메뉴 건너뛰기




Volumn 571, Issue 1-3, 2004, Pages 141-146

Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function

Author keywords

Aminotransferase; Pyridoxal 5 phosphate; Structural genomics

Indexed keywords

AMINO ACID; AMINOTRANSFERASE; ASPARTATE AMINOTRANSFERASE; HISTIDINE; LYSINE; METHIONINE; METHIONINE AMINOTRANSFERASE; PHENYLALANINE; PYRIDOXAL 5 PHOSPHATE; PYRIDOXINE; UNCLASSIFIED DRUG;

EID: 3342948464     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.06.075     Document Type: Article
Times cited : (17)

References (30)
  • 1
    • 0142186241 scopus 로고    scopus 로고
    • A genomic overview of pyridoxal-phosphate-dependent enzymes
    • Percudani R., 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
  • 2
    • 0029046782 scopus 로고
    • Modeling of the spatial structure of eukaryotic ornithine decarboxylases
    • Grishin N.V., Phillips M.A., 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
  • 5
    • 0019014846 scopus 로고
    • Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase
    • Ford G.C., Eichele G., Jansonius J.N. Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase. Proc. Natl. Acad. Sci. USA. 77:1980;2559-2563
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2559-2563
    • Ford, G.C.1    Eichele, G.2    Jansonius, J.N.3
  • 6
    • 0024297340 scopus 로고
    • Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium
    • Hyde C.C., et al. Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263:1988;17857-17871
    • (1988) J. Biol. Chem. , vol.263 , pp. 17857-17871
    • Hyde, C.C.1
  • 7
    • 0031032448 scopus 로고    scopus 로고
    • Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-Å resolution
    • Shaw J.P., Petsko G.A., Ringe D. Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-Å resolution. Biochemistry. 36:1997;1329-1342
    • (1997) Biochemistry , vol.36 , pp. 1329-1342
    • Shaw, J.P.1    Petsko, G.A.2    Ringe, D.3
  • 8
    • 0029144437 scopus 로고
    • Crystal structure of a D-amino acid aminotransferase: How the protein controls stereoselectivity
    • Sugio S., et al. Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity. Biochemistry. 34:1995;9661-9669
    • (1995) Biochemistry , vol.34 , pp. 9661-9669
    • Sugio, S.1
  • 9
    • 0017860747 scopus 로고
    • Crystallographic studies on the activity of glycogen phosphorylase b
    • Weber I.T., et al. Crystallographic studies on the activity of glycogen phosphorylase b. Nature. 274:1978;433-437
    • (1978) Nature , vol.274 , pp. 433-437
    • Weber, I.T.1
  • 11
    • 0242538842 scopus 로고    scopus 로고
    • ′-phosphate-dependent enzymes
    • ′ -phosphate-dependent enzymes J. Mol. Biol. 291:1999;857-876
    • (1999) J. Mol. Biol. , vol.291 , pp. 857-876
    • Kack, H.1
  • 12
    • 0028914569 scopus 로고
    • Pyridoxal phosphate-dependent enzymes
    • John R.A. Pyridoxal phosphate-dependent enzymes. Biochim. Biophys. Acta. 1248:1995;81-96
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 81-96
    • John, R.A.1
  • 13
    • 10744228811 scopus 로고    scopus 로고
    • Structural genomics of highly conserved microbial genes of unknown function in search of new antibacterial targets
    • Abergel C., et al. Structural genomics of highly conserved microbial genes of unknown function in search of new antibacterial targets. J. Struct. Funct. Genomics. 4:2003;141-157
    • (2003) J. Struct. Funct. Genomics , vol.4 , pp. 141-157
    • Abergel, C.1
  • 14
    • 0037351701 scopus 로고    scopus 로고
    • Medium-scale structural genomics: Strategies for protein expression and crystallization
    • Vincentelli R., et al. Medium-scale structural genomics: strategies for protein expression and crystallization. Acc. Chem. Res. 36:2003;165-172
    • (2003) Acc. Chem. Res. , vol.36 , pp. 165-172
    • Vincentelli, R.1
  • 15
    • 4243232779 scopus 로고    scopus 로고
    • A medium-throughput crystallization approach
    • Sulzenbacher G., et al. A medium-throughput crystallization approach. Acta Crystallogr. D: Biol. Crystallogr. 58(Pt 12):2002;2109-2115
    • (2002) Acta Crystallogr. D: Biol. Crystallogr. , vol.58 , Issue.12 PART , pp. 2109-2115
    • Sulzenbacher, G.1
  • 16
    • 0034681421 scopus 로고    scopus 로고
    • The molecular structure of hyperthermostable aromatic aminotransferase with novel substrate specificity from Pyrococcus horikoshii
    • Matsui I., et al. The molecular structure of hyperthermostable aromatic aminotransferase with novel substrate specificity from Pyrococcus horikoshii. J. Biol. Chem. 275:2000;4871-4879
    • (2000) J. Biol. Chem. , vol.275 , pp. 4871-4879
    • Matsui, I.1
  • 17
    • 0033732564 scopus 로고    scopus 로고
    • GATEWAY recombinational cloning: Application to the cloning of large numbers of open reading frames or ORFeomes
    • Walhout A.J., et al. GATEWAY recombinational cloning: application to the cloning of large numbers of open reading frames or ORFeomes. Methods Enzymol. 328:2000;575-592
    • (2000) Methods Enzymol. , vol.328 , pp. 575-592
    • Walhout, A.J.1
  • 18
    • 0027096461 scopus 로고
    • Crystallization of murine major histocompatibility complex class I H-2Kb with single peptides
    • Stura E.A., et al. Crystallization of murine major histocompatibility complex class I H-2Kb with single peptides. J. Mol. Biol. 228:1992;975-982
    • (1992) J. Mol. Biol. , vol.228 , pp. 975-982
    • Stura, E.A.1
  • 19
    • 0025913445 scopus 로고
    • Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium
    • Jancarik J., et al. Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium. J. Mol. Biol. 221:1991;31-34
    • (1991) J. Mol. Biol. , vol.221 , pp. 31-34
    • Jancarik, J.1
  • 20
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 21
    • 0002452464 scopus 로고
    • L. Sawyer, N.W. Isaacs, & S. Bailey. Warrington, UK: DLSCI/R34 Daresbury Laboratory
    • Otwinowski Z. Sawyer L., Isaacs N.W., Bailey S. DENZO: oscillation data and reducing program. 1993;56-63 DLSCI/R34 Daresbury Laboratory, Warrington, UK
    • (1993) DENZO: Oscillation Data and Reducing Program , pp. 56-63
    • Otwinowski, Z.1
  • 22
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for crystallography
    • CCP4 and C.C.P.N. 4, 1994. The CCP4 suite: programs for crystallography. Acta Cryst. D 50, 760-766
    • (1994) Acta Cryst. D , vol.50 , pp. 760-766
  • 23
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. Sect. A. 50:1994;157-163
    • (1994) Acta Crystallogr. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., et al. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47(Pt 2):1991;110-119
    • (1991) Acta Crystallogr. a , vol.47 , Issue.2 PART , pp. 110-119
    • Jones, T.A.1
  • 25
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger A.T., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D: Biol. Crystallogr. 54(Pt 5):1998;905-921
    • (1998) Acta Crystallogr. D: Biol. Crystallogr. , vol.54 , Issue.5 PART , pp. 905-921
    • Brunger, A.T.1
  • 26
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 27
    • 0003845223 scopus 로고    scopus 로고
    • San Carlos, CA, USA: DeLano Scientific LLC
    • W. DeLano (2004) The PyMOL Molecular Graphics System (http://www.pymol. org), San Carlos, CA, USA: DeLano Scientific LLC
    • The PyMOL Molecular Graphics System , vol.2004
    • Delano, W.1
  • 28
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L., Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20:1995;478-480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 29
    • 0033596715 scopus 로고    scopus 로고
    • Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate
    • Nakai T., et al. Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate. Biochemistry. 38:1999;2413-2424
    • (1999) Biochemistry , vol.38 , pp. 2413-2424
    • Nakai, T.1
  • 30
    • 0032540849 scopus 로고    scopus 로고
    • Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: A substrate recognition site constructed by rearrangement of hydrogen bond network
    • Okamoto A., et al. Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network. J. Mol. Biol. 280:1998;443-461
    • (1998) J. Mol. Biol. , vol.280 , pp. 443-461
    • Okamoto, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.