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Volumn 72, Issue 1, 1997, Pages 363-372

Bound ligand motion in crystalline carboxypeptidase A

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE A; DEUTERIUM; DEXTRO PHENYLALANINE; PHENYL GROUP; PHENYLACETIC ACID; PHENYLALANINE; PHENYLPROPIONIC ACID DERIVATIVE;

EID: 0031036753     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78675-2     Document Type: Article
Times cited : (5)

References (35)
  • 1
    • 0026701686 scopus 로고
    • Solid-state NMR assessment of enzyme active center structure under nonaqueous conditions
    • Burke, P. A., R. G. Griffin, and A. M. Klibanov. 1992. Solid-state NMR assessment of enzyme active center structure under nonaqueous conditions. J. Biol. Chem. 267:20057-20064.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20057-20064
    • Burke, P.A.1    Griffin, R.G.2    Klibanov, A.M.3
  • 2
    • 0027909364 scopus 로고
    • Solid-state nuclear magnetic resonance investigation of solvent dependence of tyrosyl ring motion in an enzyme
    • Burke, P. A., R. G. Griffin, and A. M. Klibanov. 1993. Solid-state nuclear magnetic resonance investigation of solvent dependence of tyrosyl ring motion in an enzyme. Biotechnol. Bioeng. 42:87-94.
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 87-94
    • Burke, P.A.1    Griffin, R.G.2    Klibanov, A.M.3
  • 3
    • 0024335390 scopus 로고
    • Binding of D-phenylalanine and D-tyrosine to carboxypeptidase A
    • Christianson, D. W., S. Mangani, G. Shoham, and W. L. Lipscomb. 1989. Binding of D-phenylalanine and D-tyrosine to carboxypeptidase A. J. Biol. Chem. 264:12849-12853.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12849-12853
    • Christianson, D.W.1    Mangani, S.2    Shoham, G.3    Lipscomb, W.L.4
  • 4
    • 33947487538 scopus 로고
    • Metallocarboxypeptidase-inhibitor complexes
    • Coleman, J. E., and B. C. Vallee. 1964. Metallocarboxypeptidase-inhibitor complexes. Biochemistry. 3:1876-1879.
    • (1964) Biochemistry , vol.3 , pp. 1876-1879
    • Coleman, J.E.1    Vallee, B.C.2
  • 5
    • 0029070171 scopus 로고
    • Omega loop: Nonregular secondary structure significant in protein function and stability
    • Fetrow, J. S. 1995. Omega loop: nonregular secondary structure significant in protein function and stability. FASEB J. 9:708-717.
    • (1995) FASEB J. , vol.9 , pp. 708-717
    • Fetrow, J.S.1
  • 8
    • 0000670869 scopus 로고
    • Molecular structure and dynamic of crystalline p-fluoro-D,L-phenylalanine: A combined x-ray/NMR investigation
    • Hiyama, Y., J. V. Silverton, D. A. Torchia, J. T. Gerig, and S. J. Hammond. 1986. Molecular structure and dynamic of crystalline p-fluoro-D,L-phenylalanine: a combined x-ray/NMR investigation. J. Am. Chem. Soc. 108:2715-2723.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 2715-2723
    • Hiyama, Y.1    Silverton, J.V.2    Torchia, D.A.3    Gerig, J.T.4    Hammond, S.J.5
  • 10
    • 0343347765 scopus 로고
    • Magnetic resonance studies of α-chymotrypsin crystals
    • Hsi, E., R. Mason, and R. G. Bryant. 1976. Magnetic resonance studies of α-chymotrypsin crystals. J. Phys. Chem. 80:2592-2597.
    • (1976) J. Phys. Chem. , vol.80 , pp. 2592-2597
    • Hsi, E.1    Mason, R.2    Bryant, R.G.3
  • 11
    • 0014942119 scopus 로고
    • The structure of carboxypeptidase A. VIII. Atomic interaction at 0.2 nm resolution, a new study of the complex of glycyltyrosine with CPA, and mechanistic deductions
    • Lipscomb, W. N., G. N. Reeke, J. A. Hartsuck, F. A. Quiocho, and P. H. Bethge. 1970. The structure of carboxypeptidase A. VIII. Atomic interaction at 0.2 nm resolution, a new study of the complex of glycyltyrosine with CPA, and mechanistic deductions. Phil. Trans. R. Soc. Lond. B. 257:177-214.
    • (1970) Phil. Trans. R. Soc. Lond. B , vol.257 , pp. 177-214
    • Lipscomb, W.N.1    Reeke, G.N.2    Hartsuck, J.A.3    Quiocho, F.A.4    Bethge, P.H.5
  • 12
    • 0038841788 scopus 로고
    • The crystal structure of and hydrogen bond in potassium hydrogen bisphenylacetate: A redetermination
    • Manojlovic, L., and J. C. Speakman. 1968. The crystal structure of and hydrogen bond in potassium hydrogen bisphenylacetate: a redetermination. Acta Crystallogr. B24:323-325.
    • (1968) Acta Crystallogr. , vol.B24 , pp. 323-325
    • Manojlovic, L.1    Speakman, J.C.2
  • 13
    • 84985721981 scopus 로고
    • Dynamics of tyrosine ring rotations in a globular protein
    • McCammon, J. A., and M. Karplus. 1980. Dynamics of tyrosine ring rotations in a globular protein. Biopolymers. 19:1375-1405.
    • (1980) Biopolymers , vol.19 , pp. 1375-1405
    • McCammon, J.A.1    Karplus, M.2
  • 14
    • 0018796418 scopus 로고
    • Picosecond dynamics of tyrosine side chains in proteins
    • McCammon, J. A., P. G. Wolynes, and M. Karplus. 1979. Picosecond dynamics of tyrosine side chains in proteins. Biochemistry. 18:927-924.
    • (1979) Biochemistry , vol.18 , pp. 927-1924
    • McCammon, J.A.1    Wolynes, P.G.2    Karplus, M.3
  • 15
    • 0006284451 scopus 로고
    • The conversion of phenylalanine to tyrosine in normal rats
    • Moss, A. R., and R. Schoenheimer. 1940. The conversion of phenylalanine to tyrosine in normal rats. J. Biol. Chem. 135:415-429.
    • (1940) J. Biol. Chem. , vol.135 , pp. 415-429
    • Moss, A.R.1    Schoenheimer, R.2
  • 16
    • 0028111532 scopus 로고
    • Catalytic conformation of carboxypeptidase A, structure of a true enzyme reaction intermediate determined by electron-nuclear double resonance
    • Mustafi, D., and M. W. Makinen. 1994. Catalytic conformation of carboxypeptidase A, structure of a true enzyme reaction intermediate determined by electron-nuclear double resonance. J. Biol. Chem. 269: 4587-4595.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4587-4595
    • Mustafi, D.1    Makinen, M.W.2
  • 17
    • 0025931861 scopus 로고
    • Conformational flexibility and protein specificity
    • D. J. Chadwick and K. Widdows, editors. Wiley Interscience Publications, New York
    • Roberts, G. C. K. 1991. Conformational flexibility and protein specificity. In Host-Guest Molecular Interaction, from Chemistry to Biology. D. J. Chadwick and K. Widdows, editors. Wiley Interscience Publications, New York. 169-186.
    • (1991) Host-Guest Molecular Interaction, from Chemistry to Biology , pp. 169-186
    • Roberts, G.C.K.1
  • 18
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost, B., and C. Sande. 1994. Conservation and prediction of solvent accessibility in protein families. Protein Struct. Funct. Genet. 20:216-226.
    • (1994) Protein Struct. Funct. Genet. , vol.20 , pp. 216-226
    • Rost, B.1    Sande, C.2
  • 19
    • 0001571760 scopus 로고
    • Phenylene ring dynamics in solid polycarbonate: An extensive probe by carbon-13 solid state NMR line-shape studies at two field strengths
    • Roy, A. K., A. A. Jones, and P. T. Inglefield. 1986. Phenylene ring dynamics in solid polycarbonate: an extensive probe by carbon-13 solid state NMR line-shape studies at two field strengths. Macromolecules. 19:1356-1362.
    • (1986) Macromolecules , vol.19 , pp. 1356-1362
    • Roy, A.K.1    Jones, A.A.2    Inglefield, P.T.3
  • 20
    • 0025877453 scopus 로고
    • Protein hydration and function
    • Rupley, J. A., and G. Careri. 1991. Protein hydration and function. Adv. Protein Chem. 41:37-172.
    • (1991) Adv. Protein Chem. , vol.41 , pp. 37-172
    • Rupley, J.A.1    Careri, G.2
  • 21
    • 0025464741 scopus 로고
    • Two-dimensional solid-state NMR studies of ultraslow chain motion: Glass transition in atactic poly(propylene) versus helical jumps in isotactic poly(propylene)
    • Schafer, D., H. W. Spiess, U. W. Suter, and W. W. Fleming. 1990. Two-dimensional solid-state NMR studies of ultraslow chain motion: glass transition in atactic poly(propylene) versus helical jumps in isotactic poly(propylene). Macromolecule. 23:3431-3439.
    • (1990) Macromolecule , vol.23 , pp. 3431-3439
    • Schafer, D.1    Spiess, H.W.2    Suter, U.W.3    Fleming, W.W.4
  • 22
    • 46149139090 scopus 로고
    • Dynamics of molecular reorientations: Direct determination of rotational angles from two-dimensional NMR of powders
    • Schmidt, C., S. Wefing, B. Blümich, and H. W. Spiess. 1986. Dynamics of molecular reorientations: direct determination of rotational angles from two-dimensional NMR of powders. Chem. Phys. Lett. 130:84-90.
    • (1986) Chem. Phys. Lett. , vol.130 , pp. 84-90
    • Schmidt, C.1    Wefing, S.2    Blümich, B.3    Spiess, H.W.4
  • 23
    • 45449122556 scopus 로고
    • Deuteron two-dimensional exchange NMR in solids
    • Schmidt, C., B. Blümich, and H. W. Spiess. 1988. Deuteron two-dimensional exchange NMR in solids. J. Magn. Reson. 79:269-290.
    • (1988) J. Magn. Reson. , vol.79 , pp. 269-290
    • Schmidt, C.1    Blümich, B.2    Spiess, H.W.3
  • 24
    • 0021767539 scopus 로고
    • Dynamic structure of membranes by deuterium NMR
    • Smith, R. L., and E. Oldfield. 1984. Dynamic structure of membranes by deuterium NMR. Science. 225:280-288.
    • (1984) Science , vol.225 , pp. 280-288
    • Smith, R.L.1    Oldfield, E.2
  • 25
    • 0010776167 scopus 로고
    • Solid echoes in the slow-motion region
    • Spiess, H. W., and H. Sillescu. 1981. Solid echoes in the slow-motion region. J. Magn. Reson. 42:381-389.
    • (1981) J. Magn. Reson. , vol.42 , pp. 381-389
    • Spiess, H.W.1    Sillescu, H.2
  • 26
    • 0002424797 scopus 로고
    • Deuteron NMR - A new tool for studying chain mobility and orientation in polymers
    • Spiess, H. W. 1985. Deuteron NMR - a new tool for studying chain mobility and orientation in polymers. Adv. Polym. Sci. 66:24-58.
    • (1985) Adv. Polym. Sci. , vol.66 , pp. 24-58
    • Spiess, H.W.1
  • 27
    • 0001187383 scopus 로고
    • Structure and dynamics of solid polymers from 2D-and 3D-NMR
    • Spiess, H. W. 1991. Structure and dynamics of solid polymers from 2D-and 3D-NMR. Chem. Rev. 91:1321-1338.
    • (1991) Chem. Rev. , vol.91 , pp. 1321-1338
    • Spiess, H.W.1
  • 28
    • 0014217198 scopus 로고
    • The structure of carboxypeptidase A. V. Studies of enzyme-substrate and enzyme-inhibitor complexes at 6 Å resolution
    • Steitz, T. A., M. L. Ludwig, F. A. Quiocho, and W. N. Lipscomb. 1967. The structure of carboxypeptidase A. V. Studies of enzyme-substrate and enzyme-inhibitor complexes at 6 Å resolution. J. Biol. Chem. 242:4662-4667.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4662-4667
    • Steitz, T.A.1    Ludwig, M.L.2    Quiocho, F.A.3    Lipscomb, W.N.4
  • 29
    • 49049140501 scopus 로고
    • Spin-lattice relaxation in solids
    • Torchia, D. A., and A. Szabo. 1982. Spin-lattice relaxation in solids. J. Magn. Reson. 49:107-121.
    • (1982) J. Magn. Reson. , vol.49 , pp. 107-121
    • Torchia, D.A.1    Szabo, A.2
  • 30
    • 84939988155 scopus 로고
    • Deuterium relaxation in molecular solids
    • Void, R. R., and R. L. Void. 1991. Deuterium relaxation in molecular solids. Adv. Magn. Opt. Reson. 16:85-169.
    • (1991) Adv. Magn. Opt. Reson. , vol.16 , pp. 85-169
    • Void, R.R.1    Void, R.L.2
  • 31
    • 36549103659 scopus 로고
    • Two-dimensional exchange NMR of powder samples. II. the dynamic evolution of two-time distribution functions
    • Wefing, S., S. Kaufmann, and H. W. Spiess. 1989. Two-dimensional exchange NMR of powder samples. II. The dynamic evolution of two-time distribution functions. J. Chem. Phys. 89:1234-1244.
    • (1989) J. Chem. Phys. , vol.89 , pp. 1234-1244
    • Wefing, S.1    Kaufmann, S.2    Spiess, H.W.3
  • 32
    • 36549101089 scopus 로고
    • Two-dimensional exchange NMR of powder samples. I. Two-time distribution functions
    • Wefing, S., and H. W. Spiess. 1989. Two-dimensional exchange NMR of powder samples. I. Two-time distribution functions. J. Chem. Phys. 89:1219-1233.
    • (1989) J. Chem. Phys. , vol.89 , pp. 1219-1233
    • Wefing, S.1    Spiess, H.W.2
  • 33
    • 36549103176 scopus 로고
    • Analysis of deuterium nuclear magnetic resonance line shapes in an isotropic media
    • Wittebort, R. J., E. T. Olejniczak, and R. G. Griffin. 1987. Analysis of deuterium nuclear magnetic resonance line shapes in an isotropic media. J. Chem. Phys. 86:5411-5420.
    • (1987) J. Chem. Phys. , vol.86 , pp. 5411-5420
    • Wittebort, R.J.1    Olejniczak, E.T.2    Griffin, R.G.3
  • 34
    • 84995104190 scopus 로고
    • X-ray crystallographic study of covalently modified carboxypeptidase a by 2-benzyl-3,4-epoxybutanoic acid, a pseudomechanism-based inactivator
    • Yun, M., C. Park, S. Kim, D. Nam, and S. C. Kim. 1992. X-ray crystallographic study of covalently modified carboxypeptidase A by 2-benzyl-3,4-epoxybutanoic acid, a pseudomechanism-based inactivator. J. Am. Chem. Soc. 114:2281-2282.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 2281-2282
    • Yun, M.1    Park, C.2    Kim, S.3    Nam, D.4    Kim, S.C.5
  • 35
    • 0028821356 scopus 로고
    • Characterization of enzyme-bound ligand dynamics by solid-state NMR in the presence of ligand exchange: L-phenylalanine on carboxypeptidase A
    • Zhang, H., and R. G. Bryant. 1995. Characterization of enzyme-bound ligand dynamics by solid-state NMR in the presence of ligand exchange: L-phenylalanine on carboxypeptidase A. Biophys. J. 68: 303-311.
    • (1995) Biophys. J. , vol.68 , pp. 303-311
    • Zhang, H.1    Bryant, R.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.