메뉴 건너뛰기




Volumn 36, Issue 5, 2004, Pages 861-869

Substrate binding to fluorescent labeled wild type, Lys213Arg, and His233Gln Saccharomyces cerevisiae phosphoenolpyruvate carboxykinases

Author keywords

HEPES; High pressure liquid chromatography; HPLC; Lamarckian genetic algorithm; LGA; N (2 hydroxyethyl)piperazine N 2(ethanesulfonic acid); P pyridoxyl; PEP; Phosphoenolpyruvate; Phosphopyridoxyl; PLP; Pyridoxal 5 phosphate; TFA

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE DIPHOSPHATE MANGANESE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MANGANESE; ARGININE; FLUORESCENT DYE; GLUTAMINE; HISTIDINE; LIGAND; LYSINE; MANGANESE; MANGANESE DERIVATIVE; MUTANT PROTEIN; NITROGEN; OXYGEN; PHOSPHOENOLPYRUVATE; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP); PYRIDOXINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 1542285126     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2003.09.008     Document Type: Article
Times cited : (5)

References (22)
  • 2
    • 0028909473 scopus 로고
    • Identification of reactive lysyl residues in Escherichia coli and Saccharomyces cerevisiae phosphoenolpyruvate carboxykinases
    • Bazaes S., Goldie H., Cardemil E., Jabalquinto A.M. Identification of reactive lysyl residues in Escherichia coli and Saccharomyces cerevisiae phosphoenolpyruvate carboxykinases. FEBS Letters. 360:1995;207-210.
    • (1995) FEBS Letters , vol.360 , pp. 207-210
    • Bazaes, S.1    Goldie, H.2    Cardemil, E.3    Jabalquinto, A.M.4
  • 3
    • 0025365503 scopus 로고
    • Reactive sulfhydryl groups in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase
    • Cardemil E., Encinas M.V., Jabalquinto A.M. Reactive sulfhydryl groups in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Biochimica et Biophysica Acta. 1040:1990;71-76.
    • (1990) Biochimica et Biophysica Acta , vol.1040 , pp. 71-76
    • Cardemil, E.1    Encinas, M.V.2    Jabalquinto, A.M.3
  • 5
    • 0036411895 scopus 로고    scopus 로고
    • Ligand interactions and protein conformational changes of phosphopyridoxyl-labeled Escherichia coli phosphoenolpyruvate carboxykinase determined by fluorescence spectroscopy
    • Encinas M.V., González-Nilo F.D., Goldie H., Cardemil E. Ligand interactions and protein conformational changes of phosphopyridoxyl-labeled Escherichia coli phosphoenolpyruvate carboxykinase determined by fluorescence spectroscopy. European Journal of Biochemistry. 269:2002;1-9.
    • (2002) European Journal of Biochemistry , vol.269 , pp. 1-9
    • Encinas, M.V.1    González-Nilo, F.D.2    Goldie, H.3    Cardemil, E.4
  • 6
    • 0027513857 scopus 로고
    • Fluorescent labeling of the nucleotide site in cytosolic rat liver phosphoenolpyruvate carboxykinase
    • Encinas M.V., Rojas M.C., Goldie H., Cardemil E. Fluorescent labeling of the nucleotide site in cytosolic rat liver phosphoenolpyruvate carboxykinase. Biochimica et Biophysica Acta. 1162:1993;195-202.
    • (1993) Biochimica et Biophysica Acta , vol.1162 , pp. 195-202
    • Encinas, M.V.1    Rojas, M.C.2    Goldie, H.3    Cardemil, E.4
  • 8
    • 0030938873 scopus 로고    scopus 로고
    • Formation and characterization of an active phosphoenolpyruvate carboxykinase-cobalt(III) complex
    • Hlavaty J.J., Nowak T. Formation and characterization of an active phosphoenolpyruvate carboxykinase-cobalt(III) complex. Biochemistry. 36:1997;3389-3403.
    • (1997) Biochemistry , vol.36 , pp. 3389-3403
    • Hlavaty, J.J.1    Nowak, T.2
  • 9
    • 0032485890 scopus 로고    scopus 로고
    • The strongly conserved lysine 256 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase is essential for phosphoryl transfer
    • Krautwurst H., Bazaes S., González F.D., Jabalquinto A.M., Frey P.A., Cardemil E. The strongly conserved lysine 256 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase is essential for phosphoryl transfer. Biochemistry. 37:1998;6295-6302.
    • (1998) Biochemistry , vol.37 , pp. 6295-6302
    • Krautwurst, H.1    Bazaes, S.2    González, F.D.3    Jabalquinto, A.M.4    Frey, P.A.5    Cardemil, E.6
  • 10
    • 0029026779 scopus 로고
    • Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: Revised amino acid sequence* site-directed mutagenesis, and microenvironment characteristics of cysteines 365 and 458
    • Krautwurst H., Encinas M.V., Marcus F., Latshaw S.P., Kemp R.G., Frey P.A., Cardemil E. Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: revised amino acid sequence* site-directed mutagenesis, and microenvironment characteristics of cysteines 365 and 458. Biochemistry. 34:1995;6382-6388.
    • (1995) Biochemistry , vol.34 , pp. 6382-6388
    • Krautwurst, H.1    Encinas, M.V.2    Marcus, F.3    Latshaw, S.P.4    Kemp, R.G.5    Frey, P.A.6    Cardemil, E.7
  • 11
    • 0037159256 scopus 로고    scopus 로고
    • Lysine 213 and histidine 233 participate in Mn(II) binding and catalysis in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase
    • Krautwurst H., Roschzttardtz H., Bazaes S., González-Nilo F.D., Nowak T., Cardemil E. Lysine 213 and histidine 233 participate in Mn(II) binding and catalysis in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Biochemistry. 41:2002;12763-12770.
    • (2002) Biochemistry , vol.41 , pp. 12763-12770
    • Krautwurst, H.1    Roschzttardtz, H.2    Bazaes, S.3    González-Nilo, F.D.4    Nowak, T.5    Cardemil, E.6
  • 12
    • 0021766645 scopus 로고
    • Phosphorus-31 nuclear relaxation rate studies of the nucleotides on phosphoenolpyruvate carboxykinase
    • Lee M.H., Nowak T. Phosphorus-31 nuclear relaxation rate studies of the nucleotides on phosphoenolpyruvate carboxykinase. Biochemistry. 23:1984;6506-6513.
    • (1984) Biochemistry , vol.23 , pp. 6506-6513
    • Lee, M.H.1    Nowak, T.2
  • 13
    • 0035937570 scopus 로고    scopus 로고
    • Mutation Arg336 to Lys in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase originates an enzyme with increased oxaloacetate decarboxylase activity
    • Llanos L., Briones R., Yévenes A., González-Nilo F.D., Frey P.A., Cardemil E. Mutation Arg336 to Lys in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase originates an enzyme with increased oxaloacetate decarboxylase activity. FEBS Letters. 493:2001;1-5.
    • (2001) FEBS Letters , vol.493 , pp. 1-5
    • Llanos, L.1    Briones, R.2    Yévenes, A.3    González-Nilo, F.D.4    Frey, P.A.5    Cardemil, E.6
  • 16
    • 0015747532 scopus 로고
    • Spectra of 3-hydroxypyridines. Band-shape analysis and evaluation of tautomeric equilibrium
    • Metzler D.E., Harris C.M., Johnson R.J., Siano D.B., Thomson J.A. Spectra of 3-hydroxypyridines. Band-shape analysis and evaluation of tautomeric equilibrium. Biochemistry. 26:1973;5377-5392.
    • (1973) Biochemistry , vol.26 , pp. 5377-5392
    • Metzler, D.E.1    Harris, C.M.2    Johnson, R.J.3    Siano, D.B.4    Thomson, J.A.5
  • 19
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Šali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. Journal of Molecular Biology. 234:1993;779-815.
    • (1993) Journal of Molecular Biology , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 21
    • 0035834540 scopus 로고    scopus 로고
    • Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 Å resolution
    • Trapani S., Linss J., Goldenberg S., Fischer H., Craievich A.F., Oliva G. Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 Å resolution. Journal of Molecular Biology. 313:2001;1059-1072.
    • (2001) Journal of Molecular Biology , vol.313 , pp. 1059-1072
    • Trapani, S.1    Linss, J.2    Goldenberg, S.3    Fischer, H.4    Craievich, A.F.5    Oliva, G.6
  • 22
    • 0027381018 scopus 로고
    • Is pyridoxal 5′-phosphate an affinity label for phosphate-binding sites in proteins? the case of bovine glutamate dehydrogenase
    • Valinger Z., Engel P.C., Metzler D.E. Is pyridoxal 5′-phosphate an affinity label for phosphate-binding sites in proteins? The case of bovine glutamate dehydrogenase. Biochemical Journal. 15:1993;835-839.
    • (1993) Biochemical Journal , vol.15 , pp. 835-839
    • Valinger, Z.1    Engel, P.C.2    Metzler, D.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.