메뉴 건너뛰기




Volumn 180, Issue 1-2, 1996, Pages 157-163

A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution

Author keywords

Amidohydrolase; cDNA cloning; CRMP 62; Dihydropyrimidine; TOAD 64; unc 33

Indexed keywords

AMIDASE; BRAIN ENZYME; COMPLEMENTARY DNA; LIVER ENZYME;

EID: 0030597343     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(96)00445-3     Document Type: Article
Times cited : (204)

References (23)
  • 1
    • 0018788906 scopus 로고
    • Dihydropyrimidine amidohydrolase is a zinc metalloenzyme
    • Brooks, K.P., Kim, B.D. and Sander, E.G. (1979) Dihydropyrimidine amidohydrolase is a zinc metalloenzyme. Biochim. Biophys. Acta 570, 213-217.
    • (1979) Biochim. Biophys. Acta , vol.570 , pp. 213-217
    • Brooks, K.P.1    Kim, B.D.2    Sander, E.G.3
  • 2
    • 0020616770 scopus 로고
    • Bovine liver dihydropyrimidine amidohydrolase: Purification, properties, and characterization as a zinc metalloenzyme
    • Brooks, K.P., Jones, E.A., Kim, B.D. and Sander, E.G. (1983) Bovine liver dihydropyrimidine amidohydrolase: purification, properties, and characterization as a zinc metalloenzyme. Arch. Biochem. Biophys. 226, 469-483.
    • (1983) Arch. Biochem. Biophys. , vol.226 , pp. 469-483
    • Brooks, K.P.1    Jones, E.A.2    Kim, B.D.3    Sander, E.G.4
  • 3
    • 0016309583 scopus 로고
    • The role of dihydropyrimidinase in the metabolism of some hydantoin and succinimide drugs
    • Dudley, K.H., Butler, T.C. and Bius, D.L. (1974) The role of dihydropyrimidinase in the metabolism of some hydantoin and succinimide drugs. Drug Metab. Dispos. 2, 103-112.
    • (1974) Drug Metab. Dispos. , vol.2 , pp. 103-112
    • Dudley, K.H.1    Butler, T.C.2    Bius, D.L.3
  • 5
    • 0000519943 scopus 로고
    • 14-labeled uracil, dihydrouracil, and β-ureidopropionic acid in rat liver slices
    • 14-labeled uracil, dihydrouracil, and β-ureidopropionic acid in rat liver slices. J. Biol. Chem. 226, 223-228.
    • (1957) J. Biol. Chem. , vol.226 , pp. 223-228
    • Fritzson, P.1
  • 6
    • 0011946527 scopus 로고
    • 14-labeled uracil, dihydrouracil, and β-ureidopropionic acid in the intact rat
    • 14-labeled uracil, dihydrouracil, and β-ureidopropionic acid in the intact rat. J. Biol. Chem. 226, 229-235.
    • (1957) J. Biol. Chem. , vol.226 , pp. 229-235
    • Fritzson, P.1    Phil, A.2
  • 7
    • 0029132912 scopus 로고
    • Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33
    • Goshima, Y., Nakamura, F., Strittmatter, P. and Strittmatter, S.M. (1995) Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33. Nature 376, 509-514.
    • (1995) Nature , vol.376 , pp. 509-514
    • Goshima, Y.1    Nakamura, F.2    Strittmatter, P.3    Strittmatter, S.M.4
  • 9
    • 0028075161 scopus 로고
    • Isolation and characterization of 21 novel expressed DNA sequences from the distal region of human chromosome 4p
    • Ishida, Y., Hadano, S., Nagayama, T., Tomiyasu, H., Wakasa, K. and Ikeda, J. (1994) Isolation and characterization of 21 novel expressed DNA sequences from the distal region of human chromosome 4p. Genomics 22, 302-312.
    • (1994) Genomics , vol.22 , pp. 302-312
    • Ishida, Y.1    Hadano, S.2    Nagayama, T.3    Tomiyasu, H.4    Wakasa, K.5    Ikeda, J.6
  • 11
    • 0017148315 scopus 로고
    • Role of enzymatically catalyzed 5-iodo-5,6-dihydrouracil ring hydrolysis on the dehalogenation of 5-iodouracil
    • Kim, B.D., Keenen, S., Bodnar, J.K. and Sander, E.G. (1976) Role of enzymatically catalyzed 5-iodo-5,6-dihydrouracil ring hydrolysis on the dehalogenation of 5-iodouracil. J. Biol. Chem. 251, 6909-6914.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6909-6914
    • Kim, B.D.1    Keenen, S.2    Bodnar, J.K.3    Sander, E.G.4
  • 12
    • 0028932319 scopus 로고
    • Isolation of 115 human chromosome 8-specific expressed-sequence tags by exon amplification
    • Koyama, K., Sudo, K. and Nakamura, Y. (1995) Isolation of 115 human chromosome 8-specific expressed-sequence tags by exon amplification. Genomics 26, 245-253.
    • (1995) Genomics , vol.26 , pp. 245-253
    • Koyama, K.1    Sudo, K.2    Nakamura, Y.3
  • 13
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak, M. (1986) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44, 283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 14
    • 0028220717 scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of the D-hydantoinase gene from Pseudomonas putida and distribution of homologous genes in other microorganisms
    • Lapointe, G., Viau, S., Leblanc, D., Robert, N. and Morin, A. (1994) Cloning, sequencing, and expression in Escherichia coli of the D-hydantoinase gene from Pseudomonas putida and distribution of homologous genes in other microorganisms. Appl. Environ. Microb. 60, 888-895.
    • (1994) Appl. Environ. Microb. , vol.60 , pp. 888-895
    • Lapointe, G.1    Viau, S.2    Leblanc, D.3    Robert, N.4    Morin, A.5
  • 15
    • 0026658652 scopus 로고
    • Analysis of the Caenorhabditis elegans axonal guidance and outgrowth gene unc-33
    • Li, W., Herman, R.K. and Shaw, J.E. (1992) Analysis of the Caenorhabditis elegans axonal guidance and outgrowth gene unc-33. Genetics 132, 675-689.
    • (1992) Genetics , vol.132 , pp. 675-689
    • Li, W.1    Herman, R.K.2    Shaw, J.E.3
  • 16
    • 0018171925 scopus 로고
    • Partial purification and characterization of dihydropyrimidinases from calf and rat liver
    • Maguire, J.H. and Dudley, K.H. (1978) Partial purification and characterization of dihydropyrimidinases from calf and rat liver. Drug Metab. Dispos. 6, 601-605.
    • (1978) Drug Metab. Dispos. , vol.6 , pp. 601-605
    • Maguire, J.H.1    Dudley, K.H.2
  • 18
    • 0029065065 scopus 로고
    • Early postmitotic neurons transiently expressed TOAD-64, a neural specific protein
    • Minturn, J.E., Geschwind, D.H., Fryer, H.J.L. and Hockfield, S. (1995) Early postmitotic neurons transiently expressed TOAD-64, a neural specific protein. J. Comp. Neurol. 355, 369-379.
    • (1995) J. Comp. Neurol. , vol.355 , pp. 369-379
    • Minturn, J.E.1    Geschwind, D.H.2    Fryer, H.J.L.3    Hockfield, S.4
  • 19
    • 85007968312 scopus 로고
    • A thermostable hydantoinase of Bacillus stearothermophilus NS112A: Cloning, sequencing, and high expression of enzyme gene, and some properties of the expressed enzyme
    • Mukohara, Y., Ishikawa, T., Watabe, K. and Nakamura, H. (1994) A thermostable hydantoinase of Bacillus stearothermophilus NS112A: cloning, sequencing, and high expression of enzyme gene, and some properties of the expressed enzyme. Biosci. Biotechnol. Biochem. 58, 1621-1626.
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 1621-1626
    • Mukohara, Y.1    Ishikawa, T.2    Watabe, K.3    Nakamura, H.4
  • 21
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N. and Nei, M. (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4, 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 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
  • 23
    • 0000053191 scopus 로고
    • The purification and properties of hydropyrimidine hydrase
    • Wallach, D.P. and Glisolia, S. (1957) The purification and properties of hydropyrimidine hydrase. J. Biol. Chem. 226, 277-288.
    • (1957) J. Biol. Chem. , vol.226 , pp. 277-288
    • Wallach, D.P.1    Glisolia, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.