.L. and Maley, F. (1969) The purification and properties of a β-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct. Arch. Biochem. Biophys., 130, 295-303
    • (1969) Arch. Biochem. Biophys. , vol.130 , pp. 295-303
    • Tarentino, A.L.1    Maley, F.2
  • 18
    • 0027451539 scopus 로고
    • The first demonstration of a procaryotic glycosylasparaginase
    • Tarentino, A.L. and Plummer, T.H. Jr. (1993) The first demonstration of a procaryotic glycosylasparaginase. Biochem. Biophys. Res. Comm., 197, 179-186
    • (1993) Biochem. Biophys. Res. Comm. , vol.197 , pp. 179-186
    • Tarentino, A.L.1    Plummer Jr., T.H.2
  • 19
    • 0028842195 scopus 로고
    • Molecular cloning and sequence analysis of Flavobacterium meningosepticum glycosylasparaginase: A single gene encodes the α and β subunits
    • Tarentino, A.L., Quinones, G., Hauer, C.R., Changchien, L.-M. and Plummer-T.H., Jr. (1994) Molecular cloning and sequence analysis of Flavobacterium meningosepticum glycosylasparaginase: a single gene encodes the α and β subunits. Arch. Biochem. Biophys., 316, 399-406.
    • (1994) Arch. Biochem. Biophys. , vol.316 , pp. 399-406
    • Tarentino, A.L.1    Quinones, G.2    Hauer, C.R.3    Changchien, L.-M.4    Plummer-TH, Jr.5
  • 20
    • 0028886713 scopus 로고
    • Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene
    • Tenhunen, K., Laan, M., Manninen, T., Palotie, A., Peltonen, L. and Jalanko, A. (1995) Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene. Genomics, 30, 244-250.
    • (1995) Genomics , vol.30 , pp. 244-250
    • Tenhunen, K.1    Laan, M.2    Manninen, T.3    Palotie, A.4    Peltonen, L.5    Jalanko, A.6
  • 21
    • 0024410435 scopus 로고
    • Purification and characterization of rat liver glycosylasparaginase
    • Tollersrud, O.K. and Aronson, N.N., Jr. (1989) Purification and characterization of rat liver glycosylasparaginase. Biochem. J., 260, 101-108.
    • (1989) Biochem. J. , vol.260 , pp. 101-108
    • Tollersrud, O.K.1    Aronson Jr., N.N.2
  • 22
    • 0026606655 scopus 로고
    • Comparison of liver glycosylasparaginases from six vertebrates
    • Tollersrud, O.K. and Aronson, N.N., Jr. (1992) Comparison of liver glycosylasparaginases from six vertebrates. Biochem. J., 282, 891-897.
    • (1992) Biochem. J. , vol.282 , pp. 891-897
    • Tollersrud, O.K.1    Aronson Jr., N.N.2
  • 23
    • 0028176078 scopus 로고
    • Human leucocyte glycosylasparaginase is an α/β-heterodimer of 19kDa α-subunit and 17 and 18 kDa β-subunit
    • Tollersrud, O.K., Heiskanen, T. and Peltonen, L. (1994) Human leucocyte glycosylasparaginase is an α/β-heterodimer of 19kDa α-subunit and 17 and 18 kDa β-subunit. Biochem. J., 300, 541-544.
    • (1994) Biochem. J. , vol.300 , pp. 541-544
    • Tollersrud, O.K.1    Heiskanen, T.2    Peltonen, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.