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Volumn 7, Issue 3, 1998, Pages 774-781

Crystal structure of glycosylasparaginase from Flavobacterium meningosepticum

Author keywords

Aspartylglucosaminidase; Crystal structure; Glycoamidase

Indexed keywords

N4 (BETA N ACETYLGLUCOSAMINYL)ASPARAGINASE; RECOMBINANT ENZYME;

EID: 0031913198     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070327     Document Type: Article
Times cited : (30)

References (30)
  • 1
    • 10544253849 scopus 로고    scopus 로고
    • Lysosomal glycosylasparaginase: A member of a family of amidases that employ a processed N-terminal threonine, serine or cysteine as a combined base-nucleophile catalyst
    • Aronson NN Jr. 1996. Lysosomal glycosylasparaginase: A member of a family of amidases that employ a processed N-terminal threonine, serine or cysteine as a combined base-nucleophile catalyst. Glycobiology 6:669-675.
    • (1996) Glycobiology , vol.6 , pp. 669-675
    • Aronson Jr., N.N.1
  • 2
    • 0024850749 scopus 로고
    • Lysosomal degradation of Asn-linked glycoproteins
    • Aronson NN Jr, Kuranda MJ. 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    Kuranda, M.J.2
  • 4
    • 0023140814 scopus 로고
    • Crystallographic R-value refinement by molecular dynamics
    • Brünger AT, Kuriyan J, Karplus M. 1987. Crystallographic R-value refinement by molecular dynamics. Science 235:458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project No. 4
    • CCP4. 1994. Collaborative Computing Project No. 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50:760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 6
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representation of macromolecules
    • Evans SV. 1993. SETOR: Hardware-lighted three-dimensional solid model representation of macromolecules. J Mol Graphics 11:134-138.
    • (1993) J Mol Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 8
    • 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 CL, Comb 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    Comb, D.7
  • 10
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 13
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, McArthur MW, Moss DS, Thomton JM. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Crystallogr 26:282-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 282-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thomton, J.M.4
  • 14
    • 0029837611 scopus 로고    scopus 로고
    • Purification, biochemistry and molecular cloning of an insect glycosylasparaginase from Spodopterafrugiperda
    • Liu Y, Dunn GS, Aronson NN Jr. 1996. Purification, biochemistry and molecular cloning of an insect glycosylasparaginase from Spodopterafrugiperda. Glycobiology 6:527-536.
    • (1996) Glycobiology , vol.6 , pp. 527-536
    • Liu, Y.1    Dunn, G.S.2    Aronson Jr., N.N.3
  • 15
    • 0025327178 scopus 로고
    • Purification and characterization of an Escherichia coli shiga-like toxin II variant
    • MacLeod DL, Gyles DL. 1990. Purification and characterization of an Escherichia coli shiga-like toxin II variant. Infect Immun 58:1232-1239.
    • (1990) Infect Immun , vol.58 , pp. 1232-1239
    • MacLeod, D.L.1    Gyles, D.L.2
  • 16
    • 0345396650 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. 1968. Solvent content of protein crystals. J Mol Biol 245: 54-68.
    • (1968) J Mol Biol , vol.245 , pp. 54-68
    • Matthews, B.W.1
  • 18
    • 0027358558 scopus 로고
    • Aspartylglycosaminuria: Protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation
    • Mononen I, Fisher KJ, Kaartinen V, Aronson NN 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
  • 20
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr A 50:157-163.
    • (1994) Acta Crystallogr A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 21
    • 0028786346 scopus 로고
    • Three-dimensional structure of human lysosomal aspartylglucosaminidase
    • Oinonen C, Tikkanen R, Rouvinen J, Peltonen L. 1995. Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nature Struct Biol 2:1102-1108.
    • (1995) Nature Struct Biol , vol.2 , pp. 1102-1108
    • Oinonen, C.1    Tikkanen, R.2    Rouvinen, J.3    Peltonen, L.4
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 23
    • 0029835573 scopus 로고    scopus 로고
    • Primary folding of aspartylglucosaminidase. Significance of disulfide bridges and evidence of early multimerization
    • Riikonen A, Rouvinen J, Tikkanen R, Julkunen I, Peltonen L, Jalanko A. 1996. Primary folding of aspartylglucosaminidase. Significance of disulfide bridges and evidence of early multimerization. J Biol Chem 271:21340-21344.
    • (1996) J Biol Chem , vol.271 , pp. 21340-21344
    • Riikonen, A.1    Rouvinen, J.2    Tikkanen, R.3    Julkunen, I.4    Peltonen, L.5    Jalanko, A.6
  • 24
    • 0000082544 scopus 로고
    • CHAIN - A crystallographic modeling program
    • Sack JS. 1988. CHAIN - A crystallographic modeling program. J Mol Graphics 6:244-245.
    • (1988) J Mol Graphics , vol.6 , pp. 244-245
    • Sack, J.S.1
  • 26
    • 0027451539 scopus 로고
    • The first demonstration of a procaryotic glycosylasparaginase
    • Tarentino AL, Plummer TH Jr. 1993. The first demonstration of a procaryotic glycosylasparaginase. Biochem Biophys Res Commun 197:179-186.
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 179-186
    • Tarentino, A.L.1    Plummer Jr., T.H.2
  • 27
    • 0028261414 scopus 로고
    • Enzymatic deglycosylation of asparagine-linked glycans: Purification, properties and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum
    • Tarentino AL, Plummer TH Jr. 1994. Enzymatic deglycosylation of asparagine-linked glycans: Purification, properties and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum. Methods Enzymol 230:44-57.
    • (1994) Methods Enzymol , vol.230 , pp. 44-57
    • Tarentino, A.L.1    Plummer Jr., T.H.2
  • 28
    • 0028842195 scopus 로고
    • Molecular cloning and sequence analysis of Flavobacterium meningosepticum glycosylasparaginase: A single gene encodes the alpha and beta subunits
    • Tarentino AL, Quinones G, Hauer CR, Changchien LM, Plummer TH Jr. 1995. Molecular cloning and sequence analysis of Flavobacterium meningosepticum glycosylasparaginase: A single gene encodes the alpha and beta subunits. Arch Biochem Biophys 316:399-406.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 399-406
    • Tarentino, A.L.1    Quinones, G.2    Hauer, C.R.3    Changchien, L.M.4    Plummer Jr., T.H.5
  • 29
    • 0029936212 scopus 로고    scopus 로고
    • Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: Implications for catalytic mechanism and autocatalytic activation
    • Tikkanen R, Riikonen A, Oinonen C, Rouvinen R, Peltonen L. 1996. Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: Implications for catalytic mechanism and autocatalytic activation. EMBO J 15:2954-2960.
    • (1996) EMBO J , vol.15 , pp. 2954-2960
    • Tikkanen, R.1    Riikonen, A.2    Oinonen, C.3    Rouvinen, R.4    Peltonen, L.5
  • 30
    • 0026606655 scopus 로고
    • Comparison of liver glycosylasparaginase from six vertebrates
    • Tollersrud OK, Aronson NN Jr. 1992. Comparison of liver glycosylasparaginase 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.