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Volumn 294, Issue 3, 1999, Pages 807-823

The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: Implications for the catalytic mechanism

Author keywords

1H NMR spectroscopy; Docking; Non heme iron; Phenylalanine hydroxylase; Phenylketonuria

Indexed keywords

IRON; PHENYLALANINE; PHENYLALANINE 4 MONOOXYGENASE; PTERIN; TYROSINE 3 MONOOXYGENASE;

EID: 0033521234     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3288     Document Type: Article
Times cited : (60)

References (62)
  • 1
    • 0030934790 scopus 로고    scopus 로고
    • Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase
    • Aberg A., Yaremchuk A., Tukalo M., Rasmussen B., Cusack S. Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase. Biochemistry. 36:1997;3084-3094.
    • (1997) Biochemistry , vol.36 , pp. 3084-3094
    • Aberg, A.1    Yaremchuk, A.2    Tukalo, M.3    Rasmussen, B.4    Cusack, S.5
  • 2
    • 0001318177 scopus 로고
    • Neutron difraction study of L-phenylalanine hydrochloride
    • Al-Karaghouli A. R., Koetzle T. F. Neutron difraction study of L-phenylalanine hydrochloride. Acta Crystallog. sect B. 31:1975;2461-2465.
    • (1975) Acta Crystallog. Sect B , vol.31 , pp. 2461-2465
    • Al-Karaghouli, A.R.1    Koetzle, T.F.2
  • 3
    • 0031573526 scopus 로고    scopus 로고
    • The 1.25 Å crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters
    • Auerbach G., Herrmann A., Gutlich M., Fischer M., Jacob U., Bacher A., Huber R. The 1.25 Å crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters. EMBO J. 16:1997;7219-7230.
    • (1997) EMBO J. , vol.16 , pp. 7219-7230
    • Auerbach, G.1    Herrmann, A.2    Gutlich, M.3    Fischer, M.4    Jacob, U.5    Bacher, A.6    Huber, R.7
  • 4
    • 0020581280 scopus 로고
    • 6,6-Dimethylpterins: Stable quinoid dihydropterin substrate for dihydropteridine reductase and tetrahydropterin cofactor for phenylalanine hydroxylase
    • Bailey S. W., Ayling J. E. 6,6-Dimethylpterins: stable quinoid dihydropterin substrate for dihydropteridine reductase and tetrahydropterin cofactor for phenylalanine hydroxylase. Biochemistry. 22:1983;1790-1798.
    • (1983) Biochemistry , vol.22 , pp. 1790-1798
    • Bailey, S.W.1    Ayling, J.E.2
  • 6
    • 0001031673 scopus 로고
    • The crystal structure of 6-methyl-7, 8-dihydropterine-monohydrochloride-monohydrate
    • Bieri J. H. The crystal structure of 6-methyl-7, 8-dihydropterine-monohydrochloride-monohydrate. Helv. Chim. Acta. 60:1977;2303-2308.
    • (1977) Helv. Chim. Acta , vol.60 , pp. 2303-2308
    • Bieri, J.H.1
  • 7
    • 0032188782 scopus 로고    scopus 로고
    • Partial characterization and three-dimensional-structural localization of eight mutations in exon 7 of the human phenylalanine hydroxylase gene associated with phenylketonuria
    • Bjørgo E., Knappskog P. M., Martínez A., Stevens R. C., Flatmark T. Partial characterization and three-dimensional-structural localization of eight mutations in exon 7 of the human phenylalanine hydroxylase gene associated with phenylketonuria. Eur. J. Biochem. 257:1998;1-10.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 1-10
    • Bjørgo, E.1    Knappskog, P.M.2    Martínez, A.3    Stevens, R.C.4    Flatmark, T.5
  • 8
    • 0015137756 scopus 로고
    • Two mechanisms for the inhibition in vitro of phenylalanine hydroxylase by catecholamines
    • Bublitz C. Two mechanisms for the inhibition in vitro of phenylalanine hydroxylase by catecholamines. Biochem. Pharmacol. 20:1971;2543-2553.
    • (1971) Biochem. Pharmacol. , vol.20 , pp. 2543-2553
    • Bublitz, C.1
  • 9
    • 0027215829 scopus 로고
    • The two-dimensional transferred nuclear Overhauser effect: Theory and practice
    • Campbell A. P., Sykes B. D. The two-dimensional transferred nuclear Overhauser effect: theory and practice. Annu. Rev. Biophys. Biomol. Struct. 22:1993;99-122.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 99-122
    • Campbell, A.P.1    Sykes, B.D.2
  • 10
    • 0000393431 scopus 로고
    • Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins
    • Clore G. M., Gronenborn A. M. Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins. J. Magn. Reson. 48:1982;402-417.
    • (1982) J. Magn. Reson. , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 12
    • 0033528728 scopus 로고    scopus 로고
    • Site-directed mutants of charged residues in the active site of tyrosine hydroxylase
    • Daubner S. C., Fitzpatrick P. F. Site-directed mutants of charged residues in the active site of tyrosine hydroxylase. Biochemistry. 38:1999;4448-4454.
    • (1999) Biochemistry , vol.38 , pp. 4448-4454
    • Daubner, S.C.1    Fitzpatrick, P.F.2
  • 13
    • 0030848479 scopus 로고    scopus 로고
    • Characterization of chimeric pterin-dependent hydroxylases: Contributions of the regulatory domains of tyrosine and phenylalanine hydroxylase to substrate specificity
    • Daubner S. C., Hillas P. J., Fitzpatrick P. F. Characterization of chimeric pterin-dependent hydroxylases: contributions of the regulatory domains of tyrosine and phenylalanine hydroxylase to substrate specificity. Biochemistry. 36:1997;11574-11582.
    • (1997) Biochemistry , vol.36 , pp. 11574-11582
    • Daubner, S.C.1    Hillas, P.J.2    Fitzpatrick, P.F.3
  • 14
    • 0024413420 scopus 로고
    • Evidence for the formation of the 4a-carbinolamine during the tyrosine- dependent oxidation of tetrahydrobiopterin by rat liver phenylalanine hydroxylase
    • Davis M. D., Kaufman S. Evidence for the formation of the 4a-carbinolamine during the tyrosine- dependent oxidation of tetrahydrobiopterin by rat liver phenylalanine hydroxylase. J. Biol. Chem. 264:1989;8585-8596.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8585-8596
    • Davis, M.D.1    Kaufman, S.2
  • 15
    • 0028109263 scopus 로고
    • Delineation of the catalytic core of phenylalanine hydroxylase and identification of glutamate 286 as a critical residue for pterin function
    • Dickson P. W., Jennings I. G., Cotton R. G. Delineation of the catalytic core of phenylalanine hydroxylase and identification of glutamate 286 as a critical residue for pterin function. J. Biol. Chem. 269:1994;20369-20375.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20369-20375
    • Dickson, P.W.1    Jennings, I.G.2    Cotton, R.G.3
  • 16
    • 0001745788 scopus 로고
    • Mechanism of oxygen activation by pteridine-dependent moooxygenases
    • Dix T. A., Benkovic S. J. Mechanism of oxygen activation by pteridine-dependent moooxygenases. Acc. Chem. Res. 21:1988;101-107.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 101-107
    • Dix, T.A.1    Benkovic, S.J.2
  • 17
    • 0031303781 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria
    • Erlandsen H., Fusetti F., Martínez A., Hough E., Flatmark T., Stevens R. C. Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nature Struct. Biol. 4:1997;995-1000.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 995-1000
    • Erlandsen, H.1    Fusetti, F.2    Martínez, A.3    Hough, E.4    Flatmark, T.5    Stevens, R.C.6
  • 18
    • 0032506049 scopus 로고    scopus 로고
    • Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 Å resolution
    • Erlandsen H., Flatmark T., Stevens R. C., Hough E. Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 Å resolution. Biochemistry. 37:1998;15638-15646.
    • (1998) Biochemistry , vol.37 , pp. 15638-15646
    • Erlandsen, H.1    Flatmark, T.2    Stevens, R.C.3    Hough, E.4
  • 19
    • 37049077608 scopus 로고
    • The use of cocrystallization as a method of stidying hydrogen bond preferences of 2-aminopyrimidine
    • Etter M. C., Adsmond D. A. The use of cocrystallization as a method of stidying hydrogen bond preferences of 2-aminopyrimidine. J. Chem. Soc. Chem. Commun. 8:1990;589-591.
    • (1990) J. Chem. Soc. Chem. Commun. , vol.8 , pp. 589-591
    • Etter, M.C.1    Adsmond, D.A.2
  • 20
    • 0025777217 scopus 로고
    • Steady-state kinetic mechanism of rat tyrosine hydroxylase
    • Fitzpatrick P. F. Steady-state kinetic mechanism of rat tyrosine hydroxylase. Biochemistry. 30:1991;3658-3662.
    • (1991) Biochemistry , vol.30 , pp. 3658-3662
    • Fitzpatrick, P.F.1
  • 21
    • 0001749787 scopus 로고    scopus 로고
    • Structural insights into the aromatic amino acid hydroxylases and their disease-related mutant forms
    • Flatmark T., Stevens R. C. Structural insights into the aromatic amino acid hydroxylases and their disease-related mutant forms. Chem. Rev. 99:1999;2137-2160.
    • (1999) Chem. Rev. , vol.99 , pp. 2137-2160
    • Flatmark, T.1    Stevens, R.C.2
  • 22
    • 0032490094 scopus 로고    scopus 로고
    • Oxygen-18 kinetic isotope effect studies of the tyrosine hydroxylase reaction: Evidence of rate limiting oxygen activation
    • Francisco W. A., Tian G. C., Fitzpatrick P. F., Klinman J. P. Oxygen-18 kinetic isotope effect studies of the tyrosine hydroxylase reaction: Evidence of rate limiting oxygen activation. J. Am. Chem. Soc. 120:1998;4057-4062.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4057-4062
    • Francisco, W.A.1    Tian, G.C.2    Fitzpatrick, P.F.3    Klinman, J.P.4
  • 23
    • 0032479302 scopus 로고    scopus 로고
    • Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria
    • Fusetti F., Erlandsen H., Flatmark T., Stevens R. C. Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria. J. Biol. Chem. 273:1998;16962-16967.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16962-16967
    • Fusetti, F.1    Erlandsen, H.2    Flatmark, T.3    Stevens, R.C.4
  • 24
    • 0031010420 scopus 로고    scopus 로고
    • Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases
    • Goodwill K. E., Sabatier C., Marks C., Raag R., Fitzpatrick P. F., Stevens R. C. Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases. Nature Struct. Biol. 4:1997;578-585.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 578-585
    • Goodwill, K.E.1    Sabatier, C.2    Marks, C.3    Raag, R.4    Fitzpatrick, P.F.5    Stevens, R.C.6
  • 25
    • 0032578427 scopus 로고    scopus 로고
    • Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 Å resolution: Self-hydroxylation of Phe300 and the pterin-binding site
    • Goodwill K. E., Sabatier C., Stevens R. C. Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 Å resolution: self-hydroxylation of Phe300 and the pterin-binding site. Biochemistry. 37:1998;13437-13445.
    • (1998) Biochemistry , vol.37 , pp. 13437-13445
    • Goodwill, K.E.1    Sabatier, C.2    Stevens, R.C.3
  • 26
    • 0025932859 scopus 로고
    • An evaluation of computational strategies for use in the determination of protein-structure from distance constraints obtained by nuclear-magnetic-resonance
    • Havel T. F. An evaluation of computational strategies for use in the determination of protein-structure from distance constraints obtained by nuclear-magnetic-resonance. Prog. Biophys. Mol. Biol. 56:1991;43-78.
    • (1991) Prog. Biophys. Mol. Biol. , vol.56 , pp. 43-78
    • Havel, T.F.1
  • 27
    • 0023430333 scopus 로고
    • Isolation and characterization of tetrahydropterin oxidation products generated in the tyrosine 3-monooxygenase (tyrosine hydroxylase) reaction
    • Haavik J., Flatmark T. Isolation and characterization of tetrahydropterin oxidation products generated in the tyrosine 3-monooxygenase (tyrosine hydroxylase) reaction. Eur. J. Biochem. 168:1987;21-26.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 21-26
    • Haavik, J.1    Flatmark, T.2
  • 28
    • 0023008949 scopus 로고
    • Stereoselective effects in the interactions of pterin cofactors with rat-liver phenylalanine 4-monooxygenase
    • Haavik J., Doskeland A. P., Flatmark T. Stereoselective effects in the interactions of pterin cofactors with rat-liver phenylalanine 4-monooxygenase. Eur. J. Biochem. 160:1986;1-8.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 1-8
    • Haavik, J.1    Doskeland, A.P.2    Flatmark, T.3
  • 29
    • 0000783838 scopus 로고    scopus 로고
    • Pterin-dependent amino acid hydroxylases
    • Kappock T. J., Caradonna J. P. Pterin-dependent amino acid hydroxylases. Chem. Rev. 96:1996;2659-2756.
    • (1996) Chem. Rev. , vol.96 , pp. 2659-2756
    • Kappock, T.J.1    Caradonna, J.P.2
  • 30
    • 0003129796 scopus 로고
    • Theoretical stereostructure of the neutral form of natural tetrahydrobiopterin
    • Katoh S., Sueoka T., Kurihara T. Theoretical stereostructure of the neutral form of natural tetrahydrobiopterin. Pteridines. 4:1993;27-31.
    • (1993) Pteridines , vol.4 , pp. 27-31
    • Katoh, S.1    Sueoka, T.2    Kurihara, T.3
  • 32
    • 0033599363 scopus 로고    scopus 로고
    • Circular dichroism and magnetic circular dichroism spectroscopy of the catalytically competent ferrous active site of phenylalanine hydroxylase and its interaction with pterin cofactor
    • Kemsley J. N., Mitic N., Zaleski K. L., Caradonna J. P., Solomon I. Circular dichroism and magnetic circular dichroism spectroscopy of the catalytically competent ferrous active site of phenylalanine hydroxylase and its interaction with pterin cofactor. J. Am. Chem. Soc. 121:1999;1528-1536.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1528-1536
    • Kemsley, J.N.1    Mitic, N.2    Zaleski, K.L.3    Caradonna, J.P.4    Solomon, I.5
  • 33
    • 0029164370 scopus 로고
    • Tryptophan fluorescence of human phenylalanine hydroxylase produced in Escherichia coli
    • Knappskog P. M., Haavik J. Tryptophan fluorescence of human phenylalanine hydroxylase produced in Escherichia coli. Biochemistry. 34:1995;11790-11799.
    • (1995) Biochemistry , vol.34 , pp. 11790-11799
    • Knappskog, P.M.1    Haavik, J.2
  • 34
    • 0028837437 scopus 로고
    • The PKU mutation S349P causes complete loss of catalytic activity in the recombinant phenylalanine hydroxylase enzyme
    • Knappskog P. M., Eiken H. G., Martínez A., Flatmark T., Apold J. The PKU mutation S349P causes complete loss of catalytic activity in the recombinant phenylalanine hydroxylase enzyme. Hum. Genet. 95:1995;171-173.
    • (1995) Hum. Genet. , vol.95 , pp. 171-173
    • Knappskog, P.M.1    Eiken, H.G.2    Martínez, A.3    Flatmark, T.4    Apold, J.5
  • 35
    • 0030437749 scopus 로고    scopus 로고
    • Structure/function relationships in human phenylalanine hydroxylase. Effect of terminal deletions on the oligomerization, activation and cooperativity of substrate binding to the enzyme
    • Knappskog P. M., Flatmark T., Aarden J. M., Haavik J., Martínez A. Structure/function relationships in human phenylalanine hydroxylase. Effect of terminal deletions on the oligomerization, activation and cooperativity of substrate binding to the enzyme. Eur. J. Biochem. 242:1996;813-821.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 813-821
    • Knappskog, P.M.1    Flatmark, T.2    Aarden, J.M.3    Haavik, J.4    Martínez, A.5
  • 38
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 39
    • 0032039677 scopus 로고    scopus 로고
    • Oxygen activating nonheme iron enzymes
    • Lange S., Que L. J. Oxygen activating nonheme iron enzymes. Curr. Opin. Chem. Biol. 2:1998;159-172.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 159-172
    • Lange, S.1    Que, L.J.2
  • 40
    • 0025011451 scopus 로고
    • Cooperative homotropic interaction of L-noradrenaline with the catalytic site of phenylalanine 4-monooxygenase
    • Martínez A., Haavik J., Flatmark T. Cooperative homotropic interaction of L-noradrenaline with the catalytic site of phenylalanine 4-monooxygenase. Eur. J. Biochem. 193:1990;211-219.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 211-219
    • Martínez, A.1    Haavik, J.2    Flatmark, T.3
  • 41
    • 0025922757 scopus 로고
    • 1H-NMR spectroscopic studies on the paramagnetic iron at the active site of phenylalanine hydroxylase and its interaction with substrates and inhibitors
    • 1H-NMR spectroscopic studies on the paramagnetic iron at the active site of phenylalanine hydroxylase and its interaction with substrates and inhibitors. Eur. J. Biochem. 198:1991;675-682.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 675-682
    • Martínez, A.1    Andersson, K.K.2    Haavik, J.3    Flatmark, T.4
  • 42
    • 0027296282 scopus 로고
    • Conformation and interaction of phenylalanine with the divalent cation at the active site of human recombinant tyrosine hydroxylase as determined by proton NMR
    • Martínez A., Abeygunawardana C., Haavik J., Flatmark T., Mildvan A. S. Conformation and interaction of phenylalanine with the divalent cation at the active site of human recombinant tyrosine hydroxylase as determined by proton NMR. Biochemistry. 32:1993a;6381-6390.
    • (1993) Biochemistry , vol.32 , pp. 6381-6390
    • Martínez, A.1    Abeygunawardana, C.2    Haavik, J.3    Flatmark, T.4    Mildvan, A.S.5
  • 43
    • 0027397303 scopus 로고
    • 1H-NMR paramagnetic relaxation. Changes in water accessibility to the iron at the active site upon substrate binding
    • 1H-NMR paramagnetic relaxation. Changes in water accessibility to the iron at the active site upon substrate binding. Eur. J. Biochem. 211:1993b;259-266.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 259-266
    • Martínez, A.1    Olafsdottir, S.2    Flatmark, T.3
  • 44
    • 0031946277 scopus 로고    scopus 로고
    • Proton NMR studies on the conformation of the pterin cofactor bound at the active site of recombinant human tyrosine hydroxylase
    • Martínez A., Vageli O., Pfleiderer W., Flatmark T. Proton NMR studies on the conformation of the pterin cofactor bound at the active site of recombinant human tyrosine hydroxylase. Pteridines. 9:1998;44-52.
    • (1998) Pteridines , vol.9 , pp. 44-52
    • Martínez, A.1    Vageli, O.2    Pfleiderer, W.3    Flatmark, T.4
  • 45
    • 0022381620 scopus 로고
    • Stereochemistry of biopterin cofactor and facile methods for the determination of the stereochemistry of a biologically active 5,6,7,8- tetrahydropterin
    • Matsuura S., Sugimoto T., Murata S., Sugawara Y., Iwasaki H. Stereochemistry of biopterin cofactor and facile methods for the determination of the stereochemistry of a biologically active 5,6,7,8- tetrahydropterin. J. Biochem. (Tokyo). 98:1985;1341-1348.
    • (1985) J. Biochem. (Tokyo) , vol.98 , pp. 1341-1348
    • Matsuura, S.1    Sugimoto, T.2    Murata, S.3    Sugawara, Y.4    Iwasaki, H.5
  • 47
    • 84986432941 scopus 로고
    • Automated docking with grid-based energy evaluation
    • Meng E. C., Shoichet B. K., Kuntz I. D. Automated docking with grid-based energy evaluation. J. Comput. Chem. 13:1992;505-524.
    • (1992) J. Comput. Chem. , vol.13 , pp. 505-524
    • Meng, E.C.1    Shoichet, B.K.2    Kuntz, I.D.3
  • 48
    • 0028057108 scopus 로고
    • Raster3D version-2.0 - A program for photorealistic molecular graphics
    • Merritt E. A., Murphy M. E. P. Raster3D version-2.0 - a program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 49
    • 0029658895 scopus 로고    scopus 로고
    • Mössbauer, electron-paramagnetic-resonance and X-ray-absorption fine- structure studies of the iron environment in recombinant human tyrosine hydroxylase
    • Meyer-Klaucke W., Winkler H., Schunemann V., Trautwein A. X., Nolting H. F., Haavik J. Mössbauer, electron-paramagnetic-resonance and X-ray-absorption fine- structure studies of the iron environment in recombinant human tyrosine hydroxylase. Eur. J. Biochem. 241:1996;432-439.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 432-439
    • Meyer-Klaucke, W.1    Winkler, H.2    Schunemann, V.3    Trautwein, A.X.4    Nolting, H.F.5    Haavik, J.6
  • 52
    • 0001087854 scopus 로고
    • Pteridine-containing ternary and quaternary complexes as models for metalloenzyme-pterin cofactor-substrate association - Structure of ternary copper(II)-2,2′-bipyridine lumazine complex and successful equilibrium study of a quaternary copper(II) system
    • Odani A., Masuda H., Inukai K., Yamauchi O. Pteridine-containing ternary and quaternary complexes as models for metalloenzyme-pterin cofactor-substrate association - Structure of ternary copper(II)-2,2′-bipyridine lumazine complex and successful equilibrium study of a quaternary copper(II) system. J. Am. Chem. Soc. 114:1992;6294-6300.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6294-6300
    • Odani, A.1    Masuda, H.2    Inukai, K.3    Yamauchi, O.4
  • 53
    • 0028067178 scopus 로고
    • The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins
    • Oh B. H., Kang C. H., De Bondt H., Kim S. H., Nikaido K., Joshi A. K., Ames G. F. The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins. J. Biol. Chem. 269:1994;4135-4143.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4135-4143
    • Oh, B.H.1    Kang, C.H.2    De Bondt, H.3    Kim, S.H.4    Nikaido, K.5    Joshi, A.K.6    Ames, G.F.7
  • 54
    • 0344178151 scopus 로고    scopus 로고
    • 1H NMR paramagnetic relaxation. Effect of L-Phe and comparison with the rat enzyme
    • 1H NMR paramagnetic relaxation. Effect of L-Phe and comparison with the rat enzyme. J. Biol. Chem. 274:1999;6280-6284.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6280-6284
    • Olafsdottir, S.1    Martínez, A.2
  • 55
    • 0026951903 scopus 로고
    • Gradient- tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenar V. Gradient- tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 57
    • 0032416666 scopus 로고    scopus 로고
    • Crystal structure of constitutive endothelial nitric oxide synthase: A paradigm for pterin function involving a novel metal center
    • Raman C. S., Li H., Martasek P., Kral V., Masters B. S., Poulos T. L. Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center. Cell. 95:1998;939-950.
    • (1998) Cell , vol.95 , pp. 939-950
    • Raman, C.S.1    Li, H.2    Martasek, P.3    Kral, V.4    Masters, B.S.5    Poulos, T.L.6
  • 59
    • 0027937757 scopus 로고
    • Regulation of rat liver phenylalanine hydroxylase. II. Substrate binding and the role of activation in the control of enzymatic activity
    • Shiman R., Xia T., Hill M. A., Gray D. W. Regulation of rat liver phenylalanine hydroxylase. II. Substrate binding and the role of activation in the control of enzymatic activity. J. Biol. Chem. 269:1994;24647-24656.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24647-24656
    • Shiman, R.1    Xia, T.2    Hill, M.A.3    Gray, D.W.4
  • 60
    • 0001350902 scopus 로고
    • Gradient-tailored water suppression for H-1-N-15 HSQC experiments optimized to retain full sensitivity
    • Sklenár V., Piotto M., Leppik R., Saudek V. Gradient-tailored water suppression for H-1-N-15 HSQC experiments optimized to retain full sensitivity. J. Magn. Reson. 102:1993;241-245.
    • (1993) J. Magn. Reson. , vol.102 , pp. 241-245
    • Sklenár, V.1    Piotto, M.2    Leppik, R.3    Saudek, V.4
  • 62
    • 0021959536 scopus 로고
    • Tetrahydrobiopterin analogues: Solution conformations of 6-methyltetrahydropterin, 7-methyltetrahydropterin, and cis- And trans- 6,7-dimethyltetrahydropterins as determined by proton nuclear magnetic resonance
    • Williams T. C., Storm C. B. Tetrahydrobiopterin analogues: solution conformations of 6-methyltetrahydropterin, 7-methyltetrahydropterin, and cis- and trans- 6,7-dimethyltetrahydropterins as determined by proton nuclear magnetic resonance. Biochemistry. 24:1985;458-466.
    • (1985) Biochemistry , vol.24 , pp. 458-466
    • Williams, T.C.1    Storm, C.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.