메뉴 건너뛰기




Volumn 63, Issue 5, 2006, Pages 517-523

Puzzling over orphan enzymes

Author keywords

Database exactitude; EC number; Gene annotation; Hidden knowledge; Orphan enzyme; Protein function; Protein sequence

Indexed keywords

4 CHLOROPHENOL; ENZYME; GLYCOSYLTRANSFERASE; HYDROLASE; ISOMERASE; LIGASE; LYASE; OXIDOREDUCTASE; PHOSPHODIESTERASE; TRANSFERASE;

EID: 33645049066     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5520-6     Document Type: Review
Times cited : (17)

References (35)
  • 1
    • 17644407349 scopus 로고    scopus 로고
    • A glimpse at the organization of the protein universe
    • USA
    • Vendruscolo M. and Dobson C. M. (2005) A glimpse at the organization of the protein universe. Proc. Natl. Acad. Sci. USA 102: 5641-5642
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 5641-5642
    • Vendruscolo, M.1    Dobson, C.M.2
  • 2
    • 14844363959 scopus 로고    scopus 로고
    • Global mapping of the protein structure space and application in structure-based inference of protein function
    • USA
    • Hou J. T., Jun S. R., Zhang C and Kim S. H. (2005) Global mapping of the protein structure space and application in structure-based inference of protein function. Proc. Natl. Acad. Sci. USA 102: 3651-3656
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 3651-3656
    • Hou, J.T.1    Jun, S.R.2    Zhang, C.3    Kim, S.H.4
  • 3
    • 0036140266 scopus 로고    scopus 로고
    • A unifold, mesofold and superfold model of protein fold use
    • Coulson A. F. W. and Moult J. (2002) A unifold, mesofold and superfold model of protein fold use. Proteins 46: 61-71
    • (2002) Proteins , vol.46 , pp. 61-71
    • Coulson, A.F.W.1    Moult, J.2
  • 4
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: Tool for the unification of biology
    • The Gene Ontology Consortium
    • Ashburner M., Ball C. A., Blake J. A., Botstein D., Butler H., Cherry J. M. et al. (2000) Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat. Genet. 25: 25-29
    • (2000) Nat. Genet. , vol.25 , pp. 25-29
    • Ashburner, M.1    Ball, C.A.2    Blake, J.A.3    Botstein, D.4    Butler, H.5    Cherry, J.M.6
  • 6
    • 0347125234 scopus 로고    scopus 로고
    • GenProtEC: An updated and improved analysis of functions of Escherichia coli K-12 proteins
    • Serres M. H., Goswami S. and Riley M. (2004) GenProtEC: an updated and improved analysis of functions of Escherichia coli K-12 proteins. Nucleic Acids Res. 32: D300-D302
    • (2004) Nucleic Acids Res. , vol.32
    • Serres, M.H.1    Goswami, S.2    Riley, M.3
  • 7
    • 19244366327 scopus 로고    scopus 로고
    • Call for an enzyme genomics initiative
    • Karp P. D. (2004) Call for an enzyme genomics initiative. Genome Biol. 5: 401
    • (2004) Genome Biol. , vol.5 , pp. 401
    • Karp, P.D.1
  • 8
  • 10
    • 0033982936 scopus 로고    scopus 로고
    • KEGG: Kyoto Encyclopedia of Genes and Genomes
    • Kanehisa M. and Goto S. (2000) KEGG: Kyoto Encyclopedia of Genes and Genomes. Nucleic Acids Res. 28: 27-30
    • (2000) Nucleic Acids Res. , vol.28 , pp. 27-30
    • Kanehisa, M.1    Goto, S.2
  • 13
    • 0027328345 scopus 로고
    • Sigma F., the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-sigma factor that is also a protein kinase
    • Min K. T., Hilditch C. M., Diederich B., Errington J. and Yudkin M. D. (1993) Sigma F., the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-sigma factor that is also a protein kinase. Cell 74: 735-742
    • (1993) Cell , vol.74 , pp. 735-742
    • Min, K.T.1    Hilditch, C.M.2    Diederich, B.3    Errington, J.4    Yudkin, M.D.5
  • 15
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation, an emerging regulator of protein function
    • Bedford M. T. and Richard S. (2005) Arginine methylation, an emerging regulator of protein function. Mol. Cell 18: 263-272
    • (2005) Mol. Cell , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 16
    • 23044485115 scopus 로고    scopus 로고
    • Genome annotation errors in pathway databases due to semantic ambiguity in partial EC numbers
    • Green ML and Karp P. D. (2005) Genome annotation errors in pathway databases due to semantic ambiguity in partial EC numbers. Nucleic Acids Res. 33: 4035-4039
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4035-4039
    • Green, M.L.1    Karp, P.D.2
  • 17
    • 0037044323 scopus 로고    scopus 로고
    • Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD
    • Karsten W. E., Tipton P. A. and Cook P. F. (2002) Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD. Biochemistry. 41: 12193-12199
    • (2002) Biochemistry. , vol.41 , pp. 12193-12199
    • Karsten, W.E.1    Tipton, P.A.2    Cook, P.F.3
  • 18
  • 19
    • 0037235543 scopus 로고    scopus 로고
    • Multifunctional proteins: Examples of gene sharing
    • Jeffery C. J. (2002) Multifunctional proteins: examples of gene sharing. Ann. Med. 35: 28-35
    • (2002) Ann. Med. , vol.35 , pp. 28-35
    • Jeffery, C.J.1
  • 20
    • 0042706146 scopus 로고    scopus 로고
    • Moonlighting proteins: Old proteins learning new tricks
    • Jeffery C. J. (2003) Moonlighting proteins: old proteins learning new tricks. Trends Genet. 19: 415-417
    • (2003) Trends Genet. , vol.19 , pp. 415-417
    • Jeffery, C.J.1
  • 21
    • 13844318224 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase, apoptosis and neurodegenerative diseases
    • Chuang D. M., Hough C. and Senatorov V. V. (2005) Glyceraldehyde-3- phosphate dehydrogenase, apoptosis and neurodegenerative diseases. Annu. Rev. Pharmacol. Toxicol. 45: 269-290
    • (2005) Annu. Rev. Pharmacol. Toxicol. , vol.45 , pp. 269-290
    • Chuang, D.M.1    Hough, C.2    Senatorov, V.V.3
  • 22
    • 9144265895 scopus 로고    scopus 로고
    • Retrieving sequence of enzymes experimentally characterized but erroneously annotated: The case of putrescine carbamoyltransferase
    • Naumoff D. G., Xu Y., Glansdorff N. and Labedan B. (2004) Retrieving sequence of enzymes experimentally characterized but erroneously annotated: the case of putrescine carbamoyltransferase. BMC Genomics 5: 52
    • (2004) BMC Genomics , vol.5 , pp. 52
    • Naumoff, D.G.1    Xu, Y.2    Glansdorff, N.3    Labedan, B.4
  • 23
    • 0028927080 scopus 로고
    • Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus
    • Mukund S. and Adams M. W. (1995) Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 270: 8389-8392
    • (1995) J. Biol. Chem. , vol.270 , pp. 8389-8392
    • Mukund, S.1    Adams, M.W.2
  • 24
    • 0032561335 scopus 로고    scopus 로고
    • The ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation
    • van der Oost J., Schut G. J., Kengen S. W. M., Hagen W. R., Thomm M. and de Vos. W. M. (1998) The ferredoxin-dependent conversion of glyceraldehyde-3- phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation. J. Biol. Chem. 273: 28149-28154
    • (1998) J. Biol. Chem. , vol.273 , pp. 28149-28154
    • Van Der Oost, J.1    Schut, G.J.2    Kengen, S.W.M.3    Hagen, W.R.4    Thomm, M.5    De Vos, W.M.6
  • 25
    • 13544250517 scopus 로고    scopus 로고
    • Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes
    • Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S. and Imanaka T. (2005) Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Res. 15: 352-363
    • (2005) Genome Res. , vol.15 , pp. 352-363
    • Fukui, T.1    Atomi, H.2    Kanai, T.3    Matsumi, R.4    Fujiwara, S.5    Imanaka, T.6
  • 26
    • 0035824553 scopus 로고    scopus 로고
    • Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase
    • Nakanishi M., Yatome C., Ishida N. and Kitade Y. (2001) Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase. J. Biol. Chem. 276: 46394-46399
    • (2001) J. Biol. Chem. , vol.276 , pp. 46394-46399
    • Nakanishi, M.1    Yatome, C.2    Ishida, N.3    Kitade, Y.4
  • 27
    • 27144441544 scopus 로고    scopus 로고
    • The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: Genetic and enzymological characterization
    • Thomas J. and Cronan J. E. (2005) The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and enzymological characterization. J. Biol. Chem. 280: 34675-34683
    • (2005) J. Biol. Chem. , vol.280 , pp. 34675-34683
    • Thomas, J.1    Cronan, J.E.2
  • 28
    • 0141816886 scopus 로고    scopus 로고
    • Characterization of an inducible chlorophenol O-methyltransferase from Trichoderma longibrachiatum involved in the formation of chloroanisoles and determination of its role in cork taint of wines
    • Coque J. J., Alvarez-Rodriguez M. L. and Larriba G. (2003) Characterization of an inducible chlorophenol O-methyltransferase from Trichoderma longibrachiatum involved in the formation of chloroanisoles and determination of its role in cork taint of wines. Appl. Environ. Microbiol. 69: 5089-5095
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5089-5095
    • Coque, J.J.1    Alvarez-Rodriguez, M.L.2    Larriba, G.3
  • 29
    • 0035875365 scopus 로고    scopus 로고
    • Fungal trehalose phosphorylase: Kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune
    • Eis C., Watkins M., Prohaska T. and Nidetzky B. (2001) Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune. Biochem. J. 356: 757-767
    • (2001) Biochem. J. , vol.356 , pp. 757-767
    • Eis, C.1    Watkins, M.2    Prohaska, T.3    Nidetzky, B.4
  • 30
    • 0035082791 scopus 로고    scopus 로고
    • p-Hydroxyphenylacetate decarboxylase from Clostridium difficile: A novel glycyl radical enzyme catalysing the formation of p-cresol
    • Selmer T. and Andrei P. I. (2001) p-Hydroxyphenylacetate decarboxylase from Clostridium difficile: a novel glycyl radical enzyme catalysing the formation of p-cresol. Eur. J. Biochem. 268: 1363-1372
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1363-1372
    • Selmer, T.1    Andrei, P.I.2
  • 31
    • 24044455869 scopus 로고    scopus 로고
    • Genome sequencing in microfabricated high-density picolitre reactors
    • Margulies M., Egholm M., Altman W. E., Attiya S., Bader J. S., Bemben L. A., et al. (2005) Genome sequencing in microfabricated high-density picolitre reactors. Nature 437: 376-380
    • (2005) Nature , vol.437 , pp. 376-380
    • Margulies, M.1    Egholm, M.2    Altman, W.E.3    Attiya, S.4    Bader, J.S.5    Bemben, L.A.6
  • 32
    • 25144471241 scopus 로고    scopus 로고
    • Genomics: Massively parallel sequencing
    • Rogers Y. H. and Venter J. C. (2005) Genomics: massively parallel sequencing. Nature 437: 326-327
    • (2005) Nature , vol.437 , pp. 326-327
    • Rogers, Y.H.1    Venter, J.C.2
  • 34
    • 84859747435 scopus 로고    scopus 로고
    • Molecular biology
    • Zalta E. N. (ed.)
    • Darden L. and Tabery J. (2005) Molecular biology. In: The Stanford Encyclopedia of Philosophy, Zalta E. N. (ed.), http://plato.stanford.edu/ archives/spr2005/entries/molecular-biology/
    • (2005) The Stanford Encyclopedia of Philosophy
    • Darden, L.1    Tabery, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.