Long-range interaction between the enzyme active site and a distant allosteric site in the human mitochondrial NAD(P)+-dependent malic enzyme

Archives of Biochemistry and Biophysics

Volumn 487, Issue 1, 2009, Pages 19-27

  Hsieh, Ju Yi ^a   Su, Kuo Liang ^a   Ho, Pei Tzu ^a   Hung, Hui Chih ^a  

^a NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

Author keywords

Allosteric regulation; Binding energy; Coupling energy; Double mutant cycle; Enzyme kinetics; Free energy; Malic enzyme; Mutagenesis

Indexed keywords

ARGININE; ASPARTIC ACID; FUMARIC ACID; MALATE DEHYDROGENASE (NADP);

ALLOSTERISM; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; GENE MUTATION; GENETIC CONSERVATION; HUMAN; MITOCHONDRION; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; SPECTROFLUOROMETRY; ULTRACENTRIFUGATION;

ALLOSTERIC SITE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARGININE; ASPARTIC ACID; BASE SEQUENCE; CATALYTIC DOMAIN; DNA PRIMERS; FUMARATES; HUMANS; KINETICS; MALATE DEHYDROGENASE; MITOCHONDRIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STATIC ELECTRICITY; THERMODYNAMICS;

EID: 67249103356     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.05.007     Document Type: Article

References (48)

1. Frenkel R. Curr. Top. Cell. Regul. 9 (1975) 157-181
2. Hsu R.Y. Mol. Cell. Biochem. 43 (1982) 3-26
3. Loeber G., Infante A.A., Maurer-Fogy I., Krystek E., and Dworkin M.B. J. Biol. Chem. 266 (1991) 3016-3021
4. Rao G.S., Coleman D.E., Kulkarni G., Goldmith E.J., Cook P.F., and Harris B.G. Protein Pept. Lett. 7 (2000) 297-304
5. Cleland W.W. Protein Pept. Lett. 7 (2000) 305-312
6. Liu D., Hwang C.C., and Cook P.F. Biochemistry 41 (2002) 12200-12203
7. Hung H.C., Chang G.G., Yang Z., and Tong L. Biochemistry 39 (2000) 14095-14102
8. Loeber G., Dworkin M.B., Infante A., and Ahorn H. FEBS Lett. 344 (1994) 181-186
9. Chang G.G., Wang J.K., Huang T.M., Lee H.J., Chou W.Y., and Meng C.L. Eur. J. Biochem. 202 (1991) 681-688
10. Chang G.G., Huang T.M., Wang J.K., Lee H.J., Chou W.Y., and Meng C.L. Arch. Biochem. Biophys. 296 (1992) 468-473
11. Loeber G., Maurer-Fogy I., and Schwendenwein R. Biochem. J. 304 (1994) 687-692
12. Mandella R.D., and Sauer L.A. J. Biol. Chem. 250 (1975) 5877-5884
13. Zolnierowicz S., Swierczynski J., and Zelewski L. Biochem. Med. Metab. Biol. 39 (1988) 208-216
14. Kuo C.C., Tsai L.C., Chin T.Y., Chang G.G., and Chou W.Y. Biochem. Biophys. Res. Commun. 270 (2000) 821-825
15. Hsieh J.Y., Liu G.Y., Chang G.G., and Hung H.C. J. Biol. Chem. 281 (2006) 23237-23245
16. Yang Z., Lanks C.W., and Tong L. Structure 10 (2002) 951-960
17. Hsu W.C., Hung H.C., Tong L., and Chang G.G. Biochemistry 43 (2004) 7382-7390
18. Hung H.C., Chien Y.C., Hsieh J.Y., Chang G.G., and Liu G.Y. Biochemistry 44 (2005) 12737-12745
19. Sauer L.A., Dauchy R.T., Nagel W.O., and Morris H.P. J. Biol. Chem. 255 (1980) 3844-3848
20. Baggetto L.G. Biochimie 74 (1992) 959-974
21. Sanz N., Diez-Fernandez D., Valverde A.M., Lorenzo M., Benito M., and Cascales M. Br. J. Cancer 75 (1997) 487-492
22. Moreadith R.W., and Lehninger A.L. J. Biol. Chem. 259 (1984) 6215-6221
23. Moreadith R.W., and Lehninger A.L. J. Biol. Chem. 259 (1984) 6222-6227
24. Fahien L.A., and Teller J.K. J. Biol. Chem. 267 (1992) 10411-10422
25. Mckeehan W.L. Cell Biol. Int. Rep. 6 (1982) 635-650
26. Xu Y., Bhargava G., Wu H., Loeber G., and Tong L. Structure 7 (1999) 877-889
27. Yang Z., Floyd D.L., Loeber G., and Tong L. Nat. Struct. Biol. 7 (2000) 251-257
28. Yang Z., Zhang H., Hung H.C., Kuo C.C., Tsai L.C., Yuan H.S., Chou W.Y., Chang G.G., and Tong L. Protein Sci. 11 (2002) 332-341
29. Coleman D.E., Rao G.S., Goldsmith E.J., Cook P.F., and Harris B.G. Biochemistry 41 (2002) 6928-6938
30. Tao X., Yang Z., and Tong L. Structure 11 (2003) 1141-1150
31. Chang G.G., and Tong L. Biochemistry 42 (2003) 12721-12733
32. Rao G.S., Coleman D.E., Karsten W.E., Cook P.F., and Harris B.G. J. Biol. Chem. 278 (2003) 38051-38058
33. Landsperger W.J., and Harris B.G. J. Biol. Chem. 251 (1976) 3599-3602
34. Lai C.J., Harris B.G., and Cook P.F. Arch. Biochem. Biophys. 299 (1992) 214-219
35. Karsten W.E., Pais J.E., Rao G.S., Harris B.G., and Cook P.F. Biochemistry 42 (2003) 9712-9721
36. Hung H.C., Kuo M.W., Chang G.G., and Liu G.Y. Biochem. J. 392 (2005) 39-45
37. Bhargava G., Mui S., Pav S., Wu H., Loeber G., and Tong L. J. Struct. Biol. 127 (1999) 72-75
38. Bradford M.M. Anal. Biochem. 72 (1976) 248-254
39. Segel I.H. Enzyme Kinetics (1975), John Wiley & Sons, New York pp. 227-272
40. Schuck P., Perugini M.A., Gonzales N.R., Howlett G.J., and Schubert D. Biophys. J. 82 (2002) 1096-1111
41. Schuck P. Anal. Biochem. 320 (2003) 104-124
42. +-dependent malic enzyme. FEBS J. 276 (2009) 983-994
43. Chou W.Y., Chang H.P., Huang C.H., Kuo C.C., Tong L., and Chang G.G. Protein Sci. 9 (2000) 242-251
44. Chen Y.I., Chen Y.H., Chou W.Y., and Chang G.G. Biochem. J. 374 (2003) 633-637
45. Faiman G.A., and Horovitz A. Protein Eng. 9 (1996) 315-316
46. Altschul S.F., Boguski M.S., Gish W., and Wootton J.C. Nat. Genet. 6 (1994) 119-129
47. Thompson J.D., Higgins D.G., and Gibson T.J. Nucleic Acids Res. 22 (1994) 4673-4680
48. Wallace A.C., Laskowski R.A., and Thornton J.M. Protein Eng. 8 (1995) 127-134