Biochemical and biophysical analysis of five disease-associated human adenylosuccinate lyase mutants

Biochemistry

Volumn 48, Issue 23, 2009, Pages 5291-5302

  Ariyananda, Lushanti De Zoysa ^a   Lee, Peychii ^a   Antonopoulos, Christina ^a   Colman, Roberta F ^a  

^a UNIVERSITY OF DELAWARE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BIOPHYSICAL ANALYSIS; CATALYTIC FUNCTIONS; CONFORMATIONAL CHANGE; COOPERATIVITY; ENZYMATIC ACTIVITIES; HOMOTETRAMER; IN-VITRO; KEY REACTIONS; MENTAL RETARDATION; METABOLIC DISEASE; MUTANT ENZYMES; NATIVE CONFORMATION; PROTEIN FLUORESCENCE; SINGLE MUTATION; SPECIFIC ACTIVITY; SUBUNIT INTERFACES; TETRAMER;

BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; CATALYSTS; CONFORMATIONS; ENZYMES;

ENZYME ACTIVITY;

ADENYLOSUCCINATE LYASE; MUTANT PROTEIN;

ADENYLOSUCCINATE LYASE DEFICIENCY; ARTICLE; CATALYSIS; CHEMICAL ANALYSIS; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME DEFICIENCY; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE SPECTROSCOPY; GEL FILTRATION CHROMATOGRAPHY; HUMAN; MOLECULAR GENETICS; MOLECULAR WEIGHT; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PURINE SYNTHESIS; SITE DIRECTED MUTAGENESIS; ULTRACENTRIFUGATION;

ADENYLOSUCCINATE LYASE; AUTISTIC DISORDER; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; HUMANS; KINETICS; MENTAL RETARDATION; MODELS, MOLECULAR; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; TEMPERATURE;

EID: 67049155773     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802321m     Document Type: Article

References (38)

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. Bridger, W. A., and Cohen, L. H. (1968) The kinetics of adenylosuccinate lyase. J. Biol. Chem. 243, 644-650.
3. Bulusu, V., Srinivasan, B., Bopanna, M. P., and Balaram, H. (2009) Elucidation of the substrate specificity, kinetic and catalytic mechanism of adenylosuccinate lyase from Plasmodium falciparum. Biochim. Biophys. Acta 1794, 642-654.
4. Wu, C.-Y., Lee, H.-J., Wu, S.-H., Chen, S.-T., Chiou, S.-H., and Chang, G.-G. (1998) Chemical mechanism of the endogenous arginosuccinate lyase activity of duck lens ä2-crystallin. Biochem. J. 333, 327-334. (Pubitemid 28379533)
5. Nuiry, I., Hermes, J. D., Weiss, P. M., Chen, C.-Y., and Cook, P. F. (1984) Kinetic mechanism and location of rate-determining steps for aspartase from Hafnia alvei. Biochemistry 23, 5168-5175.
6. 275 are required. Biochemistry 41, 2217-2226.
7. Sivendran, S., and Colman, R. F. (2008) Effect of a new non-cleavable substrate analog on wild-type and serine mutants in the signature sequence of adenylosuccinate lyase of Bacillus subtilis and Homo sapiens. Protein Sci. 17, 1162-1174. (Pubitemid 351930914)
8. Stenmark, P., Moche, M., Arrowsmith, C., Berglund, H., Busam, R., Collines, R., Dahlgren, L. G., Edwards, A., Flodin, S., Flores, A., et al. Human adenylosuccinate lyase in complex with its substrate N6-(1,2-dicarboxy-ethyl)- AMP, and its products AMP and fumarate, RCSB Protein Data Bank 2VD6.
9. Mouchegh, K., Zikanova, M., Hoffmann, G. F., Kretzschmar, B., Kuhn, T., Mildenberger, E., Stoltenburg-Didinger, G., Krijt, J., Dvorakova, L., Honzik, T., Zeman, J., Kmoch, S., and Rossi, R. (2007) Lethal fetal and early neonatal presentation of adenylosuccinate lyase deficiency: Observation of 6 Patients in 4 Families. J. Pediatr. 150, 57-61. (Pubitemid 44940889)
10. Jaeken, J., and Van den Berghe, G. (1984) An infantile autistic syndrome characterized by the presence of succinylpurines in body fluids. Lancet II, 1058-1061. (Pubitemid 15211523)
11. Jaeken, J., Wadman, S. K., Duran, M., Van Sprang, F. J., Beemer, F. A., Holl, R. A., Theunissen, P. M., de Cock, P., Van den Bergh, F., Vincent, M. F., and Van den Berghe, G. (1988) Adenylosuccinase deficiency: An inborn error of purine nucleotide synthesis. Eur. J. Pediatr. 148, 126-131.
12. Adenylosuccinate Lyase Mutations Database Home Page (http://www.icp.ucl. ac.be/adsldb/mutations.html).
13. Speigel, E. K., Colman, R. F., and Patterson, D. (2006) Adenylosuccinate lyase deficiency. Mol. Genet. Metab. 89, 19-31.
14. 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.
15. Lee, P., and Colman, R. F. (2007) Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyase. Protein Expression Purif. 51, 227-234. (Pubitemid 44821871)
16. Laemmli, U. K. (1970) Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
17. 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.
18. 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. (Pubitemid 36258657)
19. Riddles, P. W., Blakeley, R. L., and Zerner, B. (1979) Ellman's reagent: 5,5′-Dithiobis(2-nitrobenzoic acid): A reexamination. Anal. Biochem. 94, 75-81.
20. Hearne, J. L., and Colman, R. F. (2006) Catalytically active monomer of class Mu glutathione transferase from rat. Biochemistry 45, 5974-5984. (Pubitemid 43727089)
21. SEDPHAT program Home Page (http://www.analyticalultracentrifugation.com/ sedphat/sedphat.htm).
22. Laue, T. M., Shah, B. D., Ridgeway, T. M., and Pelletier, S. L. (1992) Computer-aided interpretation of analytical sedimentation data for proteins, in Analytical Ultracentrifugation 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.
23. 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.
24. Schmidt, B., Ho, L., and Hogg, P. J. (2006) Allosteric disulfide bonds. Biochemistry 45, 7429-7433. (Pubitemid 43894936)
25. Vivian, J. T., and Callis, P. R. (2001) Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 80, 2093-2109. (Pubitemid 32401976)
26. Sanchez, K. M., Gable, J. E., Schlmadinger, D. E., and Kim, J. E. (2008) Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: Lessons from the transmembrane protein OmpA. Biochemistry 47, 12844-12857.
27. Lienqueo, M. E., Mahn, A., and Asenjo, J. A. (2002) Mathematical correlations for predicting protein retention times in hydrophobic interaction chromatography. J. Chromatogr. A 978, 71-79. (Pubitemid 35292306)
28. Martorana, V., Bulone, D., San Biagio, P. L., Palma-Vittorelli, M. B., and Palma, M. U. (1997) Collective properties of hydration: Long range and specificity of hydrophobic interactions. Biophys. J. 73, 31-37. (Pubitemid 27274101)
29. Zhao, H. (2006) Viscosity B-coefficients and standard partial molar volumes of amino acids, and their roles in interpreting the protein (enzyme) stabilization. Biophys. Chem. 122, 157-183.
30. Hildebrandt, A., Blossey, R., Rjasanow, S., Kohlbacher, O., and Lenhof, H.-P. (2006) Electrostatic potentials of proteins in water: A structured continuum approach. Bioinformatics 23, e99-e103.
31. Chen, Y., and Barkley, M. D. (1998) Toward understanding tryptophan fluorescence in proteins. Biochemistry 37, 9976-9982. (Pubitemid 28366351)
32. Hernández-Alcántara, G., Rodríguez-Romero, A., Reyes-Vivas, H., Peon, J., Cabrera, N., Ortiz, C., Enríquez-Flores, S., De la Mora-De la Mora, I., and López-Velázquez, G. (2008) Unraveling the mechanism of tryptophan fluorescence quenching in the triosephosphate isomerase from Giardia lamblia. Biochim. Biophys. Acta 1784, 1493-1500.
33. Burley, S. K., and Petsko, G. A. (1985) Aromatic-aromatic interaction: A mechanism of protein structure stabilization. Science 229, 23-28.
34. Hanson, K. R. (1981) Phenylalanine ammonia-lyase: A model for the cooperativity kinetics induced by D- and L-phenylalanine. Arch. Biochem. Biophys. 211, 564-574.
35. Segel, I. H. (1975) Enzyme kinetics: Behavior and analysis of rapid equilibrium and steady-state enzyme systems, John Wiley and Sons, New York.
36. Budde, R. J. A. (1993) Evidence for kinetically distinct forms of pp60c-src with different Km values for their protein substrate. J. Biol. Chem. 268, 24868-24872.
37. Castro, M., Perez-Cerda, C., Merinero, B., Garcia, M. J., Bernar, J., Gil Nagel, A., Torres, J., Bermudez, M., Garavito, P., Marie, S., Vincent, F., Van den Berghe, G., and Ugarte, M. (2002) Screening for adenylosuccinate lyase deficiency: Clinical, biochemical and molecular findings in four patients. Neuropediatrics 33, 186-189.
38. Marie, S., Cuppens, H., Heuterspreute, M., Jaspers, M., Zambrano, T. E., Gu, X. X., Legius, E., Vincent, M. F., Jaeken, J., Cassiman, J. J., and Van den Berghe, G. (1999) Mutation analysis in adenylosuccinate lyase deficiency: Eight novel mutations in the re-evaluated full ADSL coding sequence. Hum. Mutat. 13, 197-202.