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Volumn 350, Issue 4, 2006, Pages 922-928

A threonine synthase homolog from a mammalian genome

Author keywords

Enzyme classification; Enzyme evolution; Functional genomics; Phospho lyase; Pyridoxal phosphate

Indexed keywords

2 OXOBUTYRIC ACID; AMMONIA; HOMOSERINE; LYASE; PHOSPHATE; PYRIDOXAL 5 PHOSPHATE; SYNTHETASE; THREONINE; THREONINE SYNTHETASE; UNCLASSIFIED DRUG;

EID: 33750035176     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.09.112     Document Type: Article
Times cited : (15)

References (25)
  • 1
    • 0031059740 scopus 로고    scopus 로고
    • Biosynthesis of 'essential' amino acids by scleractinian corals
    • Fitzgerald L.M., and Szmant A.M. Biosynthesis of 'essential' amino acids by scleractinian corals. Biochem. J. 322 (1997) 213-221
    • (1997) Biochem. J. , vol.322 , pp. 213-221
    • Fitzgerald, L.M.1    Szmant, A.M.2
  • 2
    • 32944463126 scopus 로고    scopus 로고
    • Retention and loss of amino acid biosynthetic pathways based on analysis of whole-genome sequences
    • Payne S.H., and Loomis W.F. Retention and loss of amino acid biosynthetic pathways based on analysis of whole-genome sequences. Eukaryot. Cell 5 (2006) 272-276
    • (2006) Eukaryot. Cell , vol.5 , pp. 272-276
    • Payne, S.H.1    Loomis, W.F.2
  • 3
    • 0242495818 scopus 로고    scopus 로고
    • Crystal structures of threonine synthase from Thermus thermophilus HB8: conformational change, substrate recognition, and mechanism
    • Omi R., Goto M., Miyahara I., Mizuguchi H., Hayashi H., Kagamiyama H., and Hirotsu K. Crystal structures of threonine synthase from Thermus thermophilus HB8: conformational change, substrate recognition, and mechanism. J. Biol. Chem. 278 (2003) 46035-46045
    • (2003) J. Biol. Chem. , vol.278 , pp. 46035-46045
    • Omi, R.1    Goto, M.2    Miyahara, I.3    Mizuguchi, H.4    Hayashi, H.5    Kagamiyama, H.6    Hirotsu, K.7
  • 5
    • 33646179897 scopus 로고    scopus 로고
    • Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site
    • Mas-Droux C., Biou V., and Dumas R. Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site. J. Biol. Chem. 281 (2006) 5188-5196
    • (2006) J. Biol. Chem. , vol.281 , pp. 5188-5196
    • Mas-Droux, C.1    Biou, V.2    Dumas, R.3
  • 6
    • 0029046782 scopus 로고
    • Modeling of the spatial structure of eukaryotic ornithine decarboxylases
    • Grishin N.V., Phillips M.A., and Goldsmith E.J. Modeling of the spatial structure of eukaryotic ornithine decarboxylases. Protein Sci. 4 (1995) 1291-1304
    • (1995) Protein Sci. , vol.4 , pp. 1291-1304
    • Grishin, N.V.1    Phillips, M.A.2    Goldsmith, E.J.3
  • 7
    • 0033649909 scopus 로고    scopus 로고
    • The molecular evolution of pyridoxal-5′-phosphate-dependent enzymes
    • Mehta P.K., and Christen P. The molecular evolution of pyridoxal-5′-phosphate-dependent enzymes. Adv. Enzymol. 74 (2000) 129-184
    • (2000) Adv. Enzymol. , vol.74 , pp. 129-184
    • Mehta, P.K.1    Christen, P.2
  • 8
    • 0142186241 scopus 로고    scopus 로고
    • A genomic overview of pyridoxal-phosphate-dependent enzymes
    • Percudani R., and Peracchi A. A genomic overview of pyridoxal-phosphate-dependent enzymes. EMBO Rep. 4 (2003) 850-854
    • (2003) EMBO Rep. , vol.4 , pp. 850-854
    • Percudani, R.1    Peracchi, A.2
  • 9
    • 0034476899 scopus 로고    scopus 로고
    • Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily
    • Zhou T., Daugherty M., Grishin N.V., Osterman A.L., and Zhang H. Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily. Structure Fold. Des. 8 (2000) 1247-1257
    • (2000) Structure Fold. Des. , vol.8 , pp. 1247-1257
    • Zhou, T.1    Daugherty, M.2    Grishin, N.V.3    Osterman, A.L.4    Zhang, H.5
  • 10
    • 0028290467 scopus 로고
    • Inactivation of Escherichia coli threonine synthase by DL-Z-2-amino-5-phosphono-3-pentenoic acid
    • Laber B., Lindell S.D., and Pohlenz H.D. Inactivation of Escherichia coli threonine synthase by DL-Z-2-amino-5-phosphono-3-pentenoic acid. Arch. Microbiol. 161 (1994) 400-403
    • (1994) Arch. Microbiol. , vol.161 , pp. 400-403
    • Laber, B.1    Lindell, S.D.2    Pohlenz, H.D.3
  • 12
    • 0028218431 scopus 로고
    • Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors
    • Laber B., Gerbling K.P., Harde C., Neff K.H., Nordhoff E., and Pohlenz H.D. Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors. Biochemistry 33 (1994) 3413-3423
    • (1994) Biochemistry , vol.33 , pp. 3413-3423
    • Laber, B.1    Gerbling, K.P.2    Harde, C.3    Neff, K.H.4    Nordhoff, E.5    Pohlenz, H.D.6
  • 13
    • 0015793310 scopus 로고
    • Threonine synthetase-catalyzed conversion of phosphohomoserine to α-ketobutyrate in Bacillus subtilis
    • Schildkraut I., and Greer S. Threonine synthetase-catalyzed conversion of phosphohomoserine to α-ketobutyrate in Bacillus subtilis. J. Bacteriol. 115 (1973) 777-785
    • (1973) J. Bacteriol. , vol.115 , pp. 777-785
    • Schildkraut, I.1    Greer, S.2
  • 14
    • 0036308741 scopus 로고    scopus 로고
    • Enzyme function less conserved than anticipated
    • Rost B. Enzyme function less conserved than anticipated. J. Mol. Biol. 318 (2002) 595-608
    • (2002) J. Mol. Biol. , vol.318 , pp. 595-608
    • Rost, B.1
  • 15
    • 2942700177 scopus 로고    scopus 로고
    • Inactive enzyme-homologues find new function in regulatory processes
    • Pils B., and Schultz J. Inactive enzyme-homologues find new function in regulatory processes. J. Mol. Biol. 340 (2004) 399-404
    • (2004) J. Mol. Biol. , vol.340 , pp. 399-404
    • Pils, B.1    Schultz, J.2
  • 16
    • 0022515539 scopus 로고
    • O-phosphohomoserine, a naturally occurring analogue of phosphonate amino acid antagonists, is an N-methyl-d-aspartate (NMDA) antagonist in rat hippocampus
    • Connick J.H., Heywood G.C., Smith D.A., and Stone T.W. O-phosphohomoserine, a naturally occurring analogue of phosphonate amino acid antagonists, is an N-methyl-d-aspartate (NMDA) antagonist in rat hippocampus. Neurosci. Lett. 68 (1986) 249-251
    • (1986) Neurosci. Lett. , vol.68 , pp. 249-251
    • Connick, J.H.1    Heywood, G.C.2    Smith, D.A.3    Stone, T.W.4
  • 17
    • 0025906074 scopus 로고
    • Distribution and contents of free O-phosphoamino acids in animal tissues
    • Kataoka H., Sakiyama N., and Makita M. Distribution and contents of free O-phosphoamino acids in animal tissues. J. Biochem. 109 (1991) 577-580
    • (1991) J. Biochem. , vol.109 , pp. 577-580
    • Kataoka, H.1    Sakiyama, N.2    Makita, M.3
  • 18
    • 0032558460 scopus 로고    scopus 로고
    • Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine
    • Curien G., Job D., Douce R., and Dumas R. Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine. Biochemistry 37 (1998) 13212-13221
    • (1998) Biochemistry , vol.37 , pp. 13212-13221
    • Curien, G.1    Job, D.2    Douce, R.3    Dumas, R.4
  • 19
    • 0014940107 scopus 로고
    • The metabolism of O-phosphorylethanolamine in animal tissues. I. O-phosphorylethanolamine phospho-lyase: partial purification and characterization
    • Fleshood H.L., and Pitot H.C. The metabolism of O-phosphorylethanolamine in animal tissues. I. O-phosphorylethanolamine phospho-lyase: partial purification and characterization. J. Biol. Chem. 245 (1970) 4414-4420
    • (1970) J. Biol. Chem. , vol.245 , pp. 4414-4420
    • Fleshood, H.L.1    Pitot, H.C.2
  • 20
    • 0016236057 scopus 로고
    • Degradation of O-phosphohydroxylysine by rat liver. Purification of the phospho-lyase
    • Tsai C.H., and Henderson L.M. Degradation of O-phosphohydroxylysine by rat liver. Purification of the phospho-lyase. J. Biol. Chem. 249 (1974) 5784-5789
    • (1974) J. Biol. Chem. , vol.249 , pp. 5784-5789
    • Tsai, C.H.1    Henderson, L.M.2
  • 21
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O'Brien P.J., and Herschlag D. Catalytic promiscuity and the evolution of new enzymatic activities. Chem. Biol. 6 (1999) R91-R105
    • (1999) Chem. Biol. , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 22
    • 0028879747 scopus 로고
    • Degradation of purines: only ureidoglycollate lyase out of four allantoin-degrading enzymes is present in mammals
    • Fujiwara S., and Noguchi T. Degradation of purines: only ureidoglycollate lyase out of four allantoin-degrading enzymes is present in mammals. Biochem. J. 312 (1995) 315-318
    • (1995) Biochem. J. , vol.312 , pp. 315-318
    • Fujiwara, S.1    Noguchi, T.2
  • 24
    • 2942709486 scopus 로고    scopus 로고
    • Evolution of cell-cell signaling in animals: did late horizontal gene transfer from bacteria have a role?
    • Iyer L.M., Aravind L., Coon S.L., Klein D.C., and Koonin E.V. Evolution of cell-cell signaling in animals: did late horizontal gene transfer from bacteria have a role?. Trends Genet. 20 (2004) 292-299
    • (2004) Trends Genet. , vol.20 , pp. 292-299
    • Iyer, L.M.1    Aravind, L.2    Coon, S.L.3    Klein, D.C.4    Koonin, E.V.5
  • 25


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.