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Volumn 8, Issue 6, 1999, Pages 1342-1349

The crystal structure of a bacterial, bifunctional 5,10 methylene- tetrahydrofolate dehydrogenase/cyclohydrolase

Author keywords

Bifunctional; Channeling; Cyclohydrolase; Dehydrogenase; Folate

Indexed keywords

BACTERIAL ENZYME; METHYLENETETRAHYDROFOLATE DEHYDROGENASE;

EID: 0033060317     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.6.1342     Document Type: Article
Times cited : (30)

References (37)
  • 1
    • 0032520234 scopus 로고    scopus 로고
    • The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 Å resolution
    • Allaire M, Li Y, MacKenzie RE, Cygler M. 1998. The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 Å resolution. Structure 6:173-182.
    • (1998) Structure , vol.6 , pp. 173-182
    • Allaire, M.1    Li, Y.2    MacKenzie, R.E.3    Cygler, M.4
  • 2
    • 0021867079 scopus 로고
    • Evidence for overlapping active sites in a multifunctional enzyme: Immunochemical and chemical modification studies on C1-tetrahydrofolate synthase from Saccharomyces cerevisiae
    • Appling DR, Rabinowitz JC. 1985. Evidence for overlapping active sites in a multifunctional enzyme: Immunochemical and chemical modification studies on C1-tetrahydrofolate synthase from Saccharomyces cerevisiae. Biochemistry 24:3540-3547.
    • (1985) Biochemistry , vol.24 , pp. 3540-3547
    • Appling, D.R.1    Rabinowitz, J.C.2
  • 3
    • 9444228785 scopus 로고    scopus 로고
    • Folic acid and the prevention of birth defects
    • Bendich A, Butterworth CEJ. 1996. Folic acid and the prevention of birth defects. Ann Rev Nutr 16:73-97.
    • (1996) Ann Rev Nutr , vol.16 , pp. 73-97
    • Bendich, A.1    Butterworth, C.E.J.2
  • 4
    • 0041059328 scopus 로고
    • On the mechanisms of action of folic acid cofactors
    • Benkovic SJ, Bullard WP. 1973. On the mechanisms of action of folic acid cofactors. Prog Bior Chem 2:133-175.
    • (1973) Prog Bior Chem , vol.2 , pp. 133-175
    • Benkovic, S.J.1    Bullard, W.P.2
  • 5
    • 0003830834 scopus 로고
    • Biochemistry of folic acid and related pteridines
    • Bloch K, ed. New York: Wiley and Sons
    • Blakeley R. 1969. Biochemistry of folic acid and related pteridines. In: Bloch K, ed. Accounts of chemical research. New York: Wiley and Sons. pp 191-237.
    • (1969) Accounts of Chemical Research , pp. 191-237
    • Blakeley, R.1
  • 7
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value. Methods and applications
    • Brünger A. 1993. Assessment of phase accuracy by cross validation: The free R value. Methods and applications. Acta Cryst D49:24-36.
    • (1993) Acta Cryst , vol.D49 , pp. 24-36
    • Brünger, A.1
  • 8
    • 0031054848 scopus 로고    scopus 로고
    • Purification, crystallization, and preliminary X-ray studies of a bifunctional 5,10-methenyl/methylene tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli
    • Cheung E, D'Ari L, Rabinowitz JC, Dyer DH, Huang J-Y, Stoddard BL. 1997. Purification, crystallization, and preliminary X-ray studies of a bifunctional 5,10-methenyl/methylene tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli. Proteins Struct Funct Genet 27:322-324.
    • (1997) Proteins Struct Funct Genet , vol.27 , pp. 322-324
    • Cheung, E.1    D'Ari, L.2    Rabinowitz, J.C.3    Dyer, D.H.4    Huang, J.-Y.5    Stoddard, B.L.6
  • 9
    • 0017796796 scopus 로고
    • Methylenetetrahydrofolate-dehydrogenase/ methenyltetrahydro-folate cyclohydrolase/formyltetrahydrofolate synthetase from porcine liver. Interaction between the dehydrogenase and cyclohydrolase activities of the multifunctional enzyme
    • Cohen L, MacKenzie RE. 1978. Methylenetetrahydrofolate-dehydrogenase/ methenyltetrahydro-folate cyclohydrolase/formyltetrahydrofolate synthetase from porcine liver. Interaction between the dehydrogenase and cyclohydrolase activities of the multifunctional enzyme. Biochim Biophys Acta 522:311-317.
    • (1978) Biochim Biophys Acta , vol.522 , pp. 311-317
    • Cohen, L.1    MacKenzie, R.E.2
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project 4. 1994. The CCP4 Suite: Programs for protein crystallography. Acta Cryst D 50:760-763.
    • (1994) Acta Cryst D , vol.50 , pp. 760-763
  • 11
    • 0002583957 scopus 로고
    • An automated procedure for phase improvement by density modification
    • Cowtan K. 1994. An automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newslett Protein Crystallogr 31:34-38.
    • (1994) Joint CCP4 and ESF-EACBM Newslett Protein Crystallogr , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 12
    • 0026325733 scopus 로고
    • Purification, characterization, clining, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from E. Coli
    • D'Ari L, Rabinowitz J. 1991. Purification, characterization, clining, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from E. coli. J Biol Chem 266:23953-23958.
    • (1991) J Biol Chem , vol.266 , pp. 23953-23958
    • D'Ari, L.1    Rabinowitz, J.2
  • 13
    • 0021089250 scopus 로고
    • Methenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase from porcine liver: Evidence to support a common dehydrogenase/cyclohydrolase site
    • Drummond D, Smith S, MacKenzie RE. 1983. Methenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase from porcine liver: Evidence to support a common dehydrogenase/cyclohydrolase site. Can J Biochem Cell Biol 61:1166-1171.
    • (1983) Can J Biochem Cell Biol , vol.61 , pp. 1166-1171
    • Drummond, D.1    Smith, S.2    MacKenzie, R.E.3
  • 15
    • 0023815995 scopus 로고
    • Substrate flux through methylenetetrahydrofolate dehydrogenase: Predicted effects of the concentration of methylenetetrahydrofolate on its partitioning into pathways leading to nucleotide biosynthesis or methionine regeneration
    • Green JM, Mackenzie RE, Matthews RG. 1988. Substrate flux through methylenetetrahydrofolate dehydrogenase: Predicted effects of the concentration of methylenetetrahydrofolate on its partitioning into pathways leading to nucleotide biosynthesis or methionine regeneration. Biochemistry 27:8014-8022.
    • (1988) Biochemistry , vol.27 , pp. 8014-8022
    • Green, J.M.1    Mackenzie, R.E.2    Matthews, R.G.3
  • 16
    • 0345660926 scopus 로고
    • Stereochemistry of hydride transfer to NADP+ by methylenetetrahydrofolate dehydrogenase from pig liver
    • Cooper BA, Whitehead VM, eds. Berlin: Walter de Gruyter and Co.
    • Green JM, Matthews RG, Mackenzie RE. 1986. Stereochemistry of hydride transfer to NADP+ by methylenetetrahydrofolate dehydrogenase from pig liver. In: Cooper BA, Whitehead VM, eds. Chemistry and biology of pteridines. Berlin: Walter de Gruyter and Co. pp 901-904.
    • (1986) Chemistry and Biology of Pteridines , pp. 901-904
    • Green, J.M.1    Matthews, R.G.2    Mackenzie, R.E.3
  • 17
    • 0025761155 scopus 로고
    • Expression of active domains of a human folate-dependent trifunctional enzyme in E. Coli
    • Hum DW, MacKenzie RE. 1991. Expression of active domains of a human folate-dependent trifunctional enzyme in E. coli. Protein Eng 4:493-500.
    • (1991) Protein Eng , vol.4 , pp. 493-500
    • Hum, D.W.1    MacKenzie, R.E.2
  • 18
    • 0031821779 scopus 로고    scopus 로고
    • Homocysteine and vitamins in cardiovascular disease
    • Jacobsen DW. 1998. Homocysteine and vitamins in cardiovascular disease. Clinical Chem 44:1833-1843.
    • (1998) Clinical Chem , vol.44 , pp. 1833-1843
    • Jacobsen, D.W.1
  • 19
    • 0030841587 scopus 로고    scopus 로고
    • Electron density map interpretation
    • Jones TA, Kjeldgaard MO. 1998. Electron density map interpretation. Methods Enzymol 277:173-208.
    • (1998) Methods Enzymol , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.O.2
  • 20
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowtan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A 47:110-119.
    • (1991) Acta Cryst A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowtan, S.W.3    Kjeldgaard, M.4
  • 21
    • 0027102178 scopus 로고
    • Cofactor triggers the conformational change in thymidylate synthase: Implications for an ordered binding mechanism
    • Kamb A, Finer-Moore JS, Stroud RM. 1992. Cofactor triggers the conformational change in thymidylate synthase: Implications for an ordered binding mechanism. Biochemistry 31:12876-12884.
    • (1992) Biochemistry , vol.31 , pp. 12876-12884
    • Kamb, A.1    Finer-Moore, J.S.2    Stroud, R.M.3
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24:946-950.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0003292939 scopus 로고    scopus 로고
    • SHARP: A maximum-likelihood heavy-atom parameter refinement and phasing program for the MIR and MAD methods
    • Bourne P, Watenpaugh K, eds. Oxford: Oxford Science Publications
    • LaFortelle E, Irwin JJ, Bricogne G. 1997. SHARP: A maximum-likelihood heavy-atom parameter refinement and phasing program for the MIR and MAD methods. In: Bourne P, Watenpaugh K, eds. Crystallographic computing. Oxford: Oxford Science Publications, pp 100-130.
    • (1997) Crystallographic Computing , pp. 100-130
    • LaFortelle, E.1    Irwin, J.J.2    Bricogne, G.3
  • 25
    • 0001042638 scopus 로고
    • Biogenesis and interconversion of substituted tetrahydrofolates
    • Blakeley R, Benkovic S, eds. New York: Wiley and Sons
    • MacKenzie RE. 1984. Biogenesis and interconversion of substituted tetrahydrofolates. In: Blakeley R, Benkovic S, eds. Folates and pterins: Chemistry and biochemistry of folates. New York: Wiley and Sons. pp 255-306.
    • (1984) Folates and Pterins: Chemistry and Biochemistry of Folates , pp. 255-306
    • MacKenzie, R.E.1
  • 26
    • 0025091668 scopus 로고
    • Stereochemical mechanism of action for thymidylate synthase based on the X-ray structure of the covalent inhibitory ternary complex with 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolate
    • Matthews DA, Villafranca JE, Janson CA, Smith WW, Welsh K, Freer S. 1990. Stereochemical mechanism of action for thymidylate synthase based on the X-ray structure of the covalent inhibitory ternary complex with 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolate. J Mol Biol 214:937-948.
    • (1990) J Mol Biol , vol.214 , pp. 937-948
    • Matthews, D.A.1    Villafranca, J.E.2    Janson, C.A.3    Smith, W.W.4    Welsh, K.5    Freer, S.6
  • 27
    • 84986432941 scopus 로고
    • Automated docking with grid-based energy evaluation
    • Meng EC, Shoichet B, Kuntz ID. 1992. Automated docking with grid-based energy evaluation. J Comp Chem 13:505-524.
    • (1992) J Comp Chem , vol.13 , pp. 505-524
    • Meng, E.C.1    Shoichet, B.2    Kuntz, I.D.3
  • 29
    • 0016283234 scopus 로고
    • Structural and functional similarities within the coenzyme binding domains of dehydrogenases
    • Ohlsson I, Nordstrom B, Branden C-I. 1974. Structural and functional similarities within the coenzyme binding domains of dehydrogenases. J Mol Biol 89:339-354.
    • (1974) J Mol Biol , vol.89 , pp. 339-354
    • Ohlsson, I.1    Nordstrom, B.2    Branden, C.-I.3
  • 30
    • 0029283717 scopus 로고
    • Flexible ligand docking using a genetic algorithm
    • Oshiro CM, Kuntz ID. 1995. Flexible ligand docking using a genetic algorithm. J Comp-Aided Mol Design 9:113-130.
    • (1995) J Comp-aided Mol Design , vol.9 , pp. 113-130
    • Oshiro, C.M.1    Kuntz, I.D.2
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, 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
  • 32
    • 0032570311 scopus 로고    scopus 로고
    • Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes
    • Pawelek PD, MacKenzie RE. 1998. Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes. Biochemistry 37:1109-1115.
    • (1998) Biochemistry , vol.37 , pp. 1109-1115
    • Pawelek, P.D.1    MacKenzie, R.E.2
  • 33
    • 0028783622 scopus 로고
    • Binding and interconversion of tetrahydrofolates at a single site in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
    • Pelletier JN, MacKenzie RE. 1995. Binding and interconversion of tetrahydrofolates at a single site in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase. Biochemistry 34:12673-12680.
    • (1995) Biochemistry , vol.34 , pp. 12673-12680
    • Pelletier, J.N.1    MacKenzie, R.E.2
  • 34
    • 0017871553 scopus 로고
    • Formyl-methenyl-methylenetetrahydrofolate synthetase from rabbit liver (combined). Evidence for a single site in the conversion of 5,10-methylenetetrahydrofolate to 10-formyltetrahydrofolate
    • Schirch L. 1978. Formyl-methenyl-methylenetetrahydrofolate synthetase from rabbit liver (combined). Evidence for a single site in the conversion of 5,10-methylenetetrahydrofolate to 10-formyltetrahydrofolate. Arch Biochem Biophys 189:283-290.
    • (1978) Arch Biochem Biophys , vol.189 , pp. 283-290
    • Schirch, L.1
  • 35
    • 0028864002 scopus 로고
    • The N-terminal, dehydrogenase/cyclohydrolase domain of yeast cytoplasmic trifunctional C1-synthase requires the C-terminal, synthetase domain for the catalytic activity in vitro
    • Song JM, Rabinowitz JC. 1995. The N-terminal, dehydrogenase/cyclohydrolase domain of yeast cytoplasmic trifunctional C1-synthase requires the C-terminal, synthetase domain for the catalytic activity in vitro. FEBS Lett 376:229-232.
    • (1995) FEBS Lett , vol.376 , pp. 229-232
    • Song, J.M.1    Rabinowitz, J.C.2
  • 36
    • 0020724291 scopus 로고
    • Kinetic relationships between the various activities of the formyl/methenyl/methylenetetrahydrofolate synthetase
    • Wasserman GF, Benkovic PA, Young M, Benkovic SJ. 1983. Kinetic relationships between the various activities of the formyl/methenyl/methylenetetrahydrofolate synthetase. Biochemistry 22:1005-1013.
    • (1983) Biochemistry , vol.22 , pp. 1005-1013
    • Wasserman, G.F.1    Benkovic, P.A.2    Young, M.3    Benkovic, S.J.4
  • 37
    • 0027530611 scopus 로고
    • Cloning and characterization of the Saccharomyces cerevisiae gene encoding NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase
    • West MG, Barlowe CK, Appling DR. 1993. Cloning and characterization of the Saccharomyces cerevisiae gene encoding NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase. J Biol Chem 268:153-160.
    • (1993) J Biol Chem , vol.268 , pp. 153-160
    • West, M.G.1    Barlowe, C.K.2    Appling, D.R.3


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