메뉴 건너뛰기




Volumn 25, Issue 3, 2000, Pages 126-132

Flavoenzymes: Diverse catalysts with recurrent features

Author keywords

[No Author keywords available]

Indexed keywords

FLAVOPROTEIN; OXIDOREDUCTASE;

EID: 0034161331     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(99)01533-9     Document Type: Review
Times cited : (451)

References (40)
  • 1
    • 0029038909 scopus 로고
    • Introduction: Flavoprotein structure and mechanism
    • Massey V. Introduction: flavoprotein structure and mechanism. FASEB J. 9:1995;473-475.
    • (1995) FASEB J. , vol.9 , pp. 473-475
    • Massey, V.1
  • 2
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein F.C.et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112:1977;535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1
  • 3
    • 0027304244 scopus 로고
    • Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate
    • Kim J.et al. Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Proc. Natl. Acad. Sci. U. S. A. 90:1993;7523-7527.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 7523-7527
    • Kim, J.1
  • 6
    • 0029780471 scopus 로고    scopus 로고
    • Three-dimensional structure of porcine kidney D-amino acid oxidase at 3 Å resolution
    • Mizutani H.et al. Three-dimensional structure of porcine kidney D-amino acid oxidase at 3 Å resolution. J. Biochem. 120:1996;14-17.
    • (1996) J. Biochem. , vol.120 , pp. 14-17
    • Mizutani, H.1
  • 7
    • 0033528745 scopus 로고    scopus 로고
    • Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants
    • Yue Q.K.et al. Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants. Biochemistry. 38:1999;4277-4286.
    • (1999) Biochemistry , vol.38 , pp. 4277-4286
    • Yue, Q.K.1
  • 8
    • 0024974962 scopus 로고
    • Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 Å resolution
    • Schreuder H.A.et al. Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 Å resolution. J. Mol. Biol. 208:1989;679-696.
    • (1989) J. Mol. Biol. , vol.208 , pp. 679-696
    • Schreuder, H.A.1
  • 9
    • 0033580880 scopus 로고    scopus 로고
    • Structure of the Escherichia coli fumarate reductase respiratory complex
    • Iverson T.M.et al. Structure of the Escherichia coli fumarate reductase respiratory complex. Science. 284:1999;1961-1966.
    • (1999) Science , vol.284 , pp. 1961-1966
    • Iverson, T.M.1
  • 10
    • 0001406338 scopus 로고    scopus 로고
    • Structure of L-aspartate oxidase: Implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family
    • Mattevi A.et al. Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. Structure. 7:1999;745-756.
    • (1999) Structure , vol.7 , pp. 745-756
    • Mattevi, A.1
  • 11
    • 0032527783 scopus 로고    scopus 로고
    • Protein folds and functions
    • Martin A.C.R.et al. Protein folds and functions. Structure. 6:1998;875-884.
    • (1998) Structure , vol.6 , pp. 875-884
    • Martin, A.C.R.1
  • 12
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • Dodson G., Wlodawer A. Catalytic triads and their relatives. Trends Biochem. Sci. 23:1998;347-352.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 13
    • 0024601564 scopus 로고
    • Mechanisms of flavoprotein-catalysed reactions
    • Ghisla S., Massey V. Mechanisms of flavoprotein-catalysed reactions. Eur. J. Biochem. 181:1989;1-17.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 14
    • 0033544926 scopus 로고    scopus 로고
    • Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase
    • Fraaije M.W.et al. Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase. J. Biol. Chem. 274:1999;35514-35520.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35514-35520
    • Fraaije, M.W.1
  • 15
    • 34548519907 scopus 로고    scopus 로고
    • A 30 Å long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase
    • Binda C.et al. A 30 Å long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase. Structure. 7:1999;265-276.
    • (1999) Structure , vol.7 , pp. 265-276
    • Binda, C.1
  • 16
    • 0026739339 scopus 로고
    • Correlation of X-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase
    • Barber M.J.et al. Correlation of X-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase. J. Biol. Chem. 267:1992;6611-6619.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6611-6619
    • Barber, M.J.1
  • 17
    • 0031423109 scopus 로고    scopus 로고
    • Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis
    • Björnberg O.et al. Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis. Biochemistry. 36:1997;16197-16205.
    • (1997) Biochemistry , vol.36 , pp. 16197-16205
    • Björnberg, O.1
  • 18
    • 0030011584 scopus 로고    scopus 로고
    • Flavinylation in wild-type trimethylamine dehydrogenase and differentially charged mutant enzymes: A study of the protein environment around the N1 of the flavin isoalloxazine
    • Mewies M.et al. Flavinylation in wild-type trimethylamine dehydrogenase and differentially charged mutant enzymes: a study of the protein environment around the N1 of the flavin isoalloxazine. Biochem. J. 317:1996;267-272.
    • (1996) Biochem. J. , vol.317 , pp. 267-272
    • Mewies, M.1
  • 19
    • 0023043185 scopus 로고
    • Oxidation-reduction properties of glycolate oxidase
    • Pace C., Stankovich M. Oxidation-reduction properties of glycolate oxidase. Biochemistry. 25:1986;2516-2522.
    • (1986) Biochemistry , vol.25 , pp. 2516-2522
    • Pace, C.1    Stankovich, M.2
  • 20
    • 0029040665 scopus 로고
    • Structure and mechanism of action of the acyl-CoA dehydrogenases
    • Thorpe C., Kim J-J.A.P. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 9:1995;718-725.
    • (1995) FASEB J. , vol.9 , pp. 718-725
    • Thorpe, C.1    Kim, J.-J.A.P.2
  • 21
    • 0032539518 scopus 로고    scopus 로고
    • Substrate activation by acyl-CoA dehydrogenase: Transition state stabilization and pKs of involved functional groups
    • Vock P.et al. Substrate activation by acyl-CoA dehydrogenase: transition state stabilization and pKs of involved functional groups. Biochemistry. 37:1998;1848-1860.
    • (1998) Biochemistry , vol.37 , pp. 1848-1860
    • Vock, P.1
  • 22
    • 0031568812 scopus 로고    scopus 로고
    • The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis
    • Rowland P.et al. The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis. Structure. 5:1997;239-252.
    • (1997) Structure , vol.5 , pp. 239-252
    • Rowland, P.1
  • 23
    • 0031047397 scopus 로고    scopus 로고
    • Kinetic characterization of wild-type and S229A mutant of MurB: Evidence for the role of Ser229 as a general acid
    • Benson T.E.et al. Kinetic characterization of wild-type and S229A mutant of MurB: evidence for the role of Ser229 as a general acid. Biochemistry. 36:1997;796-805.
    • (1997) Biochemistry , vol.36 , pp. 796-805
    • Benson, T.E.1
  • 24
    • 0032735104 scopus 로고    scopus 로고
    • Structural and mechanistic mapping of a unique fumarate reductase
    • Taylor P.et al. Structural and mechanistic mapping of a unique fumarate reductase. Nat. Struct. Biol. 6:1999;1108-1111.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1108-1111
    • Taylor, P.1
  • 25
    • 0032483986 scopus 로고    scopus 로고
    • The oxidative half-reaction of old yellow enzyme
    • Kohli R.M., Massey V. The oxidative half-reaction of old yellow enzyme. J. Biol. Chem. 273:1998;32763-32770.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32763-32770
    • Kohli, R.M.1    Massey, V.2
  • 26
    • 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.et al. Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity. Structure. 5:1997;907-920.
    • (1997) Structure , vol.5 , pp. 907-920
    • Mattevi, A.1
  • 27
    • 45549117277 scopus 로고
    • The reaction mechanism of D-amino acid oxidase: Concerted or not concerted?
    • Miura R., Miyake Y. The reaction mechanism of D-amino acid oxidase: concerted or not concerted? Bioorg. Chem. 16:1988;97-110.
    • (1988) Bioorg. Chem. , vol.16 , pp. 97-110
    • Miura, R.1    Miyake, Y.2
  • 28
    • 0029643799 scopus 로고
    • The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls
    • Benson T.E.et al. The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls. Structure. 4:1995;47-54.
    • (1995) Structure , vol.4 , pp. 47-54
    • Benson, T.E.1
  • 29
    • 0030879888 scopus 로고    scopus 로고
    • Orbital steering in the catalytic power of enzymes: Small structural changes with large catalytic consequences
    • Mesecar A.D.et al. Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences. Science. 277:1997;202-206.
    • (1997) Science , vol.277 , pp. 202-206
    • Mesecar, A.D.1
  • 30
    • 0030032041 scopus 로고    scopus 로고
    • The chemical mechanism of flavoprotein-catalysed α-hydroxy acid dehydrogenation: A mutational analysis
    • Lederer F.et al. The chemical mechanism of flavoprotein-catalysed α-hydroxy acid dehydrogenation: a mutational analysis. Biochem. Soc. Trans. 24:1996;77-83.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 77-83
    • Lederer, F.1
  • 31
    • 0031470918 scopus 로고    scopus 로고
    • Structure of D-amino acid oxidase: New insights from an old enzyme
    • Mattevi A.et al. Structure of D-amino acid oxidase: new insights from an old enzyme. Curr. Opin. Struct. Biol. 7:1997;804-810.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 804-810
    • Mattevi, A.1
  • 32
    • 0032054613 scopus 로고    scopus 로고
    • Quantum mechanical calculations on biological systems
    • Friesner R.A., Beachy M.D. Quantum mechanical calculations on biological systems. Curr. Opin. Struct. Biol. 8:1998;257-262.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 257-262
    • Friesner, R.A.1    Beachy, M.D.2
  • 33
    • 0033135955 scopus 로고    scopus 로고
    • 1.8 and 1.9 Å resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidase as a basis for modelling substrate complexes
    • Wohlfahrt G.et al. 1.8 and 1.9 Å resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidase as a basis for modelling substrate complexes. Acta Crystallogr. D55:1999;969-977.
    • (1999) Acta Crystallogr. , vol.55 , pp. 969-977
    • Wohlfahrt, G.1
  • 34
    • 0029562133 scopus 로고
    • The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit of p-cresol methylhydroxylase
    • Kim J.et al. The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit of p-cresol methylhydroxylase. J. Biol. Chem. 270:1995;31202-31209.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31202-31209
    • Kim, J.1
  • 35
    • 0030940522 scopus 로고    scopus 로고
    • Three-dimensional structures of glycolate oxidase with bound active-site inhibitors
    • Stenberg K., Lindqvist Y. Three-dimensional structures of glycolate oxidase with bound active-site inhibitors. Protein Sci. 6:1997;1009-1015.
    • (1997) Protein Sci. , vol.6 , pp. 1009-1015
    • Stenberg, K.1    Lindqvist, Y.2
  • 36
    • 0028774535 scopus 로고
    • Old yellow enzyme at 2 Å resolution: Overall structure, ligand binding and comparison with related flavoproteins
    • Fox K.M., Karplus P.A. Old yellow enzyme at 2 Å resolution: overall structure, ligand binding and comparison with related flavoproteins. Structure. 2:1994;1089-1105.
    • (1994) Structure , vol.2 , pp. 1089-1105
    • Fox, K.M.1    Karplus, P.A.2
  • 37
    • 2642708353 scopus 로고    scopus 로고
    • The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzyme function
    • Rowland P.et al. The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzyme function. Protein Sci. 7:1998;1269-1279.
    • (1998) Protein Sci. , vol.7 , pp. 1269-1279
    • Rowland, P.1
  • 38
    • 0027432601 scopus 로고
    • Crystal structure of cholesterol oxidase complexed with a steroid substrate: Implications for flavin adenine dinucleotide dependent alcohol oxidases
    • Li J.et al. Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases. Biochemistry. 32:1993;11507-11515.
    • (1993) Biochemistry , vol.32 , pp. 11507-11515
    • Li, J.1
  • 39
    • 0029068515 scopus 로고
    • The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction
    • Li R.et al. The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc. Natl. Acad. Sci. U. S. A. 92:1995;8846-8850.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 8846-8850
    • Li, R.1
  • 40
    • 0031054015 scopus 로고    scopus 로고
    • X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruovyl-UDP-N-acetylglucosamine at 1.8 Å resolution
    • Benson T.E.et al. X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruovyl-UDP-N-acetylglucosamine at 1.8 Å resolution. Biochemistry. 36:1997;806-811.
    • (1997) Biochemistry , vol.36 , pp. 806-811
    • Benson, T.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.