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Volumn 6, Issue 5, 1997, Pages 1009-1015

Three-dimensional structures of glycolate oxidase with bound active- site inhibitors

Author keywords

drug design; flavin enzyme; glycolate oxidase; inhibitor binding; molecular replacement; protein crystallography

Indexed keywords

HYDROXY ACID OXIDASE A;

EID: 0030940522     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060506     Document Type: Article
Times cited : (57)

References (25)
  • 1
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger A, Kuriyan J, Karplus M. 1987. Crystallographic R factor refinement by molecular dynamics. Science 235:458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.1    Kuriyan, J.2    Karplus, M.3
  • 2
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein crystallography
    • CCP4. 1994. Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein crystallography. Acta Cryslallogr D50:760-763.
    • (1994) Acta Cryslallogr , vol.D50 , pp. 760-763
  • 3
    • 79952608525 scopus 로고
    • Accurate bond angle parameters for X-ray protein structure refinement
    • Engh RA, Huber R. 1991. Accurate bond angle parameters for X-ray protein structure refinement. Acta Crystallogr A47:392-400.
    • (1991) Acta Crystallogr , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 4
    • 0040077039 scopus 로고
    • Studies on glycollate oxidase from pea leaves. Determination of stereospecificity and mode of inhibition by α-hydroxybutynoate
    • Fendrich G, Ghisla S. 1982. Studies on glycollate oxidase from pea leaves. Determination of stereospecificity and mode of inhibition by α-hydroxybutynoate. Biochim Biophys Acta 30:242-248.
    • (1982) Biochim Biophys Acta , vol.30 , pp. 242-248
    • Fendrich, G.1    Ghisla, S.2
  • 5
    • 84991984075 scopus 로고
    • Mechanisms of flavoprotein-catalyzed reactions
    • Ghisla S, Massey V. 1989. Mechanisms of flavoprotein-catalyzed reactions. Eur J Biochem 2:243-289.
    • (1989) Eur J Biochem , vol.2 , pp. 243-289
    • Ghisla, S.1    Massey, V.2
  • 6
    • 0028073722 scopus 로고
    • Effect of DL α-lipoic acid in glyoxylate-induced acute lithiasis
    • Jayanthi S, Saravanan N, Varalakkshmi P. 1994. Effect of DL α-lipoic acid in glyoxylate-induced acute lithiasis. Pharmacol Res 30:281-288.
    • (1994) Pharmacol Res , vol.30 , pp. 281-288
    • Jayanthi, S.1    Saravanan, N.2    Varalakkshmi, P.3
  • 7
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein 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
  • 9
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 10
    • 0025786780 scopus 로고
    • Amino acid sequence of long chain α-hydroxy acid oxidase from rat kidney, a member of the family of FMN-dependent α-hydroxy acid-oxidizing enzymes
    • Lê KHD, Lederer F. 1991. Amino acid sequence of long chain α-hydroxy acid oxidase from rat kidney, a member of the family of FMN-dependent α-hydroxy acid-oxidizing enzymes. J Biol Chem 266:20877-20881.
    • (1991) J Biol Chem , vol.266 , pp. 20877-20881
    • Lê, K.H.D.1    Lederer, F.2
  • 11
    • 0030032041 scopus 로고    scopus 로고
    • The chemical mechanism of flavoprotein-catalysed α-hydroxy acid dehydrogenation: A mutational analysis
    • Lederer F, Belmouden A, Gondry M. 1996. The chemical mechanism of flavoprotein-catalysed α-hydroxy acid dehydrogenation: A mutational analysis. Biochem Soc Trans 24:77-83.
    • (1996) Biochem Soc Trans , vol.24 , pp. 77-83
    • Lederer, F.1    Belmouden, A.2    Gondry, M.3
  • 12
    • 0018787021 scopus 로고
    • Preliminary crystallographic data for glycolate oxidase from spinach
    • Lindqvist Y, Brändén C-I. 1979. Preliminary crystallographic data for glycolate oxidase from spinach. J Biol Chem 254:7403-7404.
    • (1979) J Biol Chem , vol.254 , pp. 7403-7404
    • Lindqvist, Y.1    Brändén, C.-I.2
  • 13
    • 0024962365 scopus 로고
    • Refined structure of spinach glycolate oxidase at 2 Å resolution
    • Lindqvist Y. 1989. Refined structure of spinach glycolate oxidase at 2 Å resolution. J Mol Biol 209:151-166.
    • (1989) J Mol Biol , vol.209 , pp. 151-166
    • Lindqvist, Y.1
  • 14
    • 0024977935 scopus 로고
    • The active site of spinach glycolate oxidase
    • Lindqvist Y, Brändén C-I. 1989. The active site of spinach glycolate oxidase. J Biol Chem 264:3624-3628.
    • (1989) J Biol Chem , vol.264 , pp. 3624-3628
    • Lindqvist, Y.1    Brändén, C.-I.2
  • 15
    • 0025853478 scopus 로고
    • 2 are structurally homologous and evolutionary related enzymes with distinctly different function and flavin mononucleotide binding
    • 2 are structurally homologous and evolutionary related enzymes with distinctly different function and flavin mononucleotide binding. J Biol Chem 266:3198-3207.
    • (1991) J Biol Chem , vol.266 , pp. 3198-3207
    • Lindqvist, Y.1    Brändén, C.-I.2    Mathews, F.S.3    Lederer, F.4
  • 16
    • 0025741770 scopus 로고
    • Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: Purification and characterization
    • Macheroux P, Massey V, Thiele DJ. 1991. Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: Purification and characterization. Biochemistry 30:4612-4619.
    • (1991) Biochemistry , vol.30 , pp. 4612-4619
    • Macheroux, P.1    Massey, V.2    Thiele, D.J.3
  • 19
    • 0002452464 scopus 로고
    • DENZO
    • Sawyer L, Isaac N, Bailey S, eds. SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski Z. 1993. DENZO. In: Sawyer L, Isaac N, Bailey S, eds. Data collection and processing. SERC Daresbury Laboratory, Warrington, UK. pp 80-86.
    • (1993) Data Collection and Processing , pp. 80-86
    • Otwinowski, Z.1
  • 22
    • 0028954322 scopus 로고
    • Involvement of tyr24 and trp108 in substrate binding and substrate specificity of glycolate oxidase
    • Stenberg K, Clausen T, Lindqvist Y, Macheroux P. 1995. Involvement of tyr24 and trp108 in substrate binding and substrate specificity of glycolate oxidase. Eur J Biochem 228:408-416.
    • (1995) Eur J Biochem , vol.228 , pp. 408-416
    • Stenberg, K.1    Clausen, T.2    Lindqvist, Y.3    Macheroux, P.4
  • 23
    • 0030294805 scopus 로고    scopus 로고
    • High level expression, purification and crystallization of recombinant spinach glycolate oxidase in Escherichia coli
    • Stenberg K, Lindqvist Y. 1996. High level expression, purification and crystallization of recombinant spinach glycolate oxidase in Escherichia coli. Prot Expr Purif 8:295-298.
    • (1996) Prot Expr Purif , vol.8 , pp. 295-298
    • Stenberg, K.1    Lindqvist, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.