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Volumn 380, Issue 4, 2008, Pages 656-666

A Second Pathway to Degrade Pyrimidine Nucleic Acid Precursors in Eukaryotes

Author keywords

3 hydroxypropionic acid; metabolic pathways; nucleic acid precursors; uracil degradation; urea

Indexed keywords

AMMONIA; CARBON DIOXIDE; DIHYDROURACIL; HYDRACRYLIC ACID; NUCLEIC ACID PRECURSOR; PHOSPHORIBOSYLTRANSFERASE; PYRIMIDINE NUCLEIC ACID PRECURSOR; TRANSCRIPTION FACTOR; URACIL; URACIL PHOSPHORIBOSYLTRANSFERASE; UREA; URIDINE PHOSPHATE;

EID: 45649084019     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.05.029     Document Type: Article
Times cited : (44)

References (32)
  • 1
    • 28744451345 scopus 로고    scopus 로고
    • Nucleotide metabolism
    • Benjamin/Cummings Publishing Company, San Francisco, CA
    • Mathews C.K., van Holde K.E., and Ahern K.G. Nucleotide metabolism. Biochemistry. 3rd edit. (2000), Benjamin/Cummings Publishing Company, San Francisco, CA 794-829
    • (2000) Biochemistry. 3rd edit. , pp. 794-829
    • Mathews, C.K.1    van Holde, K.E.2    Ahern, K.G.3
  • 2
    • 0017122896 scopus 로고
    • Degradation of purines and pyrimidines by microorganisms
    • Vogels G.D., and van der Drift C. Degradation of purines and pyrimidines by microorganisms. Bacteriol. Rev. 40 (1976) 403-468
    • (1976) Bacteriol. Rev. , vol.40 , pp. 403-468
    • Vogels, G.D.1    van der Drift, C.2
  • 3
    • 0018894446 scopus 로고
    • Degradation of pyrimidines and pyrimidine analogs-pathways and mutual influences
    • Wasternack C. Degradation of pyrimidines and pyrimidine analogs-pathways and mutual influences. Pharmacol. Ther. 8 (1980) 629-651
    • (1980) Pharmacol. Ther. , vol.8 , pp. 629-651
    • Wasternack, C.1
  • 5
    • 0041804297 scopus 로고    scopus 로고
    • 5-fluorouracil and dihydropyrimidine dehydrogenase
    • Kubota T. 5-fluorouracil and dihydropyrimidine dehydrogenase. Int. J. Clin. Oncol. 8 (2003) 127-131
    • (2003) Int. J. Clin. Oncol. , vol.8 , pp. 127-131
    • Kubota, T.1
  • 6
    • 0001134323 scopus 로고
    • Metabolism of cytosine, thymine, uracil, and barbituric acid by bacterial enzymes
    • Hayaishi O., and Kornberg A. Metabolism of cytosine, thymine, uracil, and barbituric acid by bacterial enzymes. J. Biol. Chem. 197 (1952) 717-732
    • (1952) J. Biol. Chem. , vol.197 , pp. 717-732
    • Hayaishi, O.1    Kornberg, A.2
  • 7
    • 0036510575 scopus 로고    scopus 로고
    • Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism
    • Soong C.L., Ogawa J., Sakuradani E., and Shimizu S. Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism. J. Biol. Chem. 277 (2002) 7051-7058
    • (2002) J. Biol. Chem. , vol.277 , pp. 7051-7058
    • Soong, C.L.1    Ogawa, J.2    Sakuradani, E.3    Shimizu, S.4
  • 9
    • 0034723154 scopus 로고    scopus 로고
    • PYD2 encodes 5,6-dihydropyrimidine amidohydrolase, which participates in a novel fungal catabolic pathway
    • Gojkovic Z., Jahnke K., Schnackerz K.D., and Piškur J. PYD2 encodes 5,6-dihydropyrimidine amidohydrolase, which participates in a novel fungal catabolic pathway. J. Mol. Biol. 295 (2000) 1073-1087
    • (2000) J. Mol. Biol. , vol.295 , pp. 1073-1087
    • Gojkovic, Z.1    Jahnke, K.2    Schnackerz, K.D.3    Piškur, J.4
  • 10
    • 0034913997 scopus 로고    scopus 로고
    • Eukaryotic β-alanine synthases are functionally related but have a high degree of structural diversity
    • Gojkovic Z., Sandrini M.P., and Piškur J. Eukaryotic β-alanine synthases are functionally related but have a high degree of structural diversity. Genetics 158 (2001) 999-1011
    • (2001) Genetics , vol.158 , pp. 999-1011
    • Gojkovic, Z.1    Sandrini, M.P.2    Piškur, J.3
  • 11
    • 33947244361 scopus 로고    scopus 로고
    • A gene duplication led to specialized γ-aminobutyrate and β-alanine aminotransferase in yeast
    • Andersen G., Andersen B., Dobritzsch D., Schnackerz K.D., and Piškur J. A gene duplication led to specialized γ-aminobutyrate and β-alanine aminotransferase in yeast. FEBS J. 274 (2007) 1804-1817
    • (2007) FEBS J. , vol.274 , pp. 1804-1817
    • Andersen, G.1    Andersen, B.2    Dobritzsch, D.3    Schnackerz, K.D.4    Piškur, J.5
  • 12
    • 33744961438 scopus 로고    scopus 로고
    • The crystal structures of dihydropyrimidinases reaffirm the close relationship between cyclic amidohydrolases and explain their substrate specificity
    • Lohkamp B., Andersen B., Piškur J., and Dobritzsch D. The crystal structures of dihydropyrimidinases reaffirm the close relationship between cyclic amidohydrolases and explain their substrate specificity. J. Biol. Chem. 281 (2006) 13762-13776
    • (2006) J. Biol. Chem. , vol.281 , pp. 13762-13776
    • Lohkamp, B.1    Andersen, B.2    Piškur, J.3    Dobritzsch, D.4
  • 13
    • 0347695018 scopus 로고    scopus 로고
    • Yeast β-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases
    • Lundgren S., Gojkovic Z., Piškur J., and Dobritzsch D. Yeast β-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases. J. Biol. Chem. 278 (2003) 51851-51862
    • (2003) J. Biol. Chem. , vol.278 , pp. 51851-51862
    • Lundgren, S.1    Gojkovic, Z.2    Piškur, J.3    Dobritzsch, D.4
  • 14
    • 0038724989 scopus 로고    scopus 로고
    • Finding functional features in Saccharomyces genomes by phylogenetic footprinting
    • Cliften P., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J., et al. Finding functional features in Saccharomyces genomes by phylogenetic footprinting. Science 301 (2003) 71-76
    • (2003) Science , vol.301 , pp. 71-76
    • Cliften, P.1    Sudarsanam, P.2    Desikan, A.3    Fulton, L.4    Fulton, B.5    Majors, J.6
  • 15
    • 0035093803 scopus 로고    scopus 로고
    • Ability for anaerobic growth is not sufficient for development of the petite phenotype in Saccharomyces kluyveri
    • Moller K., Olsson L., and Piskur J. Ability for anaerobic growth is not sufficient for development of the petite phenotype in Saccharomyces kluyveri. J. Bacteriol. 183 (2001) 2485-2489
    • (2001) J. Bacteriol. , vol.183 , pp. 2485-2489
    • Moller, K.1    Olsson, L.2    Piskur, J.3
  • 17
    • 0018972331 scopus 로고
    • Structural analysis of the dur loci in S. cerevisiae: two domains of a single multifunctional gene
    • Cooper T.G., Lam C., and Turoscy V. Structural analysis of the dur loci in S. cerevisiae: two domains of a single multifunctional gene. Genetics 94 (1980) 555-580
    • (1980) Genetics , vol.94 , pp. 555-580
    • Cooper, T.G.1    Lam, C.2    Turoscy, V.3
  • 18
    • 0035872914 scopus 로고    scopus 로고
    • Phenotypic analysis of genes encoding yeast zinc cluster proteins
    • Akache B., Wu K., and Turcotte B. Phenotypic analysis of genes encoding yeast zinc cluster proteins. Nucleic Acids Res. 29 (2001) 2181-2190
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2181-2190
    • Akache, B.1    Wu, K.2    Turcotte, B.3
  • 19
    • 39049140674 scopus 로고    scopus 로고
    • urg1: a uracil-regulatable promoter system for fission yeast with short induction and repression times
    • Watt S., Mata J., Lopez-Maury L., Marguerat S., Burns G., and Bahler J. urg1: a uracil-regulatable promoter system for fission yeast with short induction and repression times. PLoS ONE 3 (2008) e1428
    • (2008) PLoS ONE , vol.3
    • Watt, S.1    Mata, J.2    Lopez-Maury, L.3    Marguerat, S.4    Burns, G.5    Bahler, J.6
  • 20
    • 0025126611 scopus 로고
    • The URK1 gene of Saccharomyces cerevisiae encoding uridine kinase
    • Kern L. The URK1 gene of Saccharomyces cerevisiae encoding uridine kinase. Nucleic Acids Res. 18 (1990) 5279
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5279
    • Kern, L.1
  • 21
    • 0036197502 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae URH1 (encoding uridine-cytidine N-ribohydrolase): functional complementation by a nucleoside hydrolase from a protozoan parasite and by a mammalian uridine phosphorylase
    • Mitterbauer R., Karl T., and Adam G. Saccharomyces cerevisiae URH1 (encoding uridine-cytidine N-ribohydrolase): functional complementation by a nucleoside hydrolase from a protozoan parasite and by a mammalian uridine phosphorylase. Appl. Environ. Microbiol. 68 (2002) 1336-1343
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1336-1343
    • Mitterbauer, R.1    Karl, T.2    Adam, G.3
  • 22
    • 0036951940 scopus 로고    scopus 로고
    • The URH1 uridine ribohydrolase of Saccharomyces cerevisiae
    • Kurtz J.E., Exinger F., Erbs P., and Jund R. The URH1 uridine ribohydrolase of Saccharomyces cerevisiae. Curr. Genet. 41 (2002) 132-141
    • (2002) Curr. Genet. , vol.41 , pp. 132-141
    • Kurtz, J.E.1    Exinger, F.2    Erbs, P.3    Jund, R.4
  • 23
    • 0032822048 scopus 로고    scopus 로고
    • New insights into the pyrimidine salvage pathway of Saccharomyces cerevisiae: requirement of six genes for cytidine metabolism
    • Kurtz J.E., Exinger F., Erbs P., and Jund R. New insights into the pyrimidine salvage pathway of Saccharomyces cerevisiae: requirement of six genes for cytidine metabolism. Curr. Genet. 36 (1999) 130-136
    • (1999) Curr. Genet. , vol.36 , pp. 130-136
    • Kurtz, J.E.1    Exinger, F.2    Erbs, P.3    Jund, R.4
  • 25
    • 0014243685 scopus 로고
    • The utilization of purines and pyrimidines by yeasts
    • LaRue T.A., and Spencer J.F. The utilization of purines and pyrimidines by yeasts. Can. J. Microbiol. 14 (1968) 79-86
    • (1968) Can. J. Microbiol. , vol.14 , pp. 79-86
    • LaRue, T.A.1    Spencer, J.F.2
  • 28
    • 0031807751 scopus 로고    scopus 로고
    • A new model organism for studying the catabolism of pyrimidines and purines
    • Gojkovic Z., Paracchini S., and Piskur J. A new model organism for studying the catabolism of pyrimidines and purines. Adv. Exp. Med. Biol. 431 (1998) 475-479
    • (1998) Adv. Exp. Med. Biol. , vol.431 , pp. 475-479
    • Gojkovic, Z.1    Paracchini, S.2    Piskur, J.3
  • 29
    • 0025785410 scopus 로고
    • A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors
    • Bonneaud N., Ozier-Kalogeropoulos O., Li G.Y., Labouesse M., Minvielle-Sebastia L., and Lacroute F. A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors. Yeast 7 (1991) 609-615
    • (1991) Yeast , vol.7 , pp. 609-615
    • Bonneaud, N.1    Ozier-Kalogeropoulos, O.2    Li, G.Y.3    Labouesse, M.4    Minvielle-Sebastia, L.5    Lacroute, F.6
  • 30
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach A., Brachat A., Pohlmann R., and Philippsen P. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10 (1994) 1793-1808
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 31
    • 3242741850 scopus 로고    scopus 로고
    • Design of experiments: an efficient strategy to identify factors influencing extraction and derivatization of Arabidopsis thaliana samples in metabolomic studies with gas chromatography/mass spectrometry
    • Gullberg J., Jonsson P., Nordström A., Sjöström M., and Moritz T. Design of experiments: an efficient strategy to identify factors influencing extraction and derivatization of Arabidopsis thaliana samples in metabolomic studies with gas chromatography/mass spectrometry. Anal. Biochem. 331 (2004) 283-295
    • (2004) Anal. Biochem. , vol.331 , pp. 283-295
    • Gullberg, J.1    Jonsson, P.2    Nordström, A.3    Sjöström, M.4    Moritz, T.5
  • 32
    • 20044368617 scopus 로고    scopus 로고
    • GC-MS libraries for the rapid identification of metabolites in complex biological samples
    • Schauer N., Steinhauser D., Strelkov S., Schomburg D., Allison G., Moritz T., et al. GC-MS libraries for the rapid identification of metabolites in complex biological samples. FEBS Lett. 579 (2005) 1332-1337
    • (2005) FEBS Lett. , vol.579 , pp. 1332-1337
    • Schauer, N.1    Steinhauser, D.2    Strelkov, S.3    Schomburg, D.4    Allison, G.5    Moritz, T.6


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