메뉴 건너뛰기




Volumn 37, Issue , 1997, Pages 271-293

Studies on the regulation of the mitochondrial α-ketoacid dehydrogenase complexes and their kinases

Author keywords

[No Author keywords available]

Indexed keywords

(3-METHYL-2-OXOBUTANOATE DEHYDROGENASE (LIPOAMIDE)) KINASE; (PYRUVATE DEHYDROGENASE (LIPOAMIDE))KINASE; 2 OXOACID DEHYDROGENASE; 2-OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); COCARBOXYLASE; ISOENZYME; MITOCHONDRIAL ENZYME; MULTIENZYME COMPLEX; OXIDOREDUCTASE; PROTEIN KINASE; PYRUVATE DEHYDROGENASE COMPLEX; RECOMBINANT PROTEIN;

EID: 0030769818     PISSN: 00652571     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2571(96)00009-X     Document Type: Conference Paper
Times cited : (98)

References (56)
  • 1
    • 0024578239 scopus 로고
    • The 2-oxo acid dehydrogenase complexes: Recent advances
    • 1. S. J. YEAMAN, The 2-oxo acid dehydrogenase complexes: recent advances, Biochem. J. 257, 625-632 (1989).
    • (1989) Biochem. J. , vol.257 , pp. 625-632
    • Yeaman, S.J.1
  • 2
    • 0025221771 scopus 로고
    • Molecular biology and biochemistry of pyruvate dehydrogenase complexes
    • 2. M.S. PATEL and T. E. ROCHE, Molecular biology and biochemistry of pyruvate dehydrogenase complexes, FASEB J. 4, 3224-3233 (1990).
    • (1990) FASEB J. , vol.4 , pp. 3224-3233
    • Patel, M.S.1    Roche, T.E.2
  • 3
    • 0027997588 scopus 로고
    • Expression, purification, and characterization of the dihydrolipoamide dehydrogenase-binding protein of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae
    • 3. C.-Y. MAENG, M. A. YAZDI, X.-D. NIU, H. Y. LEE and L. J. REED, Expression, purification, and characterization of the dihydrolipoamide dehydrogenase-binding protein of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae, Biochemistry 33, 13801-13807 (1994).
    • (1994) Biochemistry , vol.33 , pp. 13801-13807
    • Maeng, C.-Y.1    Yazdi, M.A.2    Niu, X.-D.3    Lee, H.Y.4    Reed, L.J.5
  • 4
    • 0026772495 scopus 로고
    • Branchedchain α-ketoacid dehydrogenase kinase: Molecular cloning, expression, and sequence similarity with histidine protein kinases
    • 4. K. M. POPOV, Y. ZHAO, Y. SHIMOMURA, M. J. KUNTZ and R. A. HARRIS, Branchedchain α-ketoacid dehydrogenase kinase: molecular cloning, expression, and sequence similarity with histidine protein kinases, J. Biol. Chem. 267, 13127-13130 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 13127-13130
    • Popov, K.M.1    Zhao, Y.2    Shimomura, Y.3    Kuntz, M.J.4    Harris, R.A.5
  • 5
    • 0027452147 scopus 로고
    • Primary structure of pyruvate dehydrogenase kinase establishes a new family of eukaryotic protein kinases
    • 5. K. M. POPOV, N. Y. KEDISHVILI, Y. ZHAO, Y. SHIMOMURA, D. W. CRABB and R. A. HARRIS, Primary structure of pyruvate dehydrogenase kinase establishes a new family of eukaryotic protein kinases, J. Biol. Chem. 268, 26602-26606 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 26602-26606
    • Popov, K.M.1    Kedishvili, N.Y.2    Zhao, Y.3    Shimomura, Y.4    Crabb, D.W.5    Harris, R.A.6
  • 7
    • 0025608883 scopus 로고
    • Purification and partial characterization of branched chain α-ketoacid dehydrogenase kinase from rat liver and rat heart
    • 7. Y. SHIMOMURA, N. NANAUMI, M. SUZUKI, K. M. POPOV and R. A. HARRIS, Purification and partial characterization of branched chain α-ketoacid dehydrogenase kinase from rat liver and rat heart, Arch. Biochem. Biophys. 283, 293-299 (1990).
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 293-299
    • Shimomura, Y.1    Nanaumi, N.2    Suzuki, M.3    Popov, K.M.4    Harris, R.A.5
  • 8
    • 0026201364 scopus 로고
    • Purification and comparative study of the kinases specific for branched chain α-ketoacid dehydrogenase and pyruvate dehydrogenase
    • 8. K. M. POPOV, Y. SHIMOMURA and R. A. HARRIS, Purification and comparative study of the kinases specific for branched chain α-ketoacid dehydrogenase and pyruvate dehydrogenase, Protein Exp. Purif. 2, 278-286 (1991).
    • (1991) Protein Exp. Purif. , vol.2 , pp. 278-286
    • Popov, K.M.1    Shimomura, Y.2    Harris, R.A.3
  • 9
    • 0030052606 scopus 로고    scopus 로고
    • Structural organization of the rat branched-chain 2-oxo-acid dehydrogenase kinase gene and partial characterization of the promoter-regulatory region
    • 9. Y.-S. HUANG and D. T. CHUANG, Structural organization of the rat branched-chain 2-oxo-acid dehydrogenase kinase gene and partial characterization of the promoter-regulatory region, Biochem. J. 313, 603-609 (1996).
    • (1996) Biochem. J. , vol.313 , pp. 603-609
    • Huang, Y.-S.1    Chuang, D.T.2
  • 10
    • 0028149769 scopus 로고
    • Molecular cloning of the p45 subunit of pyruvate dehydrogenase kinase
    • 10. K. M. POPOV, N. Y. KEDISHVILI, Y. ZHAO, R. GUDI and R. A. HARRIS, Molecular cloning of the p45 subunit of pyruvate dehydrogenase kinase, J. Biol. Chem. 269, 29720-29724 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 29720-29724
    • Popov, K.M.1    Kedishvili, N.Y.2    Zhao, Y.3    Gudi, R.4    Harris, R.A.5
  • 11
    • 0028851739 scopus 로고
    • Diversity of the pyruvate dehydrogenase kinase gene family in humans
    • 11. R. GUDI, M. M. BOWKER-KINLEY, N. Y. KEDISHVILI, Y. ZHAO and K. M. POPOV, Diversity of the pyruvate dehydrogenase kinase gene family in humans, J. Biol. Chem. 270, 28989-28994 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 28989-28994
    • Gudi, R.1    Bowker-Kinley, M.M.2    Kedishvili, N.Y.3    Zhao, Y.4    Popov, K.M.5
  • 13
    • 0021099811 scopus 로고
    • Purification and properties of pyruvate dehydrogenase kinase from bovine kidney
    • 13. L. R. STEPP, F. H. PETTIT, S. J. YEAMAN and L. J. REED, Purification and properties of pyruvate dehydrogenase kinase from bovine kidney, J. Biol. Chem. 258, 9454-9458 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 9454-9458
    • Stepp, L.R.1    Pettit, F.H.2    Yeaman, S.J.3    Reed, L.J.4
  • 14
    • 0021199303 scopus 로고
    • Purification of the branched-chain α-ketoacid dehydrogenase phosphatase from bovine kidney mitochondria
    • 14. Z. DAMUNI, M. L. MERRYFIELD and L. J. REED, Purification of the branched-chain α-ketoacid dehydrogenase phosphatase from bovine kidney mitochondria, Proc. Natl Acad. Sci. U.S.A. 81, 4335-4338 (1984).
    • (1984) Proc. Natl Acad. Sci. U.S.A. , vol.81 , pp. 4335-4338
    • Damuni, Z.1    Merryfield, M.L.2    Reed, L.J.3
  • 15
    • 0023654352 scopus 로고
    • Purification and properties of the catalytic subunit of the branched-chain α-keto acid dehydrogenase phosphatase from bovine kidney mitochondria
    • 15. Z. DAMUNI and L. J. REED, Purification and properties of the catalytic subunit of the branched-chain α-keto acid dehydrogenase phosphatase from bovine kidney mitochondria. J. Biol. Chem. 262, 5129-5132 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 5129-5132
    • Damuni, Z.1    Reed, L.J.2
  • 16
    • 0022638937 scopus 로고
    • A potent, heat-stable inhibitor of branched-chain α-keto acid dehydrogenase-phosphatase from bovine kidney mitochondria
    • 16. Z. DAMUNI, J. S. HUMPHREYS and L. J. REED, A potent, heat-stable inhibitor of branched-chain α-keto acid dehydrogenase-phosphatase from bovine kidney mitochondria. Proc. Natl Acad. Sci. U.S.A. 83, 285-289 (1986).
    • (1986) Proc. Natl Acad. Sci. U.S.A. , vol.83 , pp. 285-289
    • Damuni, Z.1    Humphreys, J.S.2    Reed, L.J.3
  • 17
    • 0020491937 scopus 로고
    • Purification and properties of pyruvate dehydrogenase phosphatase from bovine heart and kidney
    • 17. W. M. TEAGUE, F. H. PETTIT, T.-L. WU, S. R. SILBERMAN and L. J. REED, Purification and properties of pyruvate dehydrogenase phosphatase from bovine heart and kidney, Biochemistry 21, 5585-5592 (1982).
    • (1982) Biochemistry , vol.21 , pp. 5585-5592
    • Teague, W.M.1    Pettit, F.H.2    Wu, T.-L.3    Silberman, S.R.4    Reed, L.J.5
  • 18
    • 0027861114 scopus 로고
    • Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydroge-nase phosphatase and sequence similarity with protein phosphatase 2C
    • 18. J. E. LAWSON, X.-D. NIU, K. S. BROWNING, H. LE TRONG, J. YAN and L. J. REED, Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydroge-nase phosphatase and sequence similarity with protein phosphatase 2C, Biochemistry 32, 8987-8993 (1993).
    • (1993) Biochemistry , vol.32 , pp. 8987-8993
    • Lawson, J.E.1    Niu, X.-D.2    Browning, K.S.3    Le Trong, H.4    Yan, J.5    Reed, L.J.6
  • 19
    • 0028277275 scopus 로고
    • Site-directed mutagenesis of phosphorylation sites of the branched chain α-ketoacid dehydrogenase complex
    • 19. Y. ZHAO, J. W. HAWES, K. M. POPOV, J. A. JASKIEWICZ, Y. SHIMOMURA, D. W. CRABB and R. A. HARRIS, Site-directed mutagenesis of phosphorylation sites of the branched chain α-ketoacid dehydrogenase complex, J. Biol. Chem. 269, 18583-18587 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 18583-18587
    • Zhao, Y.1    Hawes, J.W.2    Popov, K.M.3    Jaskiewicz, J.A.4    Shimomura, Y.5    Crabb, D.W.6    Harris, R.A.7
  • 20
    • 0029572459 scopus 로고
    • Roles of amino acid residues surrounding phosphorylation site I of branched-chain α-ketoacid dehydrogenase (BCKDH) in catalysis and phosphorylation site recognition by BCKDH kinase
    • 20. J. W. HAWES, R. J. SCHNEPF, A. E. JENKINS, Y. SHIMOMURA, K. M. POPOV and R. A. HARRIS, Roles of amino acid residues surrounding phosphorylation site I of branched-chain α-ketoacid dehydrogenase (BCKDH) in catalysis and phosphorylation site recognition by BCKDH kinase, J. Biol. Chem. 270, 31071-31076 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 31071-31076
    • Hawes, J.W.1    Schnepf, R.J.2    Jenkins, A.E.3    Shimomura, Y.4    Popov, K.M.5    Harris, R.A.6
  • 21
    • 0024269465 scopus 로고
    • Determination of activity and activity state of branched-chain α-keto acid dehydrogenase in rat tissues
    • 21. G. W. GOODWIN, B. ZHANG, R. PAXTON and R. A. HARRIS, Determination of activity and activity state of branched-chain α-keto acid dehydrogenase in rat tissues, Methods in Enzymology 166, 189-200 (1988).
    • (1988) Methods in Enzymology , vol.166 , pp. 189-200
    • Goodwin, G.W.1    Zhang, B.2    Paxton, R.3    Harris, R.A.4
  • 22
    • 0024230522 scopus 로고
    • Branched-chain α-keto acid dehydrogenase and its kinase from rabbit liver and heart
    • 22. R. PAXTON, Branched-chain α-keto acid dehydrogenase and its kinase from rabbit liver and heart, Methods in Enzymology 166, 313-320 (1988).
    • (1988) Methods in Enzymology , vol.166 , pp. 313-320
    • Paxton, R.1
  • 23
    • 0025783215 scopus 로고
    • Pyruvate decarboxylase from Zymomonas mobilis. Structure and re-activation of apoenzyme by the cofactors thiamin diphosphate and magnesium ion
    • 23. R. J. DIEFENBACH and R. G. DUGGLEBY, Pyruvate decarboxylase from Zymomonas mobilis. Structure and re-activation of apoenzyme by the cofactors thiamin diphosphate and magnesium ion, Biochem. J. 276, 439-445 (1991).
    • (1991) Biochem. J. , vol.276 , pp. 439-445
    • Diefenbach, R.J.1    Duggleby, R.G.2
  • 25
    • 0020486992 scopus 로고
    • Regulation of the branched-chain 2-oxoacid dehydrogenase kinase reaction
    • 25. K. S. LAU, H. R. FATANIA and P. J. RANDLE, Regulation of the branched-chain 2-oxoacid dehydrogenase kinase reaction, FEBS Lett. 144, 57-62 (1982).
    • (1982) FEBS Lett. , vol.144 , pp. 57-62
    • Lau, K.S.1    Fatania, H.R.2    Randle, P.J.3
  • 26
    • 0021344737 scopus 로고
    • Regulation of branched-chain α-ketoacid dehydrogenase kinase
    • 26. R. PAXTON and R. A. HARRIS, Regulation of branched-chain α-ketoacid dehydrogenase kinase, Arch. Biochem. Biophys. 231, 48-57 (1984).
    • (1984) Arch. Biochem. Biophys. , vol.231 , pp. 48-57
    • Paxton, R.1    Harris, R.A.2
  • 27
    • 0022541742 scopus 로고
    • Effects of low protein diet and starvation on the activity of branched-chain 2-oxoacid dehydrogenase kinase in rat liver and heart
    • 27. J. ESPINAL, M. BEGGS, H. PATEL and P. J RANDLE, Effects of low protein diet and starvation on the activity of branched-chain 2-oxoacid dehydrogenase kinase in rat liver and heart, Biochem. J. 237, 285-288 (1986).
    • (1986) Biochem. J. , vol.237 , pp. 285-288
    • Espinal, J.1    Beggs, M.2    Patel, H.3    Randle, P.J.4
  • 28
    • 0026652851 scopus 로고
    • Effects of clofibric acid on the activity and activity state of the hepatic branched-chain 2-oxo acid dehydrogenase complex
    • 28. Y. ZHAO, J. JASKIEWICZ and R. A. HARRIS, Effects of clofibric acid on the activity and activity state of the hepatic branched-chain 2-oxo acid dehydrogenase complex, Biochem. J. 285, 167-172 (1992).
    • (1992) Biochem. J. , vol.285 , pp. 167-172
    • Zhao, Y.1    Jaskiewicz, J.2    Harris, R.A.3
  • 31
    • 0023191890 scopus 로고
    • Temporal relationships in the effects of protein-free diet on the activities of rat liver branched-chain ketoacid dehydrogenase complex and kinase
    • 31. M. BEGGS, H. PATEL, J. ESPINAL and P. J. RANDLE, Temporal relationships in the effects of protein-free diet on the activities of rat liver branched-chain ketoacid dehydrogenase complex and kinase, FEBS Lett. 215, 13-15 (1987).
    • (1987) FEBS Lett. , vol.215 , pp. 13-15
    • Beggs, M.1    Patel, H.2    Espinal, J.3    Randle, P.J.4
  • 32
    • 0023850026 scopus 로고
    • Effects of dietary protein intake on branched-chain keto acid dehydrogenase activity of the rat
    • 32. R. H. MILLER, R. S. EISENSTEIN and A. E. HARPER, Effects of dietary protein intake on branched-chain keto acid dehydrogenase activity of the rat, J. Biol. Chem. 263, 3454-3461 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 3454-3461
    • Miller, R.H.1    Eisenstein, R.S.2    Harper, A.E.3
  • 33
    • 0020474907 scopus 로고
    • Activation of phosphorylated branched chain 2-oxoacid dehydrogenase complex
    • 33. H. R. FATANIA, K. S. LAU and P. J. RANDLE, Activation of phosphorylated branched chain 2-oxoacid dehydrogenase complex, FEBS Lett. 147, 35-39 (1982).
    • (1982) FEBS Lett. , vol.147 , pp. 35-39
    • Fatania, H.R.1    Lau, K.S.2    Randle, P.J.3
  • 34
    • 0021181211 scopus 로고
    • Effects of diet and of alloxan-diabetes on the activity of branched-chain 2-oxo acid dehydrogenase complex and of activator protein in rat tissues
    • 34. P. A. PATSTON, J. ESPINAL and P. J. RANDLE, Effects of diet and of alloxan-diabetes on the activity of branched-chain 2-oxo acid dehydrogenase complex and of activator protein in rat tissues, Biochem. J. 222, 711-719 (1984).
    • (1984) Biochem. J. , vol.222 , pp. 711-719
    • Patston, P.A.1    Espinal, J.2    Randle, P.J.3
  • 35
    • 0021770658 scopus 로고
    • Evidence that the mitochondrial activator of phosphorylated branched-chain 2-oxoacid dehydrogenase complex is the dissociated El component of the complex
    • 35. S. J. YEAMAN, K. G. COOK, R. W. BOYD and R. LAWSON, Evidence that the mitochondrial activator of phosphorylated branched-chain 2-oxoacid dehydrogenase complex is the dissociated El component of the complex, FEBS Lett. 172, 38-42 (1984).
    • (1984) FEBS Lett. , vol.172 , pp. 38-42
    • Yeaman, S.J.1    Cook, K.G.2    Boyd, R.W.3    Lawson, R.4
  • 36
    • 0021920168 scopus 로고
    • Purification and properties of a protein activator of phosphorylated branched-chain 2-oxo acid dehydrogenase complex
    • 36. J. ESPINAL, P. A. PATSTON, H. R. FATANIA, K. S. LAU and P. J. RANDLE, Purification and properties of a protein activator of phosphorylated branched-chain 2-oxo acid dehydrogenase complex, Biochem. J. 225, 509-516 (1985).
    • (1985) Biochem. J. , vol.225 , pp. 509-516
    • Espinal, J.1    Patston, P.A.2    Fatania, H.R.3    Lau, K.S.4    Randle, P.J.5
  • 37
    • 0021739250 scopus 로고
    • Regulation of bovine kidney branched-chain 2-oxoacid dehydrogenase complex by reversible phosphorylation
    • 37. K. G. COOK, A. P. BRADFORD, S. J. YEAMAN, A. AITKEN, I. M. FEARNLEY and J. E. WALKER, Regulation of bovine kidney branched-chain 2-oxoacid dehydrogenase complex by reversible phosphorylation, Eur. J. Biochem. 145, 586-591 (1984).
    • (1984) Eur. J. Biochem. , vol.145 , pp. 586-591
    • Cook, K.G.1    Bradford, A.P.2    Yeaman, S.J.3    Aitken, A.4    Fearnley, I.M.5    Walker, J.E.6
  • 38
    • 0022586416 scopus 로고
    • Phosphorylation sites and inactivation of branched-chain α-ketoacid dehydrogenase isolated from rat heart, bovine kidney, and rabbit liver, kidney, heart, brain, and skeletal muscle
    • 38. R. PAXTON, M. J. KUNTZ and R. A. HARRIS, Phosphorylation sites and inactivation of branched-chain α-ketoacid dehydrogenase isolated from rat heart, bovine kidney, and rabbit liver, kidney, heart, brain, and skeletal muscle, Arch. Biochem. Biophys. 244, 197-201 (1986).
    • (1986) Arch. Biochem. Biophys. , vol.244 , pp. 197-201
    • Paxton, R.1    Kuntz, M.J.2    Harris, R.A.3
  • 39
    • 0027265567 scopus 로고
    • The relationships between transketolase, yeast pyruvate decarboxylase and pyruvate dehydrogenase of the pyruvate dehydrogenase complex
    • 39. B. H. ROBINSON and K. CHUN, The relationships between transketolase, yeast pyruvate decarboxylase and pyruvate dehydrogenase of the pyruvate dehydrogenase complex, FEBS Lett. 328, 99-102 (1993).
    • (1993) FEBS Lett. , vol.328 , pp. 99-102
    • Robinson, B.H.1    Chun, K.2
  • 40
    • 0028305456 scopus 로고
    • Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution
    • 40. M. NIKKOLA, Y. LINDQVIST and G. SCHNEIDER, Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution, J. Mol. Biol. 238, 387-404 (1994).
    • (1994) J. Mol. Biol. , vol.238 , pp. 387-404
    • Nikkola, M.1    Lindqvist, Y.2    Schneider, G.3
  • 41
    • 0029967678 scopus 로고    scopus 로고
    • Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 Å resolution
    • 41. P. AJURNAN, T. UMLAND, F. DYDA, S. SWAMINATHAN, W. FUREY, M. SAX, B. FARRENKOPF, Y. GAO, D. ZHANG and F. JORDAN, Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 Å resolution, J. Mol. Biol. 256, 590-600 (1996).
    • (1996) J. Mol. Biol. , vol.256 , pp. 590-600
    • Ajurnan, P.1    Umland, T.2    Dyda, F.3    Swaminathan, S.4    Furey, W.5    Sax, M.6    Farrenkopf, B.7    Gao, Y.8    Zhang, D.9    Jordan, F.10
  • 42
    • 0027479683 scopus 로고
    • Structure of the thiamine and flavin-dependent enzyme pyruvate oxidase
    • 42. Y. A. MULLER and G. A. SCHULZ, Structure of the thiamine and flavin-dependent enzyme pyruvate oxidase, Science 259, 965-967 (1993).
    • (1993) Science , vol.259 , pp. 965-967
    • Muller, Y.A.1    Schulz, G.A.2
  • 43
    • 0024432768 scopus 로고
    • A common structural motif in thiamin pyrophosphate-binding enzymes
    • 43. C. F. HAWKINS, A. BORGES and R. N. PERLMAN, A common structural motif in thiamin pyrophosphate-binding enzymes, FEBS Lett. 255, 77-82 (1989).
    • (1989) FEBS Lett. , vol.255 , pp. 77-82
    • Hawkins, C.F.1    Borges, A.2    Perlman, R.N.3
  • 44
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • 44. R. B. PEARSON and B. E. KEMP, Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations, Meth. Enzymology 200, 62-81 (1991).
    • (1991) Meth. Enzymology , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 46
    • 0021713737 scopus 로고
    • Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (type-2)
    • 46. F. MEGGIO, F. MARCHIORI, G. BORIN, G. CHESSA and L. A. PINNA, Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (type-2), J. Biol. Chem. 259, 14576-14579 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 14576-14579
    • Meggio, F.1    Marchiori, F.2    Borin, G.3    Chessa, G.4    Pinna, L.A.5
  • 47
    • 0026495331 scopus 로고
    • Three-dimensional structure of apotransketolase. Flexible loops at the active site enable cofactor binding
    • 47. M. SUNDSTRÖM, Y. LINDQVIST and G. SCHNEIDER, Three-dimensional structure of apotransketolase. Flexible loops at the active site enable cofactor binding, FEBS Lett 313, 229-231 (1992).
    • (1992) FEBS Lett , vol.313 , pp. 229-231
    • Sundström, M.1    Lindqvist, Y.2    Schneider, G.3
  • 48
    • 0027401242 scopus 로고
    • Mutations in the X-linked E1α subunit of pyruvate dehydrogenase leading to deficiency of the pyru-vate dehydrogenase complex
    • 48. K. CHUN, N. MACKAY, R. PETROVA-BENEDICT and B. H. ROBINSON, Mutations in the X-linked E1α subunit of pyruvate dehydrogenase leading to deficiency of the pyru-vate dehydrogenase complex, Hum. Mol. Genet. 2, 449-454 (1993).
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 449-454
    • Chun, K.1    MacKay, N.2    Petrova-Benedict, R.3    Robinson, B.H.4
  • 49
    • 0028927142 scopus 로고
    • The effect of phosphorylation on pyruvate dehydrogenase
    • 49. L. G. KOROTCHKINA, L. S. KHAILOVA and S. E. SEVERIN, The effect of phosphorylation on pyruvate dehydrogenase, FEBS Lett. 364, 185-188 (1995).
    • (1995) FEBS Lett. , vol.364 , pp. 185-188
    • Korotchkina, L.G.1    Khailova, L.S.2    Severin, S.E.3
  • 50
    • 0015518633 scopus 로고
    • Function of the nonidentical subunits of mammalian pyruvate dehydrogenase
    • 50. T. W. ROCHE and L. J. REED, Function of the nonidentical subunits of mammalian pyruvate dehydrogenase, Biochem. Biophys. Res. Commun. 48, 840-846 (1972).
    • (1972) Biochem. Biophys. Res. Commun. , vol.48 , pp. 840-846
    • Roche, T.W.1    Reed, L.J.2
  • 51
    • 0017115996 scopus 로고
    • The elementary reactions of the pig heart pyruvate dehydrogenase complex. A study of the inhibition by phosphorylation
    • 51. D. A. WALSH, R. H. COOPER, T. M. DENTON, B. J. BRIDGES and P. J. RANDLE, The elementary reactions of the pig heart pyruvate dehydrogenase complex. A study of the inhibition by phosphorylation, Biochem. J. 157, 41-67 (1976).
    • (1976) Biochem. J. , vol.157 , pp. 41-67
    • Walsh, D.A.1    Cooper, R.H.2    Denton, T.M.3    Bridges, B.J.4    Randle, P.J.5
  • 52
    • 0017623915 scopus 로고
    • Binding of thiamin pyrophosphate to mammalian pyruvate dehydrogenase and its effects on kinase and phosphatase activities
    • 52. J. R. BUTLER, F. H. PETTIT, P. F. DAVIS and L. J. REED, Binding of thiamin pyrophosphate to mammalian pyruvate dehydrogenase and its effects on kinase and phosphatase activities, Biochem. Biophys. Res. Commun. 74, 1667-1674 (1977).
    • (1977) Biochem. Biophys. Res. Commun. , vol.74 , pp. 1667-1674
    • Butler, J.R.1    Pettit, F.H.2    Davis, P.F.3    Reed, L.J.4
  • 53
    • 0022456123 scopus 로고
    • Kinase activator protein mediates longer-term effects of starvation on activity of pyruvate dehydrogenase kinase in rat liver mitochondria
    • 53. G. S. DENYER, A. L. KERBEY and P. J. RANDLE, Kinase activator protein mediates longer-term effects of starvation on activity of pyruvate dehydrogenase kinase in rat liver mitochondria, Biochem. J. 239, 347-354 (1986).
    • (1986) Biochem. J. , vol.239 , pp. 347-354
    • Denyer, G.S.1    Kerbey, A.L.2    Randle, P.J.3
  • 54
    • 0026510610 scopus 로고
    • Effects of recombinant monokines on hepatic pyruvate dehydrogenase, pyruvate dehydrogenase kinase, lipogenesis de novo and plasma triacylglycerols abolition by prior fasting
    • 54. K. BLACKHAM, D. CESAR, O.-J. PARK, T. C. VARY, K. WU, S. KAEMPFER, C. H. L. SHACKLETON and M. K. HELLERSTEIN, Effects of recombinant monokines on hepatic pyruvate dehydrogenase, pyruvate dehydrogenase kinase, lipogenesis de novo and plasma triacylglycerols abolition by prior fasting, Biochem. J. 284, 129-135 (1992).
    • (1992) Biochem. J. , vol.284 , pp. 129-135
    • Blackham, K.1    Cesar, D.2    Park, O.-J.3    Vary, T.C.4    Wu, K.5    Kaempfer, S.6    Shackleton, C.H.L.7    Hellerstein, M.K.8
  • 55
    • 0027520571 scopus 로고
    • Mechanisms involved in the coordinate regulation of strategic enzymes of glucose metabolism
    • 55. M. G. SUGDEN, R. M. HOWARD, M. R. MUNDAY and M. J. HOLNESS, Mechanisms involved in the coordinate regulation of strategic enzymes of glucose metabolism, Advan. Enzyme Regulation 33, 71-95 (1993).
    • (1993) Advan. Enzyme Regulation , vol.33 , pp. 71-95
    • Sugden, M.G.1    Howard, R.M.2    Munday, M.R.3    Holness, M.J.4
  • 56
    • 0026648391 scopus 로고
    • Purification and partial characterization of rat liver pyruvate dehydrogenase kinase activator protein (free pyruvate dehydrogenase kinase)
    • 56. D. A. PRIESTMAN, S. C. MISTRY, A. L. KERBEY and P. J. RANDLE, Purification and partial characterization of rat liver pyruvate dehydrogenase kinase activator protein (free pyruvate dehydrogenase kinase), FEBS Lett. 308, 83-86 (1992).
    • (1992) FEBS Lett. , vol.308 , pp. 83-86
    • Priestman, D.A.1    Mistry, S.C.2    Kerbey, A.L.3    Randle, P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.