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Volumn 3, Issue 1, 1999, Pages 23-32

Melatonin biosynthesis: The structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A; MELATONIN; N ACETYLSEROTONIN; SEROTONIN; SEROTONIN N ACETYLTRANSFERASE;

EID: 0033010021     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80171-9     Document Type: Article
Times cited : (121)

References (40)
  • 1
    • 0032510767 scopus 로고    scopus 로고
    • Structure of the hexapeptide xenobiotic acetyltransferase from Pseudomonas aeruginosa
    • Beaman, T.W., Sugantino, M., and Roderick, S.L. (1998). Structure of the hexapeptide xenobiotic acetyltransferase from Pseudomonas aeruginosa. Biochemistry 37, 6688-6696.
    • (1998) Biochemistry , vol.37 , pp. 6688-6696
    • Beaman, T.W.1    Sugantino, M.2    Roderick, S.L.3
  • 2
    • 0031738168 scopus 로고    scopus 로고
    • Transcripts encoding two melatonin synthesis enzymes in the teleost pineal organ: Circadian regulation in pike and zebrafish, but not in trout
    • Bégay, V., Falcon, J., Cahill, G.M., Klein, D.C., and Coon, S.L. (1998). Transcripts encoding two melatonin synthesis enzymes in the teleost pineal organ: Circadian regulation in pike and zebrafish, but not in trout. Endocrinology 139, 905-912.
    • (1998) Endocrinology , vol.139 , pp. 905-912
    • Bégay, V.1    Falcon, J.2    Cahill, G.M.3    Klein, D.C.4    Coon, S.L.5
  • 4
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992b). Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 6
    • 0026240806 scopus 로고
    • Ribbons 2.0
    • Carson, M. (1991). Ribbons 2.0. J. Appl. Cryst. 24, 958-961.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 958-961
    • Carson, M.1
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994). The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 10
    • 0032579377 scopus 로고    scopus 로고
    • Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87)
    • De Angelis, J., Gastel, J., Klein, D.C., and Cole, P.A. (1998). Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87). J. Biol. Chem. 273, 3045-3050.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3045-3050
    • De Angelis, J.1    Gastel, J.2    Klein, D.C.3    Cole, P.A.4
  • 11
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle, E., and Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 12
    • 0016681192 scopus 로고
    • Characteristics of serotonin-acetyl coenzyme AN-acetyltransferase in pineal gland of rat
    • Deguchi, T. (1975). Characteristics of serotonin-acetyl coenzyme AN-acetyltransferase in pineal gland of rat. J. Neurochem. 24, 1083-1085.
    • (1975) J. Neurochem. , vol.24 , pp. 1083-1085
    • Deguchi, T.1
  • 13
    • 0002864734 scopus 로고
    • Preparation of selenomethionyl protein crystals
    • A. Ducruix and R. Giegé, eds. (New York: Oxford University Press)
    • Doublié, S., and Carter, C.W., Jr. (1992). Preparation of selenomethionyl protein crystals. In Crystallization Of Nucleic Acids and Proteins, A. Ducruix and R. Giegé, eds. (New York: Oxford University Press), pp. 311-317.
    • (1992) Crystallization of Nucleic Acids and Proteins , pp. 311-317
    • Doublié, S.1    Carter C.W., Jr.2
  • 14
    • 0032555689 scopus 로고    scopus 로고
    • Structure of the histone acetyltransferase Hat1: A paradigm for the GCN5-related N-acetyltransferase superfamily
    • Dutnall, R.N., Tafrov, S.T., Sternglanz, R., and Ramakrishnan, V. (1998). Structure of the histone acetyltransferase Hat1: A paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 94, 427-438.
    • (1998) Cell , vol.94 , pp. 427-438
    • Dutnall, R.N.1    Tafrov, S.T.2    Sternglanz, R.3    Ramakrishnan, V.4
  • 15
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for processing and analyzing diffraction data from macromolecules
    • Furey, W., and Swaminathan, S. (1997). PHASES-95: A program package for processing and analyzing diffraction data from macromolecules. Methods Enzymol. 277, 590-620.
    • (1997) Methods Enzymol. , vol.277 , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 16
    • 0032570593 scopus 로고    scopus 로고
    • Melatonin production: Proteasomal proteolysis in serotonin N-acetyltransferase regulation
    • Gastel, J.A., Roseboom, P.H., Rinaldi, P.A., Weller, J.L., and Klein, D.C. (1998). Melatonin production: Proteasomal proteolysis in serotonin N-acetyltransferase regulation. Science 279, 1358-1360.
    • (1998) Science , vol.279 , pp. 1358-1360
    • Gastel, J.A.1    Roseboom, P.H.2    Rinaldi, P.A.3    Weller, J.L.4    Klein, D.C.5
  • 17
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W.A. (1991). Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and 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
  • 19
    • 0032514895 scopus 로고    scopus 로고
    • Indoleamine analogs as probes of the substrate specificity and catalytic mechanism of serotonin-N-acetyltransferase
    • Khalil, E.M., De Angelis, J., and Cole, P.A. (1998). Indoleamine analogs as probes of the substrate specificity and catalytic mechanism of serotonin-N-acetyltransferase. J. Biol. Chem. 273, 30321-30327.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30321-30327
    • Khalil, E.M.1    De Angelis, J.A.2    Cole, P.A.3
  • 20
    • 0015502984 scopus 로고
    • Rapid light induced decrease in pineal serotonin N-acetyltransferase activity
    • Klein, D.C., and Weller, J.L. (1972). Rapid light induced decrease in pineal serotonin N-acetyltransferase activity. Science 177, 532-533.
    • (1972) Science , vol.177 , pp. 532-533
    • Klein, D.C.1    Weller, J.L.2
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0025335792 scopus 로고
    • Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 Å resolution
    • Leslie, A.G.W. (1990). Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 Å resolution. J. Mol. Biol. 213, 167-186.
    • (1990) J. Mol. Biol. , vol.213 , pp. 167-186
    • Leslie, A.G.W.1
  • 24
    • 0029763523 scopus 로고    scopus 로고
    • RGFGIGS is an amino acid sequence required for acetyl coenzyme A binding and activity of human spermidine/spermine N1 acetyltransferase
    • Lu, L., Berkey, K.A., and Casero, R.A., Jr. (1996). RGFGIGS is an amino acid sequence required for acetyl coenzyme A binding and activity of human spermidine/spermine N1 acetyltransferase. J. Biol. Chem. 271, 18920-18924.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18920-18924
    • Lu, L.1    Berkey, K.A.2    Casero R.A., Jr.3
  • 25
    • 0027157439 scopus 로고
    • Refined crystal structure of the catalytic domain of dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii at 2.6 Å resolution
    • Mattevi, A., Obmolova, G., Kalk, K.H., Westphal, A.H., de Kok, A., and Hol, W.G.J. (1993). Refined crystal structure of the catalytic domain of dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii at 2.6 Å resolution. J. Mol. Biol. 230, 1183-1199.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1183-1199
    • Mattevi, A.1    Obmolova, G.2    Kalk, K.H.3    Westphal, A.H.4    De Kok, A.A.5    Hol, W.G.J.6
  • 26
    • 0030954208 scopus 로고    scopus 로고
    • GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein
    • Neuwald, A.F., and Landsman, D. (1997). Gcn5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 22, 154-155.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 0030799033 scopus 로고    scopus 로고
    • Melatonin: A clinical perspective
    • Penev, P.D., and Zee, P.C. (1997). Melatonin: A clinical perspective. Ann. Neurol. 42, 545-553.
    • (1997) Ann. Neurol. , vol.42 , pp. 545-553
    • Penev, P.D.1    Zee, P.C.2
  • 30
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan, V., Finch, J.T., Graziano, V., Lee, P.L., and Sweet, R.M. (1993). Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 362, 219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 31
    • 77956909282 scopus 로고
    • Bovine pancreatic ribonuclease
    • P.D. Boyer, ed. (New York: Academic Press)
    • Richards, F.M., and Wyckoff, H. (1971). Bovine pancreatic ribonuclease. In The Enzymes, Vol. 4, P.D. Boyer, ed. (New York: Academic Press), pp. 647-806.
    • (1971) The Enzymes , vol.4 , pp. 647-806
    • Richards, F.M.1    Wyckoff, H.2
  • 32
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J.S. (1981). The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34, 167-330.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-330
    • Richardson, J.S.1
  • 33
    • 0029894818 scopus 로고    scopus 로고
    • Melatonin synthesis: Analysis of the more than 150-fold nocturnal increase in serotonin N-acetyltransferase messenger ribonucleic acid in the rat pineal gland
    • Roseboom, P.H., Coon, S.L., Baler, R., McCune, S.K., Weller, J.L., and Klein, D.C. (1996). Melatonin synthesis: Analysis of the more than 150-fold nocturnal increase in serotonin N-acetyltransferase messenger ribonucleic acid in the rat pineal gland. Encocrinol. 137, 3033-3044.
    • (1996) Encocrinol. , vol.137 , pp. 3033-3044
    • Roseboom, P.H.1    Coon, S.L.2    Baler, R.3    McCune, S.K.4    Weller, J.L.5    Klein, D.C.6
  • 34
    • 0026730661 scopus 로고
    • Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae
    • Tercero, J.C., Riles, L.E., and Wickner, R.B. (1992). Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae. J. Biol. Chem. 267, 20270-20276.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20270-20276
    • Tercero, J.C.1    Riles, L.E.2    Wickner, R.B.3
  • 35
    • 0002889108 scopus 로고
    • MAD Phasing: Bayesian Estimates of Fa
    • Terwilliger, T.C. (1994a). MAD Phasing: Bayesian Estimates of Fa. Acta Crystallogr. D 50, 11-16.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 11-16
    • Terwilliger, T.C.1
  • 36
    • 0001940082 scopus 로고
    • MAD phasing: Treatment of dispersive differences as isomorphous replacement information
    • Terwilliger, T.C. (1994b). MAD phasing: Treatment of dispersive differences as isomorphous replacement information. Acta Crystallogr. D 50, 17-23.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 17-23
    • Terwilliger, T.C.1
  • 37
    • 0002518563 scopus 로고    scopus 로고
    • Knowledge-based B-factor restraints for the refinement of proteins
    • Tronrud, D.E. (1996). Knowledge-based B-factor restraints for the refinement of proteins. J. Appl. Cryst. 29, 100-104.
    • (1996) J. Appl. Cryst. , vol.29 , pp. 100-104
    • Tronrud, D.E.1
  • 38
    • 0022325950 scopus 로고
    • Resolution of phase ambiguity in macromolecular crystallography
    • Wang, B.C. (1985). Resolution of phase ambiguity in macromolecular crystallography. Methods Enzymol. 115, 90-112.
    • (1985) Methods Enzymol. , vol.115 , pp. 90-112
    • Wang, B.C.1
  • 39
    • 0026611267 scopus 로고
    • Involvement of Cys69 residue in the catalytic mechanism of N-hydroxyarylamine O-acetylsr transferase of Salmonella typhimurium
    • Watanabe, M., Sofuni, T., and Nohmi, T. (1992). Involvement of Cys69 residue in the catalytic mechanism of N-hydroxyarylamine O-acetylsr transferase of Salmonella typhimurium. J. Biol. Chem. 267, 8429-8436.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8429-8436
    • Watanabe, M.1    Sofuni, T.2    Nohmi, T.3
  • 40
    • 0032555691 scopus 로고    scopus 로고
    • Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase
    • Wolf, E., Vassilev, A., Makino, Y., Sali, A., Nakatani, Y., and Burley, S.K. (1998). Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase. Cell 94, 439-449.
    • (1998) Cell , vol.94 , pp. 439-449
    • Wolf, E.1    Vassilev, A.2    Makino, Y.3    Sali, A.4    Nakatani, Y.5    Burley, S.K.6


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