메뉴 건너뛰기




Volumn 47, Issue 8, 2008, Pages 2592-2600

Understanding functional divergence in proteins by studying intragenomic homologues

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; ENZYME ACTIVITY; FUNCTIONAL GROUPS; REACTION KINETICS;

EID: 39749110672     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702263z     Document Type: Article
Times cited : (9)

References (34)
  • 3
    • 1642266935 scopus 로고    scopus 로고
    • Gene duplication and biased functional retention of paralogs in bacterial genomes
    • Gevers, D., Vandepoele, K., Simillon, C., and Van de Peer, Y. (2004) Gene duplication and biased functional retention of paralogs in bacterial genomes, Trends Microbiol. 12, 148-154.
    • (2004) Trends Microbiol , vol.12 , pp. 148-154
    • Gevers, D.1    Vandepoele, K.2    Simillon, C.3    Van de Peer, Y.4
  • 4
    • 33746664765 scopus 로고    scopus 로고
    • Can sequence determine function
    • Gerlt, J. A., and Babbitt, P. C. (2000) Can sequence determine function, Genome Biol. 1, 1-10.
    • (2000) Genome Biol , vol.1 , pp. 1-10
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 5
    • 0037046560 scopus 로고    scopus 로고
    • Bentley, S. D., Chater, K. F., Cerdeno-Tarraga, A. M., Challis, G. L., Thomson, N. R., James, K. D., Harris, D. E., Quail, M. A., Kieser, H., Harper, D., Bateman, A., Brown, S., Chandra, G., Chen, C. W., Collins, M., Cronin, A., Fraser, A., Goble, A., Hidalgo, J., Hornsby, T., Howarth, S., Huang, C. H., Kieser, T., Larke, L., Murphy, L., Oliver, K., O'Neil, S., Rabbinowitsch, E., Rajandream, M. A., Rutherford, K., Rutter, S., Seeger, K., Saunders, D., Sharp, S., Squares, R., Squares, S., Taylor, K., Warren, T., Wietzorrek, A., Woodward, J., Barrell, B. G., Parkhill, J., and Hopwood, D. A. (2002) Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2), Nature 417, 141-147.
    • Bentley, S. D., Chater, K. F., Cerdeno-Tarraga, A. M., Challis, G. L., Thomson, N. R., James, K. D., Harris, D. E., Quail, M. A., Kieser, H., Harper, D., Bateman, A., Brown, S., Chandra, G., Chen, C. W., Collins, M., Cronin, A., Fraser, A., Goble, A., Hidalgo, J., Hornsby, T., Howarth, S., Huang, C. H., Kieser, T., Larke, L., Murphy, L., Oliver, K., O'Neil, S., Rabbinowitsch, E., Rajandream, M. A., Rutherford, K., Rutter, S., Seeger, K., Saunders, D., Sharp, S., Squares, R., Squares, S., Taylor, K., Warren, T., Wietzorrek, A., Woodward, J., Barrell, B. G., Parkhill, J., and Hopwood, D. A. (2002) Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2), Nature 417, 141-147.
  • 7
  • 8
    • 0036832419 scopus 로고    scopus 로고
    • Biosynthesis of vitamin B2. An essential zinc ion at the catalytic site of GTP cyclohydrolase II
    • Kaiser, J., Schramek, N., Eberhardt, S., Puttmer, S., Schuster, M., and Bacher, A. (2002) Biosynthesis of vitamin B2. An essential zinc ion at the catalytic site of GTP cyclohydrolase II, Eur. J. Biochem. 269, 5264-5270.
    • (2002) Eur. J. Biochem , vol.269 , pp. 5264-5270
    • Kaiser, J.1    Schramek, N.2    Eberhardt, S.3    Puttmer, S.4    Schuster, M.5    Bacher, A.6
  • 10
    • 0035941188 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin. Single turnover kinetic analysis of GTP cyclohydrolase II
    • Schramek, N., Bracher, A., and 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
  • 11
    • 33750706955 scopus 로고    scopus 로고
    • Evolution of New Function in the GTP Cyclohydrolase II Proteins of Streptomyces coelicolor
    • Spoonamore, J. E., Dahlgran, A. L., Jacobsen, N. E., and Bandarian, V. (2006) Evolution of New Function in the GTP Cyclohydrolase II Proteins of Streptomyces coelicolor, Biochemistry 45, 12144-12155.
    • (2006) Biochemistry , vol.45 , pp. 12144-12155
    • Spoonamore, J.E.1    Dahlgran, A.L.2    Jacobsen, N.E.3    Bandarian, V.4
  • 12
    • 0014030296 scopus 로고
    • Enzymic release of carbon atom 8 from guanosine triphosphate, an early reaction in the conversion of purines to pteridines
    • Levenberg, B., and Kaczmarek, D. K. (1966) Enzymic release of carbon atom 8 from guanosine triphosphate, an early reaction in the conversion of purines to pteridines, Biochim. Biophys. Acta 117, 272-275.
    • (1966) Biochim. Biophys. Acta , vol.117 , pp. 272-275
    • Levenberg, B.1    Kaczmarek, D.K.2
  • 13
    • 0014027128 scopus 로고
    • On the biosynthesis of toxoflavin, an azapteridine antibiotic produced by Pseudomonas cocovenenans
    • Levenberg, B., and Linton, S. N. (1966) On the biosynthesis of toxoflavin, an azapteridine antibiotic produced by Pseudomonas cocovenenans, J. Biol. Chem. 241, 846-852.
    • (1966) J. Biol. Chem , vol.241 , pp. 846-852
    • Levenberg, B.1    Linton, S.N.2
  • 14
    • 3042826857 scopus 로고    scopus 로고
    • Molecular characterization of the tox operon involved in toxoflavin biosynthesis of Burkholderia glumae
    • Suzuki, F., Sawada, H., Azegami, K., and Tsuchiya, K. (2004) Molecular characterization of the tox operon involved in toxoflavin biosynthesis of Burkholderia glumae, J. Gen. Plant Pathol. 70, 97-107.
    • (2004) J. Gen. Plant Pathol , vol.70 , pp. 97-107
    • Suzuki, F.1    Sawada, H.2    Azegami, K.3    Tsuchiya, K.4
  • 15
    • 0016789502 scopus 로고
    • Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli
    • Foor, F., and 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
  • 16
    • 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., and 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
  • 19
    • 0021860884 scopus 로고
    • Anion-exchange high performance liquid chromatography method for the quantitation of nucleotides in human blood cells
    • de Korte, D., Haverkort, W. A., Roos, D., and van Gennip, A. H. (1985) Anion-exchange high performance liquid chromatography method for the quantitation of nucleotides in human blood cells, Clin. Chim. Acta 148, 185-196.
    • (1985) Clin. Chim. Acta , vol.148 , pp. 185-196
    • de Korte, D.1    Haverkort, W.A.2    Roos, D.3    van Gennip, A.H.4
  • 22
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 25
    • 26644444335 scopus 로고    scopus 로고
    • Novel reaction mechanism of GTP cyclohydrolase I. High-resolution X-ray crystallography of Thermus thermophilus HB8 enzyme complexed with a transition state analogue, the 8-oxoguanine derivative
    • Tanaka, Y., Nakagawa, N., Kuramitsu, S., Yokoyama, S., and Masui, R. (2005) Novel reaction mechanism of GTP cyclohydrolase I. High-resolution X-ray crystallography of Thermus thermophilus HB8 enzyme complexed with a transition state analogue, the 8-oxoguanine derivative, J. Biochem. (Tokyo) 138, 263-275.
    • (2005) J. Biochem. (Tokyo) , vol.138 , pp. 263-275
    • Tanaka, Y.1    Nakagawa, N.2    Kuramitsu, S.3    Yokoyama, S.4    Masui, R.5
  • 27
    • 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., and 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
  • 28
    • 0037126723 scopus 로고    scopus 로고
    • A member of a new class of GTP cyclohydrolases produces formylaminopyrimidine nucleotide monophosphates
    • Graham, D. E., Xu, H., and White, R. H. (2002) A member of a new class of GTP cyclohydrolases produces formylaminopyrimidine nucleotide monophosphates, Biochemistry 41, 15074-15084.
    • (2002) Biochemistry , vol.41 , pp. 15074-15084
    • Graham, D.E.1    Xu, H.2    White, R.H.3
  • 29
    • 34249874032 scopus 로고    scopus 로고
    • 2+-dependent archaeal-specific GTP cyclohydrolase, MptA, from Methanocaldococcus jannaschii
    • 2+-dependent archaeal-specific GTP cyclohydrolase, MptA, from Methanocaldococcus jannaschii, Biochemistry 46, 6658-6667.
    • (2007) Biochemistry , vol.46 , pp. 6658-6667
    • Grochowski, L.L.1    Xu, H.2    Leung, K.3    White, R.H.4
  • 30
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz, T. A., and Steitz, J. A. (1993) A general two-metal-ion mechanism for catalytic RNA, Proc. Natl. Acad. Sci. U.S.A. 90, 6498-6502.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 31
    • 0032425454 scopus 로고    scopus 로고
    • The adenylyl and guanylyl cyclase superfamily
    • Hurley, J. H. (1998) The adenylyl and guanylyl cyclase superfamily, Curr. Opin. Struct. Biol. 8, 770-777.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 770-777
    • Hurley, J.H.1
  • 34
    • 37849022102 scopus 로고    scopus 로고
    • A new use for a familiar fold: The X-ray crystal structure of GTP-bound GTP cyclohydrolase III from Methanocaldococcus jannaschii reveals a two metal ion catalytic mechanism
    • Morrison, S. D., Roberts, S. A., Zegeer, A. M., Montfort, W. A., and Bandarian, V. (2008) A new use for a familiar fold: The X-ray crystal structure of GTP-bound GTP cyclohydrolase III from Methanocaldococcus jannaschii reveals a two metal ion catalytic mechanism, Biochemistry 47, 230-242.
    • (2008) Biochemistry , vol.47 , pp. 230-242
    • Morrison, S.D.1    Roberts, S.A.2    Zegeer, A.M.3    Montfort, W.A.4    Bandarian, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.