Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Penicillium amagasakiense

The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigation...

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Published inJournal of molecular biology Vol. 223; no. 4; pp. 1167 - 1169
Main Authors Hendle, Jörg, Hecht, Hans-Jürgen, Kalisz, Henryk M., Schmid, Rolf D., Schomburg, Dietmar
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 20.02.1992
Elsevier
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Abstract The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 Å resolution and belong to the orthorhombic space group P2 12 12 1, with refined lattice constants of a = 59.3 A ̊ , b = 136.3 A ̊ and c = 156.7 A ̊ . Assuming two monomers (≈ 135 kDa) per asymmetric unit the V m value is 2.3 Å 3/Da.
AbstractList The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 angstroms resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 angstroms, b = 136.3 angstroms and c = 156.7 angstroms. Assuming two monomers (approximately 135 kDa) per asymmetric unit the Vm value is 2.3 cubic angstroms/Da.
The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 A, b = 136.3 A and c = 156.7 A. Assuming two monomers (approximately 135 kDa) per asymmetric unit the Vm value is 2.3 A3/Da.
The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 A, b = 136.3 A and c = 156.7 A. Assuming two monomers (approximately 135 kDa) per asymmetric unit the Vm value is 2.3 A3/Da.The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 A, b = 136.3 A and c = 156.7 A. Assuming two monomers (approximately 135 kDa) per asymmetric unit the Vm value is 2.3 A3/Da.
The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and purification to isoelectric homogeneity were shown to be an important prerequisite step to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme were reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 Å resolution and belong to the orthorhombic space group P2 12 12 1, with refined lattice constants of a = 59.3 A ̊ , b = 136.3 A ̊ and c = 156.7 A ̊ . Assuming two monomers (≈ 135 kDa) per asymmetric unit the V m value is 2.3 Å 3/Da.
The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD.
Author Hecht, Hans-Jürgen
Kalisz, Henryk M.
Schmid, Rolf D.
Schomburg, Dietmar
Hendle, Jörg
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Cites_doi 10.1016/S0022-2836(05)80179-2
10.1016/0021-9673(90)85049-2
10.1016/0022-2836(68)90205-2
10.1271/bbb1961.39.1803
10.1016/0006-3002(60)91406-2
10.1021/bi00892a018
10.1016/0014-5793(89)81061-0
10.1016/S0021-9258(19)39664-4
10.1016/0005-2744(76)90221-7
10.1107/S0021889887086436
10.1016/S0021-9673(01)85007-X
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Issue 4
Keywords crystallization
Penicillium amagasakiense
glucose oxidase
Fungi
Glucose oxidase
Unit cell
Purification
Enzyme
Crystallization
Coenzyme enzyme complex
Fungi Imperfecti
X ray diffraction
Thallophyta
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References Kriechbaum, Heilmann, Wientjes, Hahn, Jany, Gassen, Sharif, Alaeddinoglu (BIB11) 1989; 255
Nakamatsu, Akamatsu, Miyajima, Shiio (BIB15) 1975; 39
(BIB19) 1987
Schmid, Karube (BIB18) 1988; vol. 6b
Röhr, Kubicek, Kominek (BIB17) 1983; vol. 3
Kalisz, Hendle, Schmid (BIB10) 1990; 521
Kusai, Sekuzu, Hagihara, Okunuki, Yamauchi, Nakai (BIB12) 1960; 40
Blundell, Johnson (BIB2) 1976
Abalikhina, Morozkin, Bogdanov, Kaverzneva (BIB1) 1971; 36
Matthews (BIB14) 1968; 33
Bright, Porter (BIB3) 1975; vol. 12
Howard, Gilliland, Finzel, Poulos (BIB8) 1987; 20
Eriksson, Kourteva, Yao, Liao, Kilar, Hjerten (BIB5) 1987; 397
Hayashi, Nakamura (BIB7) 1976; 438
Crueger, Creuger (BIB4) 1984; vol. 6a
Pazur, Kleppe (BIB16) 1964; 3
Kalisz, Hecht, Schomburg, Schmid (BIB9) 1990; 213
McPherson (BIB13) 1982
Frederick, Tung, Emerick, Masiarz, Chamberlain, Vasavada, Rosenberg, Chakraborty, Schopter, Massey (BIB6) 1990; 265
Frederick (10.1016/0022-2836(92)90267-N_BIB6) 1990; 265
(10.1016/0022-2836(92)90267-N_BIB19) 1987
McPherson (10.1016/0022-2836(92)90267-N_BIB13) 1982
Kalisz (10.1016/0022-2836(92)90267-N_BIB9) 1990; 213
Blundell (10.1016/0022-2836(92)90267-N_BIB2) 1976
Hayashi (10.1016/0022-2836(92)90267-N_BIB7) 1976; 438
Howard (10.1016/0022-2836(92)90267-N_BIB8) 1987; 20
Abalikhina (10.1016/0022-2836(92)90267-N_BIB1) 1971; 36
Kriechbaum (10.1016/0022-2836(92)90267-N_BIB11) 1989; 255
Röhr (10.1016/0022-2836(92)90267-N_BIB17) 1983; vol. 3
Bright (10.1016/0022-2836(92)90267-N_BIB3) 1975; vol. 12
Nakamatsu (10.1016/0022-2836(92)90267-N_BIB15) 1975; 39
Kusai (10.1016/0022-2836(92)90267-N_BIB12) 1960; 40
Crueger (10.1016/0022-2836(92)90267-N_BIB4) 1984; vol. 6a
Eriksson (10.1016/0022-2836(92)90267-N_BIB5) 1987; 397
Pazur (10.1016/0022-2836(92)90267-N_BIB16) 1964; 3
Matthews (10.1016/0022-2836(92)90267-N_BIB14) 1968; 33
Schmid (10.1016/0022-2836(92)90267-N_BIB18) 1988; vol. 6b
Kalisz (10.1016/0022-2836(92)90267-N_BIB10) 1990; 521
References_xml – year: 1987
  ident: BIB19
  publication-title: Biosensors-Fundamentals and Applications
– start-page: 82
  year: 1982
  end-page: 159
  ident: BIB13
  publication-title: Preparation and Analysis of Protein Crystal
– volume: vol. 3
  start-page: 455
  year: 1983
  end-page: 465
  ident: BIB17
  publication-title: Biotechnology
– volume: 265
  start-page: 3793
  year: 1990
  end-page: 3802
  ident: BIB6
  article-title: Glucose oxidase from
  publication-title: J. Biol. Chem
– volume: 397
  start-page: 239
  year: 1987
  end-page: 249
  ident: BIB5
  article-title: Application of high-performance chromatographic and electrophoretic methods to the purification and characterization of glucose oxidase and catalase from
  publication-title: J. Chromatogr
– volume: 39
  start-page: 1803
  year: 1975
  end-page: 1811
  ident: BIB15
  article-title: Microbial production of glucose oxidase
  publication-title: Agric. Biol. Chem
– volume: 36
  start-page: 191
  year: 1971
  end-page: 198
  ident: BIB1
  article-title: Composition and structure of glucose oxidase from
  publication-title: Biokhimiya
– volume: 20
  start-page: 383
  year: 1987
  end-page: 387
  ident: BIB8
  article-title: The use of imaging proportional counter in macromolecular crystallography
  publication-title: J. Appl. Crystallogr
– volume: 213
  start-page: 207
  year: 1990
  end-page: 209
  ident: BIB9
  article-title: Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from
  publication-title: J. Mol. Biol
– volume: 40
  start-page: 555
  year: 1960
  end-page: 557
  ident: BIB12
  article-title: Crystallization of glucose oxidase from
  publication-title: Biochim. Biophys. Acta
– volume: 255
  start-page: 63
  year: 1989
  end-page: 66
  ident: BIB11
  article-title: Cloning and DNA sequence analysis of the glucose oxidase gene from
  publication-title: FEBS Letters
– volume: vol. 12
  start-page: 421
  year: 1975
  end-page: 505
  ident: BIB3
  publication-title: The Enzymes
– start-page: 59
  year: 1976
  end-page: 82
  ident: BIB2
  publication-title: Protein Crystallography
– volume: vol. 6a
  start-page: 421
  year: 1984
  end-page: 457
  ident: BIB4
  publication-title: Biotechnology
– volume: 438
  start-page: 37
  year: 1976
  end-page: 48
  ident: BIB7
  article-title: Comparison of fungal glucose oxidases. Chemical, physicochemical and immunological studies
  publication-title: Biochim. Biophys. Acta
– volume: 521
  start-page: 245
  year: 1990
  end-page: 250
  ident: BIB10
  article-title: Purification of the glycoprotein glucose oxidase from
  publication-title: J. Chromatogr
– volume: 3
  start-page: 578
  year: 1964
  end-page: 583
  ident: BIB16
  article-title: The oxidation of glucose and related compounds by glucose oxidase from
  publication-title: Biochemistry
– volume: 33
  start-page: 491
  year: 1968
  end-page: 497
  ident: BIB14
  article-title: Solvent content of protein crystals
  publication-title: J. Mol. Biol
– volume: vol. 6b
  start-page: 317
  year: 1988
  end-page: 365
  ident: BIB18
  publication-title: Biotechnology
– volume: 213
  start-page: 207
  year: 1990
  ident: 10.1016/0022-2836(92)90267-N_BIB9
  article-title: Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Aspergillus niger
  publication-title: J. Mol. Biol
  doi: 10.1016/S0022-2836(05)80179-2
– volume: 521
  start-page: 245
  year: 1990
  ident: 10.1016/0022-2836(92)90267-N_BIB10
  article-title: Purification of the glycoprotein glucose oxidase from Penicillium amagasakiense by high-performance liquid chromatography
  publication-title: J. Chromatogr
  doi: 10.1016/0021-9673(90)85049-2
– volume: 33
  start-page: 491
  year: 1968
  ident: 10.1016/0022-2836(92)90267-N_BIB14
  article-title: Solvent content of protein crystals
  publication-title: J. Mol. Biol
  doi: 10.1016/0022-2836(68)90205-2
– volume: 39
  start-page: 1803
  year: 1975
  ident: 10.1016/0022-2836(92)90267-N_BIB15
  article-title: Microbial production of glucose oxidase
  publication-title: Agric. Biol. Chem
  doi: 10.1271/bbb1961.39.1803
– volume: 40
  start-page: 555
  year: 1960
  ident: 10.1016/0022-2836(92)90267-N_BIB12
  article-title: Crystallization of glucose oxidase from Penicillium amagasakiense
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0006-3002(60)91406-2
– volume: 3
  start-page: 578
  year: 1964
  ident: 10.1016/0022-2836(92)90267-N_BIB16
  article-title: The oxidation of glucose and related compounds by glucose oxidase from Aspergillus niger
  publication-title: Biochemistry
  doi: 10.1021/bi00892a018
– start-page: 82
  year: 1982
  ident: 10.1016/0022-2836(92)90267-N_BIB13
– volume: 255
  start-page: 63
  year: 1989
  ident: 10.1016/0022-2836(92)90267-N_BIB11
  article-title: Cloning and DNA sequence analysis of the glucose oxidase gene from Aspergillus niger NRRL-3
  publication-title: FEBS Letters
  doi: 10.1016/0014-5793(89)81061-0
– start-page: 59
  year: 1976
  ident: 10.1016/0022-2836(92)90267-N_BIB2
– volume: 265
  start-page: 3793
  year: 1990
  ident: 10.1016/0022-2836(92)90267-N_BIB6
  article-title: Glucose oxidase from Aspergillus niger. Cloning, gene sequence, secretion from Saccharomyces cerevisiae and kinetic analysis of a yeast-derived enzyme
  publication-title: J. Biol. Chem
  doi: 10.1016/S0021-9258(19)39664-4
– volume: vol. 3
  start-page: 455
  year: 1983
  ident: 10.1016/0022-2836(92)90267-N_BIB17
– volume: 438
  start-page: 37
  year: 1976
  ident: 10.1016/0022-2836(92)90267-N_BIB7
  article-title: Comparison of fungal glucose oxidases. Chemical, physicochemical and immunological studies
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0005-2744(76)90221-7
– volume: vol. 12
  start-page: 421
  year: 1975
  ident: 10.1016/0022-2836(92)90267-N_BIB3
– volume: 36
  start-page: 191
  year: 1971
  ident: 10.1016/0022-2836(92)90267-N_BIB1
  article-title: Composition and structure of glucose oxidase from Penicillium vitale
  publication-title: Biokhimiya
– volume: 20
  start-page: 383
  year: 1987
  ident: 10.1016/0022-2836(92)90267-N_BIB8
  article-title: The use of imaging proportional counter in macromolecular crystallography
  publication-title: J. Appl. Crystallogr
  doi: 10.1107/S0021889887086436
– year: 1987
  ident: 10.1016/0022-2836(92)90267-N_BIB19
– volume: 397
  start-page: 239
  year: 1987
  ident: 10.1016/0022-2836(92)90267-N_BIB5
  article-title: Application of high-performance chromatographic and electrophoretic methods to the purification and characterization of glucose oxidase and catalase from Penicillium chrysogenum
  publication-title: J. Chromatogr
  doi: 10.1016/S0021-9673(01)85007-X
– volume: vol. 6b
  start-page: 317
  year: 1988
  ident: 10.1016/0022-2836(92)90267-N_BIB18
– volume: vol. 6a
  start-page: 421
  year: 1984
  ident: 10.1016/0022-2836(92)90267-N_BIB4
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Snippet The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation...
The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated purified and crystallized as a complex with its coenzyme FAD. Deglycosylation and...
The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD. Deglycosylation...
The dimeric glucose oxidase from Penicillium amagasakiense was deglycosylated, purified and crystallized as a complex with its coenzyme FAD.
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SubjectTerms Biological and medical sciences
crystal structure
Crystalline structure
crystallization
Crystallography
crystals
dimensions
enzymology
FAD
Fundamental and applied biological sciences. Psychology
glucose oxidase
Glucose Oxidase - ultrastructure
interaction
Molecular biophysics
Penicillium
Penicillium - enzymology
Penicillium amagasakiense
Protein Conformation
purification
Structure in molecular biology
ultrastructure
X-ray crystallography
X-Ray Diffraction
Title Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Penicillium amagasakiense
URI https://dx.doi.org/10.1016/0022-2836(92)90267-N
https://www.ncbi.nlm.nih.gov/pubmed/1538394
https://www.proquest.com/docview/16214106
https://www.proquest.com/docview/49943708
https://www.proquest.com/docview/72815855
Volume 223
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