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Volumn 269, Issue 21, 2002, Pages 5264-5270

Biosynthesis of vitamin B2. An essential zinc ion at the catalytic site of GTP cyclohydrolase II

Author keywords

Formate; GTP cyclohydrolase; Imidazole ring; Pyrophosphate; Zinc ion

Indexed keywords

2 AMINO 5 FORMYLAMINO 6 RIBOSYLAMINO 4(3H) PYRIMIDINONE 5' TRIPHOSPHATE; 2,5 DIAMINO 6 RIBOSYLAMINO 4(3H) PYRIMIDONE 5' PHOSPHATE; CYANOCOBALAMIN; CYSTEINE; FORMIC ACID; GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE II; GUANOSINE TRIPHOSPHATE DERIVATIVE; MUTANT PROTEIN; PROTEIN SUBUNIT; PYROPHOSPHATE; RIBOFLAVIN; SERINE; UNCLASSIFIED DRUG; ZINC ION; DEOXYGUANOSINE PHOSPHATE; DEOXYGUANOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE I; ZINC;

EID: 0036832419     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03239.x     Document Type: Article
Times cited : (42)

References (29)
  • 1
    • 0014409033 scopus 로고
    • The biosynthesis of folic acid. VIII. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate
    • Burg, A.W. & Brown, G.M. (1968) The biosynthesis of folic acid. VIII. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate. J. Biol. Chem. 243, 2349-2358.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2349-2358
    • Burg, A.W.1    Brown, G.M.2
  • 2
    • 0013817679 scopus 로고
    • Enzymatic synthesis of the pteridine moiety of dihydrofolate from guanine nucleotides
    • Shiota, T. & Palumbo, M.P. (1965) Enzymatic synthesis of the pteridine moiety of dihydrofolate from guanine nucleotides. J. Biol. Chem. 240, 4449-4453.
    • (1965) J. Biol. Chem. , vol.240 , pp. 4449-4453
    • Shiota, T.1    Palumbo, M.P.2
  • 3
    • 0001064828 scopus 로고
    • Biosynthesis of folic acid, riboflavin, thiamine, and pantothenic acid
    • Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M. & Umbarger, H.E., eds. American Society for Microbiology, Washington, DC
    • Brown, G.M. & Williamson, J.M. (1987) Biosynthesis of folic acid, riboflavin, thiamine, and pantothenic acid. In Escherichia coli and Salmonella typhimurium (Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M. & Umbarger, H.E., eds), pp. 521-538. American Society for Microbiology, Washington, DC.
    • (1987) Escherichia coli and Salmonella typhimurium , pp. 521-538
    • Brown, G.M.1    Williamson, J.M.2
  • 4
    • 0021891891 scopus 로고
    • Biosynthesis and metabolism of tetrahydrobiopterin and molybdopterin
    • Nichol, C.A., Smith, G.K. & Duch, D.S. (1985) Biosynthesis and metabolism of tetrahydrobiopterin and molybdopterin. Annu. Rev. Biochem. 54, 729-764.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 729-764
    • Nichol, C.A.1    Smith, G.K.2    Duch, D.S.3
  • 5
    • 0016789502 scopus 로고
    • Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli
    • Foor, F. & Brown, G.M. (1975) Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli. J. Biol. Chem. 250, 3545-3551.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3545-3551
    • Foor, F.1    Brown, G.M.2
  • 7
    • 0032500588 scopus 로고    scopus 로고
    • Potential of Escherichia coli GTP cyclohydrolase II for hydrolyzing 8-oxo-dGTP, a mutagenic substrate for DNA synthesis
    • Kobayashi, M., Ohara-Nemoto, Y., Kaneko, M., Hayakawa, H., Sekiguchi, M. & Yamamoto, K. (1998) Potential of Escherichia coli GTP cyclohydrolase II for hydrolyzing 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 273, 26394-26399.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26394-26399
    • Kobayashi, M.1    Ohara-Nemoto, Y.2    Kaneko, M.3    Hayakawa, H.4    Sekiguchi, M.5    Yamamoto, K.6
  • 9
    • 0033546186 scopus 로고    scopus 로고
    • Histidine 179 mutants of GTP cyclohydrolase I catalyze the formation of 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate
    • Bracher, A., Fischer, M., Eisenreich, W., Ritz, H., Schramek, N., Boyle, P., Gentili, P., Huber, R., Nar, H., Auerbach, G. & Bacher, A. (1999) Histidine 179 mutants of GTP cyclohydrolase I catalyze the formation of 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate. J. Biol. Chem. 274, 16727-16735.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16727-16735
    • Bracher, A.1    Fischer, M.2    Eisenreich, W.3    Ritz, H.4    Schramek, N.5    Boyle, P.6    Gentili, P.7    Huber, R.8    Nar, H.9    Auerbach, G.10    Bacher, A.11
  • 10
    • 0002447044 scopus 로고
    • Recombination and mutagenesis of DNA sequences using PCR
    • McPherson, M.J., ed. Oxford University Press, New York
    • Horton, R.M. & Pease, L.R. (1991) Recombination and mutagenesis of DNA sequences using PCR. In Directed Mutagenesis (McPherson, M.J., ed.), pp. 217-246. Oxford University Press, New York.
    • (1991) Directed Mutagenesis , pp. 217-246
    • Horton, R.M.1    Pease, L.R.2
  • 11
    • 0344568130 scopus 로고
    • Biosynthesis of riboflavin. Cloning, sequencing, mapping, and hyperexpression of the genes ribA coding for GTP cyclohydrolase II and ribC coding for riboflavin synthase of Escherichia coli
    • De Gruyter, Berlin, Germany
    • Eberhardt, S., Richter, G., Ritz, H., Brandt, J. & Bacher, A. (1994) Biosynthesis of riboflavin. Cloning, sequencing, mapping, and hyperexpression of the genes ribA coding for GTP cyclohydrolase II and ribC coding for riboflavin synthase of Escherichia coli. In Flavins Flavoproteins 1993: Proceedings of the 11th International Symposium. pp. 63-66. De Gruyter, Berlin, Germany.
    • (1994) Flavins Flavoproteins 1993: Proceedings of the 11th International Symposium , pp. 63-66
    • Eberhardt, S.1    Richter, G.2    Ritz, H.3    Brandt, J.4    Bacher, A.5
  • 13
    • 0035941188 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin. Single turnover kinetic analysis of GTP cyclohydrolase II
    • Schramek, N., Bracher, A. & Bacher, A. (2001) Biosynthesis of riboflavin. Single turnover kinetic analysis of GTP cyclohydrolase II. J. Biol. Chem. 276, 44157-44162.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44157-44162
    • Schramek, N.1    Bracher, A.2    Bacher, A.3
  • 14
    • 0020214783 scopus 로고
    • Flavinogenesis regulation in riboflavin-dependent Escherichia coli mutants
    • Shavlovskii, G.M., Tesliar, G.E. & Strugovshchikova, L.P. (1982) Flavinogenesis regulation in riboflavin-dependent Escherichia coli mutants. Mikrobiologiia 51, 986-992.
    • (1982) Mikrobiologiia , vol.51 , pp. 986-992
    • Shavlovskii, G.M.1    Tesliar, G.E.2    Strugovshchikova, L.P.3
  • 15
    • 17444441446 scopus 로고
    • Detection in Pichia guilliermondii of GTP-cyclohydrolase, an enzyme involved in the 1st stage of flavinogenesis
    • Shavlovskii, G.M., Logvinenko, E.M., Kashchenko, V.E., Koltun, L.V. & Zakal'skii, A.E. (1976) Detection in Pichia guilliermondii of GTP-cyclohydrolase, an enzyme involved in the 1st stage of flavinogenesis. Dokl. Akad. Nauk SSSR 230, 1485-1487.
    • (1976) Dokl. Akad. Nauk SSSR , vol.230 , pp. 1485-1487
    • Shavlovskii, G.M.1    Logvinenko, E.M.2    Kashchenko, V.E.3    Koltun, L.V.4    Zakal'skii, A.E.5
  • 16
    • 84941437184 scopus 로고
    • Growth of Candida guilliermondii deficiency mutants with ethyl methanesulfonate
    • Oltmanns, O., Bacher, A. & Lingens, F. (1968) Growth of Candida guilliermondii deficiency mutants with ethyl methanesulfonate. Z. Naturforsch. B 23, 1556.
    • (1968) Z. Naturforsch. B , vol.23 , pp. 1556
    • Oltmanns, O.1    Bacher, A.2    Lingens, F.3
  • 18
    • 0025361947 scopus 로고
    • Dihydrofolate reductase as a therapeutic target
    • Schweitzer, B.I., Dicker, A.P. & Bertino, J.R. (1990) Dihydrofolate reductase as a therapeutic target. FASEB J. 4, 2441-2452.
    • (1990) FASEB J. , vol.4 , pp. 2441-2452
    • Schweitzer, B.I.1    Dicker, A.P.2    Bertino, J.R.3
  • 19
    • 0015246411 scopus 로고
    • Folate antagonists as antibacterial and antiprotozoal agents
    • Hitchings, G.H. (1971) Folate antagonists as antibacterial and antiprotozoal agents. Ann. NY Acad. Sci. 186, 444-451.
    • (1971) Ann. NY Acad. Sci. , vol.186 , pp. 444-451
    • Hitchings, G.H.1
  • 20
    • 0014696486 scopus 로고
    • The biosynthesis of folic acid. X. Evidence for an Amadori rearrangement in the enzymatic formation of dihydroneopterin triphosphate from GTP
    • Wolf, W.A. & Brown, G.M. (1969) The biosynthesis of folic acid. X. Evidence for an Amadori rearrangement in the enzymatic formation of dihydroneopterin triphosphate from GTP. Biochim. Biophys. Acta 192, 468-478.
    • (1969) Biochim. Biophys. Acta , vol.192 , pp. 468-478
    • Wolf, W.A.1    Brown, G.M.2
  • 21
    • 0014683605 scopus 로고
    • The assignment of structure to the formamidopyrimidine nucleoside triphosphate precursor of pteridines
    • Shiota, T., Baugh, C.M. & Myrick, J. (1969) The assignment of structure to the formamidopyrimidine nucleoside triphosphate precursor of pteridines. Biochim. Biophys. Acta 192, 205-210.
    • (1969) Biochim. Biophys. Acta , vol.192 , pp. 205-210
    • Shiota, T.1    Baugh, C.M.2    Myrick, J.3
  • 22
    • 0032561180 scopus 로고    scopus 로고
    • Biosynthesis of pteridines. NMR studies on the reaction mechanisms of GTP cyclohydrolase I, pyruvoyltetrahydropterin synthase, and sepiapterin reductase
    • Bracher, A., Eisenreich, W., Schramek, N., Ritz, H., Götze, E., Herrmann, A., Gütlich, M. & Bacher, A. (1998) Biosynthesis of pteridines. NMR studies on the reaction mechanisms of GTP cyclohydrolase I, pyruvoyltetrahydropterin synthase, and sepiapterin reductase. J. Biol. Chem. 273, 28132-28141.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28132-28141
    • Bracher, A.1    Eisenreich, W.2    Schramek, N.3    Ritz, H.4    Götze, E.5    Herrmann, A.6    Gütlich, M.7    Bacher, A.8
  • 23
    • 0035951839 scopus 로고    scopus 로고
    • Ring opening is not rate-limiting in the GTP cyclohydrolase I reaction
    • Schramek, N., Bracher, A. & Bacher, A. (2001) Ring opening is not rate-limiting in the GTP cyclohydrolase I reaction. J. Biol. Chem. 276, 2622-2626.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2622-2626
    • Schramek, N.1    Bracher, A.2    Bacher, A.3
  • 24
    • 0036300682 scopus 로고    scopus 로고
    • Reaction mechanisms of GTP cyclohydrolase I. Single turnover experiments using a kinetically competent reaction intermediate
    • Schramek, N., Bracher, A., Fischer, M., Auerbach, G., Nar, H., Huber, R. & Bacher, A. (2002) Reaction mechanisms of GTP cyclohydrolase I. Single turnover experiments using a kinetically competent reaction intermediate. J. Mol. Biol. 316, 829-837.
    • (2002) J. Mol. Biol. , vol.316 , pp. 829-837
    • Schramek, N.1    Bracher, A.2    Fischer, M.3    Auerbach, G.4    Nar, H.5    Huber, R.6    Bacher, A.7
  • 25
    • 0024419886 scopus 로고
    • Short and long spacer sequences and other structural features of zinc binding sites in zinc enzymes
    • Vallee, B.L. & Auld, D.S. (1989) Short and long spacer sequences and other structural features of zinc binding sites in zinc enzymes. FEBS Lett. 257, 138-140.
    • (1989) FEBS Lett. , vol.257 , pp. 138-140
    • Vallee, B.L.1    Auld, D.S.2
  • 26
    • 0000596754 scopus 로고
    • Mechanism of carboxypeptidase A: Hydration of a ketonic substrate analogue
    • Christianson, D.W., David, P.R. & Lipscomb, W.N. (1987) Mechanism of carboxypeptidase A: Hydration of a ketonic substrate analogue. Proc. Natl. Acad. Sci. USA 84, 1512-1515.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1512-1515
    • Christianson, D.W.1    David, P.R.2    Lipscomb, W.N.3
  • 28
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli with beta galactosidase selection
    • Bullock, W.O., Fernandez, J.M. & Short, J.M. (1987) XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli with beta galactosidase selection. Bio Techniques 5, 376-380.
    • (1987) Bio Techniques , vol.5 , pp. 376-380
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 29
    • 0000926770 scopus 로고
    • System for high-level production in Escherichia coli and rapid purification of recombinant proteins: Application to epitope mapping, preparation of antibodies, and structure-function analysis
    • Lefkovits, I. & Pernis, P., eds. Academic Press, Orlando, FL
    • Stüber, D., Matile, H. & Garotta, G. (1990) System for high-level production in Escherichia coli and rapid purification of recombinant proteins: Application to epitope mapping, preparation of antibodies, and structure-function analysis. In Immunological Methods (Lefkovits, I. & Pernis, P., eds), pp. 121-152. Academic Press, Orlando, FL.
    • (1990) Immunological Methods , pp. 121-152
    • Stüber, D.1    Matile, H.2    Garotta, G.3


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