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Volumn 7, Issue 3, 1999, Pages 265-276

A 30 Å long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase

Author keywords

Enzyme catalysis; Flavoenzymes; Monoamine oxidase; Polyamine oxidase; X ray crystallography

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; POLYAMINE OXIDASE; SPERMIDINE; SPERMINE; AMINE OXIDASE (FLAVIN CONTAINING); DRUG DERIVATIVE; ENZYME INHIBITOR; N,N' BIS(2,3 BUTADIENYL)PUTRESCINE; OXIDOREDUCTASE; POLYAMINE; PUTRESCINE; VEGETABLE PROTEIN;

EID: 34548519907     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80037-9     Document Type: Article
Times cited : (165)

References (44)
  • 1
    • 0021155448 scopus 로고
    • Polyamines
    • Tabor, C.W. & Tabor, H. (1984). Polyamines. Annu. Rev. Biochem. 53, 749-790.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 749-790
    • Tabor, H.1
  • 2
    • 0028956729 scopus 로고
    • Polyamines as targets for therapeutic intervention
    • Marton, L.J. & Pegg, A.E. (1995). Polyamines as targets for therapeutic intervention. Annu. Rev. Pharmacol. Toxicol. 35, 55-91.
    • (1995) Annu. Rev. Pharmacol. Toxicol. , vol.35 , pp. 55-91
    • Marton, L.J.1    Pegg, A.E.2
  • 3
    • 0030861055 scopus 로고    scopus 로고
    • Binding of polyamines to an autonomous domain of the regulatory subunit of protein kinase CK2 induces a conformational change in the holoenzyme
    • Leroy, D., Heriché, J.K., Filhol, O., Chambaz, E.M. & Cochet, C. (1997). Binding of polyamines to an autonomous domain of the regulatory subunit of protein kinase CK2 induces a conformational change in the holoenzyme. J. Biol. Chem. 272, 20820-20827.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20820-20827
    • Leroy, D.1    Heriché, J.K.2    Filhol, O.3    Chambaz, E.M.4    Cochet, C.5
  • 4
    • 0026356182 scopus 로고
    • Aggregation of IGF-I receptors or insulin receptors and activation of their kinase activity are simultaneously caused by the presence of polycations or K-ras basic peptides
    • Xu, Q.Y., Li, S.L., LeBon, T.R. & Fujita-Yamaguchi, Y. (1991). Aggregation of IGF-I receptors or insulin receptors and activation of their kinase activity are simultaneously caused by the presence of polycations or K-ras basic peptides. Biochemistry 30, 11811-11819.
    • (1991) Biochemistry , vol.30 , pp. 11811-11819
    • Xu, Q.Y.1    Li, S.L.2    LeBon, T.R.3    Fujita-Yamaguchi, Y.4
  • 5
    • 0031811591 scopus 로고    scopus 로고
    • Polyamines and cerebral ischemia
    • Johnson, T.D. (1998). Polyamines and cerebral ischemia. Prog. Drug Res. 50, 193-258.
    • (1998) Prog. Drug Res. , vol.50 , pp. 193-258
    • Johnson, T.D.1
  • 6
    • 0032503057 scopus 로고    scopus 로고
    • Maize polyamine oxidase: Primary structure from protein and cDNA sequencing
    • Tavladoraki, P., & Angelini, R., Et Al. (1998). Maize polyamine oxidase: Primary structure from protein and cDNA sequencing. FEBS Letters 426, 62-66.
    • (1998) FEBS Letters , vol.426 , pp. 62-66
    • Tavladoraki, P.1    Angelini, R.2
  • 8
    • 0029610668 scopus 로고
    • Polyamine oxidase, properties and functions
    • Seiler, N. (1995). Polyamine oxidase, properties and functions. Prog. Brain Res. 106, 333-344.
    • (1995) Prog. Brain Res. , vol.106 , pp. 333-344
    • Seiler, N.1
  • 9
    • 0029157157 scopus 로고
    • Effect of polyamine analogues and inhibition of polyamine oxidase on spermidine/spermine N1- Acetyltransferase activity and cell proliferation
    • Pegg, A.E. & Hu, R.H. (1995). Effect of polyamine analogues and inhibition of polyamine oxidase on spermidine/spermine N1- Acetyltransferase activity and cell proliferation. Cancer Lett. 95, 247-252.
    • (1995) Cancer Lett. , vol.95 , pp. 247-252
    • Pegg, A.E.1    Hu, R.H.2
  • 10
    • 0030684153 scopus 로고    scopus 로고
    • Rapid induction of apoptosis by deregulated uptake of polyamine analogues
    • Hu, R.H. & Pegg, A.e. (1997). Rapid induction of apoptosis by deregulated uptake of polyamine analogues. Biochem. J. 328, 307-316.
    • (1997) Biochem. J. , vol.328 , pp. 307-316
    • Hu, R.H.P.1
  • 11
    • 0001547001 scopus 로고    scopus 로고
    • The role of polyamine catabolism in polyamine analogue-induced programmed cell death
    • Ha, H.C., Woster, P.M., Yager, J.D. & Casero, R.A. Jr. (1997). The role of polyamine catabolism in polyamine analogue-induced programmed cell death. Proc. Natl Acad. Sci. USA 94, 11557-11562.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11557-11562
    • Ha, H.C.1    Woster, P.M.2    Yager, J.D.3    Casero R.A., Jr.4
  • 12
    • 0031571090 scopus 로고    scopus 로고
    • Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: The shape of the active-site cavity controls substrate specificity
    • Mattevi, A., Fraaije, M.W., Mozzarelli, A., Olivi, L., Coda, A. & van Berkel, W.J.H. (1997). Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: The shape of the active-site cavity controls substrate specificity. Structure 5, 907-920.
    • (1997) Structure , vol.5 , pp. 907-920
    • Mattevi, A.1    Fraaije, M.W.2    Mozzarelli, A.3    Olivi, L.4    Coda, A.5    Van Berkel, W.J.H.6
  • 13
    • 0031470918 scopus 로고    scopus 로고
    • Structure of D-amino acid oxidase: New insights from an old enzyme
    • Mattevi, A., Vanoni, M.A. & Curti, B. (1997). Structure of D-amino acid oxidase: New insights from an old enzyme. Curr. Opin. Struct. Biol. 7, 804-810.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 804-810
    • Mattevi, A.1    Vanoni, M.A.2    Curti, B.3
  • 14
    • 0021095474 scopus 로고
    • Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD-as well as NADPH-binding domains of glutathione reductase
    • Wierenga, R.K., Drenth, J. & Schulz, G.E. (1983). Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD-as well as NADPH-binding domains of glutathione reductase. J. Mol. Biol. 167, 725-739.
    • (1983) J. Mol. Biol. , vol.167 , pp. 725-739
    • Wierenga, R.K.1    Drenth, J.2    Schulz, G.E.3
  • 16
    • 0024974962 scopus 로고
    • Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 å resolution
    • Schreuder, H.A., & Drenth, J., Et Al. (1989). Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 å resolution. J. Mol. Biol. 208, 679-696.
    • (1989) J. Mol. Biol. , vol.208 , pp. 679-696
    • Schreuder, H.A.1    Drenth, J.2
  • 17
    • 0025793579 scopus 로고
    • Crystal structure of cholesterol oxidase from brevibacterium sterolicum refined at 1.8 å resolution
    • Vrielink, A., Lloyd, L.F. & Blow, D.M. (1991). Crystal structure of cholesterol oxidase from brevibacterium sterolicum refined at 1.8 å resolution. J. Mol. Biol. 219, 533-554.
    • (1991) J. Mol. Biol. , vol.219 , pp. 533-554
    • Vrielink, A.1    Lloyd, L.F.2    Blow, D.M.3
  • 18
    • 0027397187 scopus 로고
    • Crystal structure of glucose oxidase from aspergillus niger refined at 2.3 å resolution
    • Hecht, H.J., Kalisz, H.M., Hendle, J., Schmid, R.D. & Schomburg, D. (1993). Crystal structure of glucose oxidase from aspergillus niger refined at 2.3 å resolution. J. Mol. Biol. 229, 153-172.
    • (1993) J. Mol. Biol. , vol.229 , pp. 153-172
    • Hecht, H.J.1    Kalisz, H.M.2    Hendle, J.3    Schmid, R.D.4    Schomburg, D.5
  • 20
    • 0032498830 scopus 로고    scopus 로고
    • The PHBH fold: Not only flavoenzymes
    • Mattevi, A. (1998). The PHBH fold: Not only flavoenzymes. Biophys. Chem. 70, 217-222.
    • (1998) Biophys. Chem. , vol.70 , pp. 217-222
    • Mattevi, A.1
  • 21
    • 0002113403 scopus 로고
    • Properties of the polyamine oxidase from the cell wall of maize seedlings
    • Federico, R., Alisi, C. & Forlani, F. (1989). Properties of the polyamine oxidase from the cell wall of maize seedlings. Phytochemistry 28, 45-46.
    • (1989) Phytochemistry , vol.28 , pp. 45-46
    • Federico, R.1    Alisi, C.2    Forlani, F.3
  • 23
    • 0030043489 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D.A. (1996). Cation-pi interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp. Science 271, 163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 24
    • 0028978764 scopus 로고
    • The occurrence of C-H - O hydrogen bonds in proteins
    • Derewenda, Z.S., Lee, L. & Derewenda, U. (1995). The occurrence of C-H - O hydrogen bonds in proteins. J. Mol. Biol. 252, 248-262.
    • (1995) J. Mol. Biol. , vol.252 , pp. 248-262
    • Derewenda, Z.S.1    Lee, L.2    Derewenda, U.3
  • 25
    • 0023465103 scopus 로고
    • Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients
    • Abraham, D.J. & Leo, A.J. (1987). Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients. Proteins 2, 130-152.
    • (1987) Proteins , vol.2 , pp. 130-152
    • Abraham, D.J.1    Leo, A.J.2
  • 26
    • 0029933361 scopus 로고    scopus 로고
    • Crystal structure of PotD, the primary receptor of the polyamine transport system in escherichia coli
    • Sugiyama, S., Vassylyev, D.G., Matsushima, M., Kashiwagi, K., Igarashi, K. & Morikawa, K. (1996). Crystal structure of PotD, the primary receptor of the polyamine transport system in escherichia coli. J. Biol. Chem. 271, 9519-9525.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9519-9525
    • Sugiyama, S.1    Vassylyev, D.G.2    Matsushima, M.3    Kashiwagi, K.4    Igarashi, K.5    Morikawa, K.6
  • 27
    • 0032518247 scopus 로고    scopus 로고
    • Crystal structure of the NAD complex of human deoxyhypusine synthase: An enzyme with a ball-and-chain mechanism for blocking the active site
    • Liao, D.-I., Wolff, E.G., Park, M.H. & Davies, D.R. (1998). Crystal structure of the NAD complex of human deoxyhypusine synthase: An enzyme with a ball-and-chain mechanism for blocking the active site. Structure 6, 23-32.
    • (1998) Structure , vol.6 , pp. 23-32
    • Liao, D.-I.1    Wolff, E.G.2    Park, M.H.3    Davies, D.R.4
  • 28
    • 0021989550 scopus 로고
    • A potent irreversible inactivator of mammalian polyamine oxidase
    • Bey, P., Bolkenius, F.N., Seiler, N. & Casara, P. (1985). A potent irreversible inactivator of mammalian polyamine oxidase. J. Med. Chem. 28, 1-2.
    • (1985) J. Med. Chem. , vol.28 , pp. 1-2
    • Bey, P.1    Bolkenius, F.N.2    Seiler, N.3    Casara, P.4
  • 29
    • 0032577574 scopus 로고    scopus 로고
    • Identification of an FAD superfamily containing protoporphyrinogen oxidases, monoamine oxidases, and phytoene desaturase
    • Dailey, T.A. & Dailey H.a. (1998). Identification of an FAD superfamily containing protoporphyrinogen oxidases, monoamine oxidases, and phytoene desaturase. J. Biol. Chem. 273, 13658-13662.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13658-13662
    • Dailey, T.A.1    Dailey, H.A.2
  • 30
    • 0028809441 scopus 로고
    • Structure activity studies of the substrate binding site in monoamine oxidase B
    • Edmondson, D.e. (1995). Structure activity studies of the substrate binding site in monoamine oxidase B. Biochimie 77, 643-650.
    • (1995) Biochimie , vol.77 , pp. 643-650
  • 31
    • 0029034786 scopus 로고
    • Monoamine oxidases: Old friends hold many surprises
    • Singer, T.P. & Ramsay, R.R. (1995). Monoamine oxidases: Old friends hold many surprises. FASEB J. 9, 605-610.
    • (1995) FASEB J. , vol.9 , pp. 605-610
    • Singer, T.P.1    Ramsay, R.R.2
  • 32
    • 0032213790 scopus 로고    scopus 로고
    • Crystallisation and preliminary X-ray analysis of polyamine oxidase from Zea mays L
    • Binda, C., Coda, A., Angelini, R., Federico, R., Ascenzi, P. & Mattevi, A. (1998). Crystallisation and preliminary X-ray analysis of polyamine oxidase from Zea mays L. Acta Crystallogr. D 54, 1429-1431.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 1429-1431
    • Binda, C.1    Coda, A.2    Angelini, R.3    Federico, R.4    Ascenzi, P.5    Mattevi, A.6
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4.
    • Collaborative Computational Project Number 4. (1994). The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-767.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-767
  • 35
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross validation in iterated density-modification calculations
    • Cowtan, K.D. & Main, P. (1996). Phase combination and cross validation in iterated density-modification calculations. Acta Crystallogr. D 52, 43-48.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 43-48
    • Cowtan, K.D.1    Main, P.2
  • 36
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, AT. (1992). Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 37
    • 0013484996 scopus 로고
    • Density modification: Theory and practice
    • (Moras, D., Podjarny, A.D. & Thierry, J.C., eds), Oxford University Press, Oxford.
    • Podjarny, A.D. & Rees, B. (1991). Density modification: Theory and practice. In Crystallographic Computing 5: From Chemistry to Biology. (Moras, D., Podjarny, A.D. & Thierry, J.C., eds), pp. 361-372, Oxford University Press, Oxford.
    • (1991) Crystallographic Computing 5: from Chemistry to Biology. , pp. 361-372
    • Podjarny, A.D.1    Rees, B.2
  • 38
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 39
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud, D.E., Ten Eyck, L.F. & Matthews, B.W. (1987). An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallogr. A 43, 489-501.
    • (1987) Acta Crystallogr. A , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 41
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt, G.J. & Jones, T.A. (1994). Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr. D 50, 178-185.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 42
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (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
  • 43
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 44
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: Graphical representation and analysis of surface properties. Biophys. J. 64, 166-170.
    • (1993) Biophys. J. , vol.64 , pp. 166-170
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3


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