메뉴 건너뛰기




Volumn 52, Issue 8, 2013, Pages 1446-1455

Mutagenesis of a specificity-determining residue in tyrosine hydroxylase establishes that the enzyme is a robust phenylalanine hydroxylase but a fragile tyrosine hydroxylase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ALANINE-SCANNING MUTAGENESIS; AMINO ACID RESIDUES; AROMATIC AMINO ACID HYDROXYLASES; FITZPATRICK; HYDROPHOBIC INTERACTIONS; MUTANT PROTEINS; NEGATIVE CORRELATION; PHENYLALANINE HYDROXYLASE; SATURATION MUTAGENESIS; SUBSTRATE SPECIFICITY; TYROSINE HYDROXYLASE;

EID: 84874416569     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400031n     Document Type: Article
Times cited : (9)

References (60)
  • 1
    • 0033660818 scopus 로고    scopus 로고
    • The aromatic amino acid hydroxylases
    • (Purich, D. L. Ed.) John Wiley & Sons, Inc. New York
    • Fitzpatrick, P. F. (2000) The aromatic amino acid hydroxylases. In Advances in Enzymology and Related Areas of Molecular Biology (Purich, D. L., Ed.) pp 235-294, John Wiley & Sons, Inc., New York.
    • (2000) Advances in Enzymology and Related Areas of Molecular Biology , pp. 235-294
    • Fitzpatrick, P.F.1
  • 2
    • 0032852842 scopus 로고    scopus 로고
    • The tetrahydropterin-dependent amino acid hydroxylases
    • Fitzpatrick, P. F. (1999) The tetrahydropterin-dependent amino acid hydroxylases Annu. Rev. Biochem. 68, 355-381
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 355-381
    • Fitzpatrick, P.F.1
  • 3
    • 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., and Fitzpatrick, P. F. (1997) Characterization of chimeric pterin-dependent hydroxylases: Contributions of the regulatory domains of tyrosine and phenylalanine hydroxylase to substrate specificity Biochemistry 36, 11574-11582
    • (1997) Biochemistry , vol.36 , pp. 11574-11582
    • Daubner, S.C.1    Hillas, P.J.2    Fitzpatrick, P.F.3
  • 4
    • 0022417659 scopus 로고
    • Homology between phenylalanine and tyrosine hydroxylases reveals common structural and functional domains
    • Ledley, F. D., DiLella, A. G., Kwok, S. C. M., and Woo, S. L. C. (1985) Homology between phenylalanine and tyrosine hydroxylases reveals common structural and functional domains Biochemistry 24, 3389-3394
    • (1985) Biochemistry , vol.24 , pp. 3389-3394
    • Ledley, F.D.1    Dilella, A.G.2    Kwok, S.C.M.3    Woo, S.L.C.4
  • 5
    • 0023393590 scopus 로고
    • Full-length cDNA for rabbit tryptophan hydroxylase: Functional domains and evolution of aromatic amino acid hydroxylases
    • Grenett, H. E., Ledley, F. D., Reed, L. L., and Woo, S. L. C. (1987) Full-length cDNA for rabbit tryptophan hydroxylase: Functional domains and evolution of aromatic amino acid hydroxylases Proc. Natl. Acad. Sci. U.S.A. 84, 5530-5534
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 5530-5534
    • Grenett, H.E.1    Ledley, F.D.2    Reed, L.L.3    Woo, S.L.C.4
  • 6
    • 0345492036 scopus 로고    scopus 로고
    • Mechanism of aromatic amino acid hydroxylation
    • Fitzpatrick, P. F. (2003) Mechanism of aromatic amino acid hydroxylation Biochemistry 42, 14083-14091
    • (2003) Biochemistry , vol.42 , pp. 14083-14091
    • Fitzpatrick, P.F.1
  • 7
    • 3643061399 scopus 로고    scopus 로고
    • A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines
    • Hillas, P. J. and Fitzpatrick, P. F. (1996) A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines Biochemistry 35, 6969-6975
    • (1996) Biochemistry , vol.35 , pp. 6969-6975
    • Hillas, P.J.1    Fitzpatrick, P.F.2
  • 8
    • 33748496877 scopus 로고    scopus 로고
    • Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation
    • Pavon, J. A. and Fitzpatrick, P. F. (2006) Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation Biochemistry 45, 11030-11037
    • (2006) Biochemistry , vol.45 , pp. 11030-11037
    • Pavon, J.A.1    Fitzpatrick, P.F.2
  • 9
    • 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., and Stevens, R. C. (1997) Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases Nat. Struct. Biol. 4, 578-585
    • (1997) Nat. 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
  • 11
    • 0028826732 scopus 로고
    • Identification of Iron Ligands in Tyrosine-Hydroxylase by Mutagenesis of Conserved Histidinyl Residues
    • Ramsey, A. J., Daubner, S. C., Ehrlich, J. I., and Fitzpatrick, P. F. (1995) Identification of Iron Ligands in Tyrosine-Hydroxylase by Mutagenesis of Conserved Histidinyl Residues Protein Sci. 4, 2082-2086
    • (1995) Protein Sci. , vol.4 , pp. 2082-2086
    • Ramsey, A.J.1    Daubner, S.C.2    Ehrlich, J.I.3    Fitzpatrick, P.F.4
  • 12
    • 0033600563 scopus 로고    scopus 로고
    • Phenylalanine residues in the active site of tyrosine hydroxylase: Mutagenesis of Phe300 and Phe309 to alanine and metal ion-catalyzed hydroxylation of Phe300
    • Ellis, H. R., Daubner, S. C., McCulloch, R. I., and Fitzpatrick, P. F. (1999) Phenylalanine residues in the active site of tyrosine hydroxylase: Mutagenesis of Phe300 and Phe309 to alanine and metal ion-catalyzed hydroxylation of Phe300 Biochemistry 38, 10909-10914
    • (1999) Biochemistry , vol.38 , pp. 10909-10914
    • Ellis, H.R.1    Daubner, S.C.2    McCulloch, R.I.3    Fitzpatrick, P.F.4
  • 13
    • 0034093759 scopus 로고    scopus 로고
    • Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase
    • Erlandsen, H., Bjorgo, E., Flatmark, T., and Stevens, R. C. (2000) Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase Biochemistry 39, 2208-2217
    • (2000) Biochemistry , vol.39 , pp. 2208-2217
    • Erlandsen, H.1    Bjorgo, E.2    Flatmark, T.3    Stevens, R.C.4
  • 14
    • 0033528728 scopus 로고    scopus 로고
    • Site-directed mutants of charged residues in the active site of tyrosine hydroxylase
    • Daubner, S. C. and Fitzpatrick, P. F. (1999) Site-directed mutants of charged residues in the active site of tyrosine hydroxylase Biochemistry 38, 4448-4454
    • (1999) Biochemistry , vol.38 , pp. 4448-4454
    • Daubner, S.C.1    Fitzpatrick, P.F.2
  • 15
    • 0036083220 scopus 로고    scopus 로고
    • Role of tryptophan hydroxylase Phe313 in determining substrate specificity
    • Daubner, S. C., Moran, G. R., and Fitzpatrick, P. F. (2002) Role of tryptophan hydroxylase Phe313 in determining substrate specificity Biochem. Biophys. Res. Commun. 292, 639-641
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 639-641
    • Daubner, S.C.1    Moran, G.R.2    Fitzpatrick, P.F.3
  • 16
    • 0034664038 scopus 로고    scopus 로고
    • Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: Aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation
    • Daubner, S. C., Melendez, J., and Fitzpatrick, P. F. (2000) Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: Aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation Biochemistry 39, 9652-9661
    • (2000) Biochemistry , vol.39 , pp. 9652-9661
    • Daubner, S.C.1    Melendez, J.2    Fitzpatrick, P.F.3
  • 17
    • 0020491525 scopus 로고
    • Specificity of amino acids as activators and substrates for phenylalanine hydroxylase
    • Kaufman, S. and Mason, K. (1982) Specificity of amino acids as activators and substrates for phenylalanine hydroxylase J. Biol. Chem. 257, 14667-14678
    • (1982) J. Biol. Chem. , vol.257 , pp. 14667-14678
    • Kaufman, S.1    Mason, K.2
  • 18
    • 33745558560 scopus 로고    scopus 로고
    • A flexible loop in tyrosine hydroxylase controls coupling of amino acid hydroxylation to tetrahydropterin oxidation
    • Daubner, S. C., McGinnis, J. T., Gardner, M., Kroboth, S. L., Morris, A. R., and Fitzpatrick, P. F. (2006) A flexible loop in tyrosine hydroxylase controls coupling of amino acid hydroxylation to tetrahydropterin oxidation J. Mol. Biol. 359, 299-307
    • (2006) J. Mol. Biol. , vol.359 , pp. 299-307
    • Daubner, S.C.1    McGinnis, J.T.2    Gardner, M.3    Kroboth, S.L.4    Morris, A.R.5    Fitzpatrick, P.F.6
  • 20
    • 3643077110 scopus 로고    scopus 로고
    • Mutation to phenylalanine of tyrosine 371 in tyrosine hydroxylase increases the affinity for phenylalanine
    • Daubner, S. C. and Fitzpatrick, P. F. (1998) Mutation to phenylalanine of tyrosine 371 in tyrosine hydroxylase increases the affinity for phenylalanine Biochemistry 37, 16440-16444
    • (1998) Biochemistry , vol.37 , pp. 16440-16444
    • Daubner, S.C.1    Fitzpatrick, P.F.2
  • 21
    • 0035951089 scopus 로고    scopus 로고
    • Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase. Important role of Phe313 in substrate specificity
    • McKinney, J., Teigen, K., Frøystein, N. A., Salaün, C., Knappskog, P. M., Haavik, J., and Martínez, A. (2001) Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase. Important role of Phe313 in substrate specificity Biochemistry 40, 15591-15601
    • (2001) Biochemistry , vol.40 , pp. 15591-15601
    • McKinney, J.1    Teigen, K.2    Frøystein, N.A.3    Salaün, C.4    Knappskog, P.M.5    Haavik, J.6    Martínez, A.7
  • 22
    • 66649111062 scopus 로고    scopus 로고
    • Identification by hydrogen/deuterium exchange of structural changes in tyrosine hydroxylase associated with regulation
    • Wang, S., Sura, G. R., Dangott, L. J., and Fitzpatrick, P. F. (2009) Identification by hydrogen/deuterium exchange of structural changes in tyrosine hydroxylase associated with regulation Biochemistry 48, 4972-4979
    • (2009) Biochemistry , vol.48 , pp. 4972-4979
    • Wang, S.1    Sura, G.R.2    Dangott, L.J.3    Fitzpatrick, P.F.4
  • 23
    • 0026776269 scopus 로고
    • Site-directed mutagenesis of serine 40 of rat tyrosine hydroxylase. Effects of dopamine and cAMP-dependent phosphorylation on enzyme activity
    • Daubner, S., Lauriano, C., Haycock, J., and Fitzpatrick, P. (1992) Site-directed mutagenesis of serine 40 of rat tyrosine hydroxylase. Effects of dopamine and cAMP-dependent phosphorylation on enzyme activity J. Biol. Chem. 267, 12639-12646
    • (1992) J. Biol. Chem. , vol.267 , pp. 12639-12646
    • Daubner, S.1    Lauriano, C.2    Haycock, J.3    Fitzpatrick, P.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0025777217 scopus 로고
    • The steady state kinetic mechanism of rat tyrosine hydroxylase
    • Fitzpatrick, P. F. (1991) The steady state kinetic mechanism of rat tyrosine hydroxylase Biochemistry 30, 3658-3662
    • (1991) Biochemistry , vol.30 , pp. 3658-3662
    • Fitzpatrick, P.F.1
  • 26
    • 0031574292 scopus 로고    scopus 로고
    • Expression and characterization of the catalytic domain of human phenylalanine hydroxylase
    • Daubner, S. C., Hillas, P. J., and Fitzpatrick, P. F. (1997) Expression and characterization of the catalytic domain of human phenylalanine hydroxylase Arch. Biochem. Biophys. 348, 295-302
    • (1997) Arch. Biochem. Biophys. , vol.348 , pp. 295-302
    • Daubner, S.C.1    Hillas, P.J.2    Fitzpatrick, P.F.3
  • 27
    • 0142106379 scopus 로고    scopus 로고
    • 2.0 Å Resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)- l -alanine or l -norleucine: Substrate specificity and molecular motions related to substrate binding
    • Andersen, O. A., Stokka, A. J., Flatmark, T., and Hough, E. (2003) 2.0 Å Resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)- l -alanine or l -norleucine: Substrate specificity and molecular motions related to substrate binding J. Mol. Biol. 333, 747-757
    • (2003) J. Mol. Biol. , vol.333 , pp. 747-757
    • Andersen, O.A.1    Stokka, A.J.2    Flatmark, T.3    Hough, E.4
  • 28
    • 79952783028 scopus 로고    scopus 로고
    • Evidence for a high spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylase
    • Panay, A. J., Lee, M., Krebs, C., Bollinger, J. M., Jr., and Fitzpatrick, P. F. (2011) Evidence for a high spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylase Biochemistry 50, 1928-1933
    • (2011) Biochemistry , vol.50 , pp. 1928-1933
    • Panay, A.J.1    Lee, M.2    Krebs, C.3    Bollinger, Jr.J.M.4    Fitzpatrick, P.F.5
  • 30
    • 0025900994 scopus 로고
    • Studies of the rate-limiting step in the tyrosine hydroxylase reaction: Alternate substrates, solvent isotope effects, and transition state analogs
    • Fitzpatrick, P. F. (1991) Studies of the rate-limiting step in the tyrosine hydroxylase reaction: Alternate substrates, solvent isotope effects, and transition state analogs Biochemistry 30, 6386-6391
    • (1991) Biochemistry , vol.30 , pp. 6386-6391
    • Fitzpatrick, P.F.1
  • 32
    • 0034636184 scopus 로고    scopus 로고
    • Mutation of serine 395 of tyrosine hydroxylase decouples oxygen-oxygen bond cleavage and tyrosine hydroxylation
    • Ellis, H. R., Daubner, S. C., and Fitzpatrick, P. F. (2000) Mutation of serine 395 of tyrosine hydroxylase decouples oxygen-oxygen bond cleavage and tyrosine hydroxylation Biochemistry 39, 4174-4181
    • (2000) Biochemistry , vol.39 , pp. 4174-4181
    • Ellis, H.R.1    Daubner, S.C.2    Fitzpatrick, P.F.3
  • 33
    • 0037465514 scopus 로고    scopus 로고
    • Characterization of metal ligand mutants of tyrosine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad
    • Fitzpatrick, P. F., Ralph, E. C., Ellis, H. R., Willmon, O. J., and Daubner, S. C. (2003) Characterization of metal ligand mutants of tyrosine hydroxylase: insights into the plasticity of a 2-histidine-1-carboxylate triad Biochemistry 42, 2081-2088
    • (2003) Biochemistry , vol.42 , pp. 2081-2088
    • Fitzpatrick, P.F.1    Ralph, E.C.2    Ellis, H.R.3    Willmon, O.J.4    Daubner, S.C.5
  • 34
    • 0346434118 scopus 로고    scopus 로고
    • Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps
    • Frantom, P. A. and Fitzpatrick, P. F. (2003) Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps J. Am. Chem. Soc. 125, 16190-16191
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16190-16191
    • Frantom, P.A.1    Fitzpatrick, P.F.2
  • 35
    • 0015977588 scopus 로고
    • The interpretation of protein structures: Total volume, group volume distributions and packing density
    • Richards, F. M. (1974) The interpretation of protein structures: Total volume, group volume distributions and packing density J. Mol. Biol. 82, 1-14
    • (1974) J. Mol. Biol. , vol.82 , pp. 1-14
    • Richards, F.M.1
  • 37
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins
    • Chothia, C. (1976) The nature of the accessible and buried surfaces in proteins J. Mol. Biol. 105, 1-12
    • (1976) J. Mol. Biol. , vol.105 , pp. 1-12
    • Chothia, C.1
  • 38
    • 0000484499 scopus 로고
    • Hydrophobic parameters π of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides
    • Fauchere, J.-L. and Pliska, V. (1983) Hydrophobic parameters π of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides Eur. J. Med. Chem. 18, 369-375
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchere, J.-L.1    Pliska, V.2
  • 39
    • 0021977590 scopus 로고
    • Amino acid side-chain partition energies and distribution of residues in soluble proteins
    • Guy, H. R. (1985) Amino acid side-chain partition energies and distribution of residues in soluble proteins Biophys. J. 47, 61-70
    • (1985) Biophys. J. , vol.47 , pp. 61-70
    • Guy, H.R.1
  • 40
    • 0022861340 scopus 로고
    • The role of solvent polarity in the free energy of transfer of amino acid side chains from water to organic solvents
    • Damodaran, S. and Song, K. B. (1986) The role of solvent polarity in the free energy of transfer of amino acid side chains from water to organic solvents J. Biol. Chem. 261, 7220-7222
    • (1986) J. Biol. Chem. , vol.261 , pp. 7220-7222
    • Damodaran, S.1    Song, K.B.2
  • 41
    • 33845280446 scopus 로고
    • Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution
    • Radzicka, A. and Wolfenden, R. (1988) Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution Biochemistry 27, 1664-1670
    • (1988) Biochemistry , vol.27 , pp. 1664-1670
    • Radzicka, A.1    Wolfenden, R.2
  • 42
    • 0031008576 scopus 로고    scopus 로고
    • Hydrophobicity regained
    • Karplus, P. A. (1997) Hydrophobicity regained Protein Sci. 6, 1302-1307
    • (1997) Protein Sci. , vol.6 , pp. 1302-1307
    • Karplus, P.A.1
  • 43
    • 0028039678 scopus 로고
    • Kinetic isotope effects on hydroxylation of ring-deuterated phenylalanines by tyrosine hydroxylase provide evidence against partitioning of an arene oxide intermediate
    • Fitzpatrick, P. F. (1994) Kinetic isotope effects on hydroxylation of ring-deuterated phenylalanines by tyrosine hydroxylase provide evidence against partitioning of an arene oxide intermediate J. Am. Chem. Soc. 116, 1133-1134
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 1133-1134
    • Fitzpatrick, P.F.1
  • 44
    • 0025804515 scopus 로고
    • Hydroxylation of 4-methylphenylalanine by rat liver phenylalanine hydroxylase
    • Siegmund, H.-U. and Kaufman, S. (1991) Hydroxylation of 4-methylphenylalanine by rat liver phenylalanine hydroxylase J. Biol. Chem. 266, 2903-2910
    • (1991) J. Biol. Chem. , vol.266 , pp. 2903-2910
    • Siegmund, H.-U.1    Kaufman, S.2
  • 45
    • 28444448357 scopus 로고    scopus 로고
    • Intrinsic isotope effects on benzylic hydroxylation by the aromatic amino acid hydroxylases: Evidence for hydrogen tunneling, coupled motion, and similar reactivities
    • Pavon, J. A. and Fitzpatrick, P. F. (2005) Intrinsic isotope effects on benzylic hydroxylation by the aromatic amino acid hydroxylases: Evidence for hydrogen tunneling, coupled motion, and similar reactivities J. Am. Chem. Soc. 127, 16414-16415
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16414-16415
    • Pavon, J.A.1    Fitzpatrick, P.F.2
  • 46
    • 0027247791 scopus 로고
    • Products of the tyrosine-dependent oxidation of tetrahydrobiopterin by rat liver phenylalanine hydroxylase
    • Davis, M. D. and Kaufman, S. (1993) Products of the tyrosine-dependent oxidation of tetrahydrobiopterin by rat liver phenylalanine hydroxylase Arch. Biochem. Biophys. 304, 9-16
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 9-16
    • Davis, M.D.1    Kaufman, S.2
  • 47
    • 79959251862 scopus 로고    scopus 로고
    • Identification of Phenylalanine 3-Hydroxylase for meta-Tyrosine Biosynthesis
    • Zhang, W., Ames, B. D., and Walsh, C. T. (2011) Identification of Phenylalanine 3-Hydroxylase for meta-Tyrosine Biosynthesis Biochemistry 50, 5401-5403
    • (2011) Biochemistry , vol.50 , pp. 5401-5403
    • Zhang, W.1    Ames, B.D.2    Walsh, C.T.3
  • 48
    • 0034811728 scopus 로고    scopus 로고
    • Steric Control of Oxygenation Regiochemistry in Soybean Lipoxygenase-1
    • Knapp, M. J., Seebeck, F. P., and Klinman, J. P. (2001) Steric Control of Oxygenation Regiochemistry in Soybean Lipoxygenase-1 J. Am. Chem. Soc. 123, 2931-2932
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2931-2932
    • Knapp, M.J.1    Seebeck, F.P.2    Klinman, J.P.3
  • 49
    • 0017272554 scopus 로고
    • Enzyme Recruitment in Evolution of New Function
    • Jensen, R. A. (1976) Enzyme Recruitment in Evolution of New Function Annu. Rev. Microbiol. 30, 409-425
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 50
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O'Brien, P. J. and Herschlag, D. (1999) Catalytic promiscuity and the evolution of new enzymatic activities Chem. Biol. 6, R91-R105
    • (1999) Chem. Biol. , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 51
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme Promiscuity: A Mechanistic and Evolutionary Perspective
    • Tawfik, D. S. and Khersonsky, O. (2010) Enzyme Promiscuity: A Mechanistic and Evolutionary Perspective Annu. Rev. Biochem. 79, 471-505
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 471-505
    • Tawfik, D.S.1    Khersonsky, O.2
  • 52
    • 84855291324 scopus 로고    scopus 로고
    • Toward a systems biology perspective on enzyme evolution
    • Copley, S. D. (2012) Toward a systems biology perspective on enzyme evolution J. Biol. Chem. 287, 3-10
    • (2012) J. Biol. Chem. , vol.287 , pp. 3-10
    • Copley, S.D.1
  • 53
    • 79952449396 scopus 로고    scopus 로고
    • Tyrosine hydroxylase and regulation of dopamine synthesis
    • Daubner, S. C., Le, T., and Wang, S. (2011) Tyrosine hydroxylase and regulation of dopamine synthesis Arch. Biochem. Biophys. 508, 1-12
    • (2011) Arch. Biochem. Biophys. , vol.508 , pp. 1-12
    • Daubner, S.C.1    Le, T.2    Wang, S.3
  • 54
    • 84857812487 scopus 로고    scopus 로고
    • Allosteric regulation of phenylalanine hydroxylase
    • Fitzpatrick, P. F. (2012) Allosteric regulation of phenylalanine hydroxylase Arch. Biochem. Biophys. 519, 194-201
    • (2012) Arch. Biochem. Biophys. , vol.519 , pp. 194-201
    • Fitzpatrick, P.F.1
  • 55
    • 0038777517 scopus 로고    scopus 로고
    • Evaluation of methods for measuring amino acid hydrophobicities and interactions
    • Biswas, K. M., DeVido, D. R., and Dorsey, J. G. (2003) Evaluation of methods for measuring amino acid hydrophobicities and interactions J. Chromatogr., A 1000, 637-655
    • (2003) J. Chromatogr., A , vol.1000 , pp. 637-655
    • Biswas, K.M.1    Devido, D.R.2    Dorsey, J.G.3
  • 56
    • 75649097134 scopus 로고    scopus 로고
    • Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: Comparison with other hydrophilicity/hydrophobicity scales
    • Mant, C. T., Kovacs, J. M., Kim, H.-M., Pollock, D. D., and Hodges, R. S. (2009) Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: Comparison with other hydrophilicity/hydrophobicity scales Pept. Sci. 92, 573-595
    • (2009) Pept. Sci. , vol.92 , pp. 573-595
    • Mant, C.T.1    Kovacs, J.M.2    Kim, H.-M.3    Pollock, D.D.4    Hodges, R.S.5
  • 57
    • 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., and Stevens, R. C. (1998) 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, 13437-13445
    • (1998) Biochemistry , vol.37 , pp. 13437-13445
    • Goodwill, K.E.1    Sabatier, C.2    Stevens, R.C.3
  • 58
    • 0036071847 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)- l -alanine, and its implications for the mechanism of catalysis and substrate activation
    • Andersen, O. A., Flatmark, T., and Hough, E. (2002) Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)- l -alanine, and its implications for the mechanism of catalysis and substrate activation J. Mol. Biol. 320, 1095-1108
    • (2002) J. Mol. Biol. , vol.320 , pp. 1095-1108
    • Andersen, O.A.1    Flatmark, T.2    Hough, E.3
  • 59
    • 33747086893 scopus 로고    scopus 로고
    • Effects of ligands on the mobility of an active-site loop in tyrosine hydroxylase as monitored by fluorescence anisotropy
    • Sura, G. R., Lasagna, M., Gawandi, V., Reinhart, G. D., and Fitzpatrick, P. F. (2006) Effects of ligands on the mobility of an active-site loop in tyrosine hydroxylase as monitored by fluorescence anisotropy Biochemistry 45, 9632-9638
    • (2006) Biochemistry , vol.45 , pp. 9632-9638
    • Sura, G.R.1    Lasagna, M.2    Gawandi, V.3    Reinhart, G.D.4    Fitzpatrick, P.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.