메뉴 건너뛰기




Volumn 186, Issue 20, 2004, Pages 6928-6937

Effect of dimer dissociation on activity and thermostability of the α-glucuronidase from Geobacillus stearothermophilus: Dissecting the different oligomeric forms of family 67 glycoside hydrolases

Author keywords

[No Author keywords available]

Indexed keywords

4 O METHYL DEXTRO GLUCURONIC ACID; AGUA PROTEIN; ALPHA GLUCURONIDASE; BACTERIAL PROTEIN; BETA GLUCURONIDASE; DIMER; GLC67A PROTEIN; GLUCURONIC ACID; GLYCOSIDASE; HEMICELLULOSE; MONOMER; OLIGOMER; UNCLASSIFIED DRUG; XYLOSE;

EID: 4944265460     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.20.6928-6937.2004     Document Type: Article
Times cited : (44)

References (35)
  • 1
    • 0029942954 scopus 로고    scopus 로고
    • Disruption of the aldolase A tetramer into catalytically active monomers
    • Beernink, P. T., and D. R. Tolan. 1996. Disruption of the aldolase A tetramer into catalytically active monomers. Proc. Natl. Acad. Sci. USA 93:5374-5379.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5374-5379
    • Beernink, P.T.1    Tolan, D.R.2
  • 2
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett, M. J., M. P. Schlunegger, and D. Eisenberg. 1995. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4:2455-2468.
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 3
    • 0034193803 scopus 로고    scopus 로고
    • Inverting character of alpha-glucuronidase A from Aspergillus tubingensis
    • Biely, P., R. P. de Vries, M. Vrsanska, and J. Visser. 2000. Inverting character of alpha-glucuronidase A from Aspergillus tubingensis. Biochim. Biophys. Acta 1474:360-364.
    • (2000) Biochim. Biophys. Acta , vol.1474 , pp. 360-364
    • Biely, P.1    De Vries, R.P.2    Vrsanska, M.3    Visser, J.4
  • 4
    • 0029064373 scopus 로고
    • An interface point-mutation variant of triosephosphate isomerase is compactly folded and monomeric at low protein concentrations
    • Borchert, T. V., J. P. Zeelen, W. Schliebs, M. Callens, W. Minke, R. Jaenicke, and R. K. Wierenga. 1995. An interface point-mutation variant of triosephosphate isomerase is compactly folded and monomeric at low protein concentrations. FEBS Lett. 367:315-318.
    • (1995) FEBS Lett. , vol.367 , pp. 315-318
    • Borchert, T.V.1    Zeelen, J.P.2    Schliebs, W.3    Callens, M.4    Minke, W.5    Jaenicke, R.6    Wierenga, R.K.7
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-252.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-252
    • Bradford, M.1
  • 8
    • 0346306092 scopus 로고    scopus 로고
    • Why are there so many carbohydrate-active enzyme-related genes in plants?
    • Coutinho, P. M., M. Stam, E. Blanc, and B. Henrissat. 2003. Why are there so many carbohydrate-active enzyme-related genes in plants? Trends Plant Sci. 8:563-565.
    • (2003) Trends Plant Sci. , vol.8 , pp. 563-565
    • Coutinho, P.M.1    Stam, M.2    Blanc, E.3    Henrissat, B.4
  • 9
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies, G. J., K. S. Wilson, and B. Henrissat. 1997. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321:557-559.
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 11
    • 0031909985 scopus 로고    scopus 로고
    • aguA, the gene encoding an extracellular α-glucuronidase from Aspergillus tubingensis, is specifically induced on xylose and not on glucuronic acid
    • de Vries, R. P., C. H. Poulsen, S. Madrid, and J. Visser. 1998. aguA, the gene encoding an extracellular α-glucuronidase from Aspergillus tubingensis, is specifically induced on xylose and not on glucuronic acid. J. Bacteriol. 180:243-249.
    • (1998) J. Bacteriol. , vol.180 , pp. 243-249
    • De Vries, R.P.1    Poulsen, C.H.2    Madrid, S.3    Visser, J.4
  • 12
    • 9144241621 scopus 로고    scopus 로고
    • Crystal structures of Geobacillus stearothermophilus α- glucuronidase complexed with its substrate and products: Mechanistic implications
    • Golan, G., D. Shallom, A. Teplitsky, G. Zaide, S. Shulami, T. Baasov, V. Stojanoff, A. Thompson, Y. Shoham, and G. Shoham. 2004. Crystal structures of Geobacillus stearothermophilus α-glucuronidase complexed with its substrate and products: mechanistic implications. J. Biol. Chem. 279:3014-3024.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3014-3024
    • Golan, G.1    Shallom, D.2    Teplitsky, A.3    Zaide, G.4    Shulami, S.5    Baasov, T.6    Stojanoff, V.7    Thompson, A.8    Shoham, Y.9    Shoham, G.10
  • 13
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat, B., and G. Davies. 1997. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7:637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 14
    • 0034506072 scopus 로고    scopus 로고
    • Glycoside hydrolases and glycosyl-transferases. Families, modules, and implications for genomics
    • Henrissat, B., and G. J. Davies. 2000. Glycoside hydrolases and glycosyl-transferases. Families, modules, and implications for genomics. Plant Physiol. 124:1515-1519.
    • (2000) Plant Physiol. , vol.124 , pp. 1515-1519
    • Henrissat, B.1    Davies, G.J.2
  • 15
    • 0033042555 scopus 로고    scopus 로고
    • Stability and folding of domain proteins
    • Jaenicke, R. 1999. Stability and folding of domain proteins. Prog. Biophys. Mol. Biol. 71:155-241.
    • (1999) Prog. Biophys. Mol. Biol. , vol.71 , pp. 155-241
    • Jaenicke, R.1
  • 16
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones, S., and J. M. Thornton. 1996. Principles of protein-protein interactions. Proc. Natl. Acad. Sci. USA 93:13-20.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 17
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • Jones, S., and J. M. Thornton. 1995. Protein-protein interactions: a review of protein dimer structures. Prog. Biophys. Mol. Biol. 63:31-65.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 18
    • 0024763430 scopus 로고
    • Purification and characterization of an alpha-D-glucuronidase from a thermophilic fungus, Thermoascus aurantiacus
    • Khandke, K. M., P. J. Vithayathil, and S. K. Murthy. 1989. Purification and characterization of an alpha-D-glucuronidase from a thermophilic fungus, Thermoascus aurantiacus. Arch. Biochem. Biophys. 274:511-517.
    • (1989) Arch. Biochem. Biophys. , vol.274 , pp. 511-517
    • Khandke, K.M.1    Vithayathil, P.J.2    Murthy, S.K.3
  • 20
    • 0000854587 scopus 로고
    • A copper reagent for the determination of hexuronic acids and certain ketohexoses
    • Milner, Y., and G. Avigad. 1967. A copper reagent for the determination of hexuronic acids and certain ketohexoses. Carbohyd. Res. 4:359-361.
    • (1967) Carbohyd. Res. , vol.4 , pp. 359-361
    • Milner, Y.1    Avigad, G.2
  • 21
    • 0036716744 scopus 로고    scopus 로고
    • The membrane-bound α-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan
    • Nagy, T., K. Emami, C. M. Fontes, L. M. Ferreira, D. R. Humphry, and H. J. Gilbert. 2002. The membrane-bound α-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan. J. Bacteriol. 184:4925-4929.
    • (2002) J. Bacteriol. , vol.184 , pp. 4925-4929
    • Nagy, T.1    Emami, K.2    Fontes, C.M.3    Ferreira, L.M.4    Humphry, D.R.5    Gilbert, H.J.6
  • 22
    • 0037490140 scopus 로고    scopus 로고
    • The alpha-glucuronidase, GIcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants
    • Nagy, T., D. Nurizzo, G. J. Davies, P. Biely, J. H. Lakey, D. N. Bolam, and H. J. Gilbert. 2003. The alpha-glucuronidase, GIcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants. J. Biol. Chem. 278:20286-20292.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20286-20292
    • Nagy, T.1    Nurizzo, D.2    Davies, G.J.3    Biely, P.4    Lakey, J.H.5    Bolam, D.N.6    Gilbert, H.J.7
  • 23
    • 0036223466 scopus 로고    scopus 로고
    • The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GIcA67A
    • Nurizzo, D., T. Nagy, H. J. Gilbert, and G. J. Davies. 2002. The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GIcA67A. Structure (Cambridge) 10:547-556.
    • (2002) Structure (Cambridge) , vol.10 , pp. 547-556
    • Nurizzo, D.1    Nagy, T.2    Gilbert, H.J.3    Davies, G.J.4
  • 24
    • 0036839243 scopus 로고    scopus 로고
    • The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers
    • Ottosen, M. B., O. Bjornberg, S. Norager, S. Larsen, B. A. Palfey, and K. F. Jensen. 2002. The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers. Protein Sci. 11:2575-2583.
    • (2002) Protein Sci. , vol.11 , pp. 2575-2583
    • Ottosen, M.B.1    Bjornberg, O.2    Norager, S.3    Larsen, S.4    Palfey, B.A.5    Jensen, K.F.6
  • 25
    • 0030203863 scopus 로고    scopus 로고
    • Tree View: An application to display phylogenetic trees on personal computers
    • Page, R. D. 1996. Tree View: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12:357-358.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 26
    • 0037008089 scopus 로고    scopus 로고
    • Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation
    • Rodriguez-Zavala, J. S., and H. Weiner. 2002. Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation. Biochemistry 41:8229-8237.
    • (2002) Biochemistry , vol.41 , pp. 8229-8237
    • Rodriguez-Zavala, J.S.1    Weiner, H.2
  • 27
    • 0030857332 scopus 로고    scopus 로고
    • A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability
    • Schliebs, W., N. Thanki, R. Jaenicke, and R. K. Wierenga. 1997. A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability. Biochemistry 36:9655-9662.
    • (1997) Biochemistry , vol.36 , pp. 9655-9662
    • Schliebs, W.1    Thanki, N.2    Jaenicke, R.3    Wierenga, R.K.4
  • 28
    • 0032980767 scopus 로고    scopus 로고
    • The glucuronic acid utilization gene cluster from Bacillus stearothermophilus T-6
    • Shulami, S., O. Gat, A. L. Sonenshein, and Y. Shoham. 1999. The glucuronic acid utilization gene cluster from Bacillus stearothermophilus T-6. J. Bacteriol. 181:3695-3704.
    • (1999) J. Bacteriol. , vol.181 , pp. 3695-3704
    • Shulami, S.1    Gat, O.2    Sonenshein, A.L.3    Shoham, Y.4
  • 29
    • 0033997724 scopus 로고    scopus 로고
    • Protein structure alignment using a genetic algorithm
    • Szustakowski, J. D., and Z. Weng. 2000. Protein structure alignment using a genetic algorithm. Proteins 38:428-440.
    • (2000) Proteins , vol.38 , pp. 428-440
    • Szustakowski, J.D.1    Weng, Z.2
  • 30
    • 0033119383 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of alpha-D-glucuronidase from Bacillus stearothermophilus T-6
    • Teplitsky, A., S. Shulami, S. Moryles, G. Zaide, Y. Shoham, and G. Shoham. 1999. Crystallization and preliminary X-ray analysis of alpha-D-glucuronidase from Bacillus stearothermophilus T-6. Acta Crystallogr. Sect. D 55:869-872.
    • (1999) Acta Crystallogr. Sect. D , vol.55 , pp. 869-872
    • Teplitsky, A.1    Shulami, S.2    Moryles, S.3    Zaide, G.4    Shoham, Y.5    Shoham, G.6
  • 31
    • 0036240788 scopus 로고    scopus 로고
    • Functional maps of the junctions between interglobular contacts and active sites in glycolytic enzymes: A comparative analysis of the biochemical and structural data
    • Torshin, I. Y. 2002. Functional maps of the junctions between interglobular contacts and active sites in glycolytic enzymes: a comparative analysis of the biochemical and structural data. Med. Sci. Monit. 8:123-135.
    • (2002) Med. Sci. Monit. , vol.8 , pp. 123-135
    • Torshin, I.Y.1
  • 32
    • 0028230082 scopus 로고
    • Dissociation of enzyme oligomers: A mechanism for allosteric regulation
    • Traut, T. W. 1994. Dissociation of enzyme oligomers: a mechanism for allosteric regulation. Crit. Rev. Biochem. Mol. Biol. 29:125-163.
    • (1994) Crit. Rev. Biochem. Mol. Biol. , vol.29 , pp. 125-163
    • Traut, T.W.1
  • 33
    • 0001480778 scopus 로고
    • Purification and characterization of intracellular α-glucuronidase from Aspergillus niger 5-16
    • Uchida, H., T. Nanri, Y. Kawabata, I. Kusakabe, and K. Murakami. 1992. Purification and characterization of intracellular α-glucuronidase from Aspergillus niger 5-16. Biosci. Biotech. Biochem. 56:1608-1615.
    • (1992) Biosci. Biotech. Biochem. , vol.56 , pp. 1608-1615
    • Uchida, H.1    Nanri, T.2    Kawabata, Y.3    Kusakabe, I.4    Murakami, K.5
  • 35
    • 0034833426 scopus 로고    scopus 로고
    • Biochemical characterization and identification of catalytic residues in alpha-glucuronidase from Bacillus stearothermophilus T-6
    • Zaide, G., D. Shallom, S. Shulami, G. Zolotnitsky, G. Golan, T. Baasov, G. Shoham, and Y. Shoham. 2001. Biochemical characterization and identification of catalytic residues in alpha-glucuronidase from Bacillus stearothermophilus T-6. Eur. J. Biochem. 268:3006-3016.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3006-3016
    • Zaide, G.1    Shallom, D.2    Shulami, S.3    Zolotnitsky, G.4    Golan, G.5    Baasov, T.6    Shoham, G.7    Shoham, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.