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Structural and Functional Relationship of the Catalytical Subunit of Recombinant Pyruvate Dehydrogenase Phosphatase (rPDPc): Limited Proteolysis  

Kim, Young-Mi (Department of Pharmacy, Duksung Women′s University)
Publication Information
Environmental Analysis Health and Toxicology / v.17, no.1, 2002 , pp. 73-80 More about this Journal
Keywords
Limited proteolysis; Functional domain; Recombinant catalytic subunit of pyruvate dehydrogenase phosphatase(rPDPc); Inner lipoyl domain(L2); Dihydrolipoamide acetyltransferase (E2); Pyruvate dehydrogenase complex (PDC);
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1 Bradford, M. A rapid and sensitive method for the quanti-tation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976; 72 : 248-254   DOI   PUBMED   ScienceOn
2 Pettit, F.H., Roche, T.E., and Reed, L.J. Function of calcium ions in pyruvate dehydrogenase phosphatase activity. Biochem. Biophy. Res. Comun. 1972; 49: 563-571   DOI   ScienceOn
3 Chen, G., Wang, L., Liu, S., Chuang, C., and Roche, T.E. Activated Function of the Pyruvate Dehydrogenase Phosphatase through $Ca^{2+}$-facilitated Binding to the Inner Lipoyl Domain of the Dihydrolipoyl Acetyl transferase. J. Biol. Chem.1996; 271 : 28064-28070   DOI   PUBMED   ScienceOn
4 Neurath, H. In Protein Folding (Jaenicke, R., Ed.) 1980; pp 501-523, Elsevier, Amsterdam
5 Denton, R.M., Randle, P.J., and Martin, B.R. Simulation by calcium ion of Pyruvate dehydrogenase phophate phosphatase. Biochem. J. 1972; 128: 161-163   DOI
6 Lawson, J.E., Niu, X.-D., Browning, K.S., LeTrong, H., Yan, J., and Reed, L.J. Molecular cloning and Expression of the Catalytic Subunit of Bovine Pyruvate Dehydrogenase Phosphatase and Sequence Similarity with Protein Phosphatase 2C. Biochemistry 1993; 32 : 8987-8993   DOI   ScienceOn
7 Choi, W.S., Yan, J., McCarthy, D.B., Park, S.H., and Reed, LJ. One-step purification of the recombinant catalytic subunit of pyruvate dehydrogenase phosphatase. Protein Expression and Purification 2000; 20 : 128-131   DOI   ScienceOn
8 Hubbard, S.J. The structural aspects of limited proteolysis of native proteins. Biochim. Biophys. Acta, 1998; 1382 : 191-206   DOI
9 Linn, T.C., Pettit, F.H., and Reed, L.J. $\alpha$-Keto acid Dehydrogenase Complex, X. Regulation of the activity of the Pyruvate Dehydrogenase Complex from beef kidney mitochondria by phosphorylation and dephosphorylation. Proc. Natl. Acad. Sci. U.S.A. 1969; 62, 234-241   DOI   ScienceOn
10 Damuni, Z., Humphreys, J.S., and Reed, LJ. Stimulation of pyruvate dehydrogenase phosphatase activity by poly-amines. Biochem. Biophy. Res. Comun. 1984; 124: 95-99   DOI   ScienceOn
11 Teague, W.M., Pettit, F.H., Wu, T.-L., Silberman, S.R., and Reed, L.J. Purification and Properties of Pyruvate Dehydrogenase Phosphatase from Bovine Heart and Kidney. Biochemistry 1982; 21 : 5585-5592   DOI   ScienceOn
12 Pratt, M.L., Maher, J.F., and Roche, T.E. Purification of Bovine Kidney and Heart Pyruvate Dehydrogenase Phosphatase on Sepharose derivatized with Pyruvate Dehydrogenase Complex. Eur. J. Biochem. 1982; 125 : 349-355   DOI   ScienceOn
13 Yan, J., Lawson, J.E., and Reed, L.J. Role of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase. Proc. Natl. Acad. Sci. U.S.A. 1996; 93 : 4953-4956   DOI   ScienceOn