Evaluation of types of interactions in subunit association in Bacillus subtilis adenylosuccinate lyase

Biochemistry

Volumn 47, Issue 9, 2008, Pages 2923-2934

  Ariyananda, Lushanti De Zoysa ^a   Colman, Roberta F ^a  

^a UNIVERSITY OF DELAWARE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION REACTIONS; CATALYST ACTIVITY; HYDROPHOBICITY; MONOMERS; MUTAGENESIS; OLIGOMERS;

ENZYME DISSOCIATES; HOMOTETRAMERS; OLIGOMERIC STRUCTURE; ULTRACENTRIFUGATION;

ENZYME KINETICS;

ADENYLOSUCCINATE LYASE;

ARTICLE; BACILLUS SUBTILIS; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBUNIT; HYDROPHOBICITY; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; ULTRACENTRIFUGATION;

ADENYLOSUCCINATE LYASE; BACILLUS SUBTILIS; CIRCULAR DICHROISM; COMPUTER SIMULATION; DIMERIZATION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; TEMPERATURE;

BACILLUS SUBTILIS;

EID: 40149109878     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701400c     Document Type: Article

References (26)

1. Ratner, S. (1972) Argininosuccinases and adenylosuccinases, in The Enzymes (Boyer, P. D., Ed.) 3rd ed., Vol. 7, pp 167-197, Academic Press, New York.
2. Hanson, K. R., and Havir, E. A. (1972) The enzymatic elimination of ammonia, in The Enzymes (Boyer, P. D., Ed.) 3rd ed., Vol. 7, pp 75-166, Academic Press, New York.
3. 141 in the active site of Bacillus subtilis adenylosuccinate lyase by affinity labeling with 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5′-monophosphate. J. Biol. Chem. 272, 458-465.
4. 68 in the substrate site of Bacillus subtilis adenylosuccinate lyase by mutagenesis and affinity labeling with 2-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5′-monophosphate. Biochemistry 37, 8481-8489.
5. 141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis. Biochemistry 38, 22-32.
6. 89 of adenylosuccinate lyase of Bacillus subtilis. Biochemistry 39, 13336-13343.
7. 275 are required. Biochemistry 41, 2217-2226.
8. Palenchar, J. B., and Colman, R. F. (2003) Characterization of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase deficiency: Asparagine 276 plays an important structural role. Biochemistry 42, 1831-1841.
9. 301 are critical for catalysis by adenylosuccinate lyase. Biochemistry 43, 7391-7402.
10. De Zoysa Ariyananda, L., and Colman, R. F. (2007) FASEB J. 21, A641.
11. Redinbo, M. R., Eide, S. M., Stone, R. L., Dixon, J. E., and Yeates, T. O. (1996) Crystallization and preliminary structural analysis of Bacillus subtilis adenylosuccinate lyase, an enzyme implicated in infantile autism. Protein Sci. 5, 786-788.
12. Tornheim, K., and Lowenstein, J. M. (1972) The purine nucleotide cycle: The production of ammonia from aspartate by extracts of rat skeletal muscle. J. Biol. Chem. 247, 162-169.
13. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
14. Hearne, J. L., and Colman, R. F. (2006) Catalytically active monomer of class Mu glutathione transferase from rat. Biochemistry 45, 5974-5984.
15. SEDPHAT program Home Page (http://www.analyticalultracentrifugation.com/ sedphat/sedphat.htm).
16. Laue, T., Shaw, B. D., Ridgeway, T. M., and Pelletier, S. L. (1992) in Biochemistry and Polymer Science (Harding, S. E., Rowe, A., and Horton, J. C., Eds.) pp 90-125, Royal Society of Chemistry, Cambridge, U.K.
17. Toth, E. A., and Yeates, T. O. (2000) The structure of adenylosuccinate lyase, an enzyme with dual acitivity in the de novo purine biosynthesis pathway. Structure 8, 163-174.
18. Rodriguez-Zavala, J., and Weiner, H. (2002) Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation. Biochemistry 41, 8229-8237.
19. Jencks, W. P. (1969) Electrostatic interactions, in Catalysis in Chemistry and Enzymology (Hume, D. N., Stork, G., King, E. L., Herschbach, D. R., and Pople, J. A., Eds.) pp 351-392, McGraw-Hill, New York.
20. Oakenfull, D., and Fenwick, D. E. (1977) Thermodynamics and mechanism of hydrophobic interaction. Aust. J. Chem. 30, 741-752.
21. Southall, N. T., Dill, K. A., and Haymet, A. D. J. (2002) A view of the hydrophobic effect. J. Phys. Chem. B 106, 521-533.
22. Ramos, C. H. I., and Baldwin, R. L. (2002) Sulfate anion stabilization of native ribonuclease A both by anion binding and by Hofmeister effect. Protein Sci. 11, 1771-1778.
23. Perez-Jimenez, R., Godoy-Ruiz, R., Ibarra-Molero, B., and Sanchez-Ruiz, J. M. (2004) The efficiency of different salts to screen charge interactions in proteins: a Hofmeister effect? Biophys. J. 86, 2414-2429.
24. Van den Berghe, G., and Jaeken, J. (2001) Adenylosuccinate lyase deficiency, in The Metabolic and Molecular Basis of Inherited Diseases (Scriver, C. R., Beaudt, A. L., Valle, D., Sly, W. S., Childs, B., Kinzler, K. W., and Vogelstein, B., Eds.) 8th ed., Vol. II, pp 2653-2662, McGraw-Hill, New York.
25. Adenylosuccinate Lyase Mutations Database Home Page (http://www.icp.ucl. ac.be/adsldb/mutations.html).
26. Spiegel, E. K., Colman, R. F., and Patterson, D. (2006) Adenylosuccinate lyase deficiency. Mol. Genet. Metab. 89, 19-31.