Effects of the G376E and G157D mutations on the stability of yeast enolase - A model for human muscle enolase deficiency

FEBS Journal

Volumn 275, Issue 1, 2008, Pages 97-106

  Zhao, Songping ^a   Choy, Bonny S F ^a   Kornblatt, Mary J ^a  

^a Gina Cody School of Engineering and Computer Science   (Canada)

Author keywords

Muscle enolase; Mutations; Proteolysis; Stability; Subunit interactions

Indexed keywords

ENOLASE; TRYPSIN;

ARTICLE; DISSOCIATION; ENZYME STABILITY; HUMAN MUSCLE ENOLASE DEFICIENCY; MUTATION; PRIORITY JOURNAL; PROTEIN DEFICIENCY; PROTEIN FOLDING; PROTEIN STRUCTURE; YEAST;

CIRCULAR DICHROISM; ENZYME STABILITY; HUMANS; KINETICS; MODELS, MOLECULAR; MUSCLE, SKELETAL; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHOSPHOPYRUVATE HYDRATASE; PROTEIN CONFORMATION; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE;

EID: 37349087115     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06177.x     Document Type: Article

References (32)

1. Comi GP, Fortunato F, Lucchiari S, Bordoni A, Prelle A, Jann S, Keller A, Ciscato P, Galbiati S, Chiveri L et al. (2001) β-Enolase deficiency, a new metabolic myopathy of distal glycolysis. Ann Neurol 50, 202 207.
2. 2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-Å resolution. Biochemistry 33, 9333 9342.
3. 2+-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-Å resolution. Biochemistry 30, 2817 2822.
4. Poyner RR, Laughlin LT, Sowa GA Reed GH (1996) Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants. Biochemistry 35, 1692 1699.
5. Vinarov DA Nowak T (1999) Role of His159 in yeast enolase catalysis. Biochemistry 38, 12138 12149.
6. Stec B Lebioda L (1990) Refined structure of yeast apo-enolase at 2.25-Å resolution. J Mol Biol 211, 235 248.
7. da Silva Giotto MT, Hannaert V, Vertommen D, de AS Navarro MV, Rider MH, Michels PA, Garratt RC Rigden DJ (2003) The crystal structure of Trypanosoma brucei enolase: visualisation of the inhibitory metal binding site III and potential as target for selective, irreversible inhibition. J Mol Biol 331, 653 665.
8. Chai G, Brewer JM, Lovelace LL, Aoki T, Minor W Lebioda L (2004) Expression, purification and the 1.8 Å resolution crystal structure of human neuron specific enolase. J Mol Biol 341, 1015 1021.
9. Kuhnel K Luisi BF (2001) Crystal structure of the Escherichia coli RNA degradosome component enolase. J Mol Biol 313, 583 592.
10. Duquerroy S, Camus C Janin J (1995) X-ray structure and catalytic mechanism of lobster enolase. Biochemistry 34, 12513 12523.
11. Lobley A, Whitmore L Wallace BA (2002) DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18, 211 212.
12. Whitmore L Walllace BA (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32, W668 W673.
13. Manavalan P Johnson WC (1987) Variable selection method improves the prediction of protein secondary structure from circular dichroism. Anal Biochem 167, 76 85.
14. Anderson VE Cleland WW (1990) Phosphonate analogue substrates for enolase. Biochemistry 29, 10498 10503.
15. Brewer JM Weber G (1968) The reversible dissociation of yeast enolase. Proc Natl Acad Sci USA 59, 216 223.
16. Keresztes-Nagy S Orman R (1971) Dissociation of yeast enolase into active monomers. Biochemistry 10, 2506 2508.
17. Holleman WH (1973) The use of absorption optics to measure dissociation of yeast enolase into enzymatically active monomers. Biochim Biophys Acta 327, 176 185.
18. Brewer JM, Robson RL, Glover CV, Holland MJ Lebioda L (1993) Preparation and characterization of the E168Q site-directed mutant of yeast enolase 1. Proteins 17, 426 434.
19. Brewer JM, Glover CV, Holland MJ Lebioda L (1997) Effect of site-directed mutagenesis of His373 of yeast enolase on some of its physical and enzymatic properties. Biochim Biophys Acta 1340, 88 96.
20. Liu HY, Zhang YK Yang WT (2000) How is the active site of enolase organized to catalyze two different reaction steps? Journal of the American Chemical Society 122, 6560 6570.
21. Paladini AA Weber G (1981) Pressure-induced reversible dissociation of yeast enolase. Biochemistry 20, 2587 2593.
22. Brewer JM, Bastiaens P Lee J (1987) Investigation of conformational changes in yeast enolase using dynamic fluorescence and steady-state quenching measurements. Biochem Biophys Res Commun 147, 329 334.
23. Kornblatt MJ, Al-Ghanim A Kornblatt JA (1996) The effects of sodium perchlorate on rabbit muscle enolase - spectral characterization of the monomer. Eur J Biochem 236, 78 84.
24. Kornblatt MJ, Lange R Balny C (1998) Can monomers of yeast enolase have enzymatic activity? Eur J Biochem 251, 775 780.
25. Brewer JM, Faini GJ, Wu CA, Goss LP, Carreira LA Wojcik R (1995) Characterization of the subunit dissociation of yeast enolase. In Physical Aspects of Protein Interactions (Catsimpoolas N, ed. pp. 57 78. Elsevier, North-Holland, Amsterdam.
26. Kornblatt MJ, Lange R Balny C (2004) Use of hydrostatic pressure to produce 'native' monomers of yeast enolase. Eur J Biochem 271, 3897 3904.
27. Horn JR, Kraybill B, Petro EJ, Coales SJ, Morrow JA, Hamuro Y Kossiakoff AA (2006) The role of protein dynamics in increasing binding affinity for an engineered protein-protein interaction established by H/D exchange mass spectrometry. Biochemistry 45, 8488 8498.
28. Shen TYS Westhead EW (1973) Divalent cation and pH-dependent primary isotope effects in the enolase reaction. Biochemistry 12, 3333 3337.
29. Kornblatt MJ Klugerman A (1989) Characterization of the enolase isozymes of rabbit brain: kinetic differences between mammalian and yeast enolases. Biochem Cell Biol 67, 103 107.
30. Sims PA Reed GH (2005) Method for the enzymatic synthesis of 2-phospho-D-glycerate from adenosine 5′-triphosphate and D-glycerate via D-glycerate-2-kinase. J Mol Catal, B Enzym 32, 77 81.
31. Cole JL (1996) Characterization of human cytomegalovirus protease dimerization by analytical centrifugation. Biochemistry 35, 15601 15610.
32. Pace CN Scholtz JM (1997) Measuring the conformational stability of a protein. In Protein Structure (Creighton TE, ed. pp 299 321. IRL Press, Oxford.