Unique holoenzyme dimers of the tetrameric enzyme Escherichia coli methylenetetrahydrofolate reductase: Characterization of structural features associated with modulation of the enzyme's function

Biochemistry

Volumn 42, Issue 13, 2003, Pages 3921-3928

  Misra, Sandeep K ^a   Bhakuni, Vinod ^a  

^a CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOVASCULAR DISEASES;

CARDIOVASCULAR SYSTEM; DIMERS; ELECTROSTATICS; PLASMA APPLICATIONS;

ESCHERICHIA COLI;

5,10 METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); DIMER; FLAVINE ADENINE NUCLEOTIDE; HOLOENZYME; MONOMER; SODIUM CHLORIDE; TETRAMER; UREA;

ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; CORRELATION ANALYSIS; DISSOCIATION; ELECTRICITY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME REGULATION; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING;

BACTERIAL PROTEINS; CHLORATES; CIRCULAR DICHROISM; CROSS-LINKING REAGENTS; DIMERIZATION; ENZYME STABILITY; ESCHERICHIA COLI; FLAVIN-ADENINE DINUCLEOTIDE; GLUTARAL; HEAT; HOLOENZYMES; HUMANS; METHYLENETETRAHYDROFOLATE REDUCTASE (NADPH2); MUTATION; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PLASMIDS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP; UREA;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0037426371     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0340200     Document Type: Article

References (22)

1. Refsum, H., Ueland, P. M., Nygard, O., and Vollset, S. (1998) Annu. Rev. Med. 49, 31-62.
2. Mills, J. L., Scott, J. M., Kirke, P. N., McPartlin, J. M., Conley, M. R., Weir, D. G., Molloy, A. M., and Lee, Y. J. (1996) J. Nutr. 126, 756-760.
3. Ashfield-Watt, P. A., Maot, S. J., Doshi, S. N., and McDowell, I. F. (2001) Biomed. Pharmacother. 55, 425-433.
4. van der Put, N. M., van Straaten, H. W., Trijbels, F. J., and Blom, H. J. (2001) Exp. Biol. Med. 226, 243-270.
5. Trimmer, F. E., Ballou, D. P., Ludwig, M. L., and Matthews, R. G. (2001) Biochemistry 40, 621-626.
6. Verhoef, P., Kok, F. J., Kluijtmens, L. A., Blom, H. J., Refsum, H., Ueland, P. M., and Kruyssen, D. A. (1997) Atherosclerosis 132, 105-13.
7. Cortese, C., and Motti, C. (2001) Public Health Nutr. 4, 493-497.
8. Guenther, B. D., Sheppard, C. A., Tran, P., Rozen, R., Matthews, R. G., and Ludwig, M. L. (1999) Nat. Struct. Biol. 6, 359-365.
9. Daubner, S. C., and Matthews, R. G. (1982) J. Biol. Chem. 257, 140-145.
10. Yamada, K., Chen, Z., Rozen, R., and Matthews, R. G. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 14853-14858.
11. Goyotte, P., Summer, J. S., Milos, R., Duncan, A. M. V., Rosenblatt, D. S., Matthews, R. G., and Rozen, R. (1994) Nat. Genet. 7, 195-200.
12. Sheppard, C. A., Trimmer, E. E., and Matthews, R. G. (1999) J. Bacteriol. 181, 718-725.
13. Sumner, J., Jenks, D. A., Khani, S., and Matthews, R. G. (1986) J. Biol. Chem. 261, 7697-7700.
14. Laemmli, U. K. (1970) Nature 227, 680-685.
15. Matthews, R. G. (1986) Methods Enzymol. 122, 372-381.
16. Ghisla, S., Massey, V., Lhoste, J. M., and Mayhew, S. (1974) Biochemistry 13, 589-597.
17. Bastieans, P. I., van Hoek, A., van Berkel, J. H., de Kok, A., and Visser, A. J. W. G. (1992) Biochemistry 31, 7061-7068.
18. Visser, A. J. W. G., Berkel, W. J. H., and deKok, A. (1995) Biochim. Biophys. Acta 1229, 381-385.
19. Ahmad, A., Akhtar, Md. S., and Bhakuni, V. (2001) Biochemistry 40, 1947-1955.
20. Akhtar, Md. S., Ahmad, A., and Bhakuni, V. (2002) Biochemistry 41, 3819-3827.
21. Trimmer, E. E., Ballou, D. P., Ludwig, M. L., and Matthews, R. G. (2001) Biochemistry 40, 6216-6226.
22. Sumner, J. S., and Matthews, R. G. (1992) J. Am. Chem. Soc. 114, 6949-6956.