Hydron transfer catalyzed by triosephosphate isomerase. Products of the direct and phosphite-activated isomerization of [1-13C]- glycolaldehyde in D2O

Biochemistry

Volumn 48, Issue 24, 2009, Pages 5769-5778

  Go, Maybelle K ^a   Amyes, Tina L ^a   Richard, John P ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON-13; CARBONYL CARBON; CATALYZED REACTIONS; CLOSED FORM; DIANION; ENZYME ACTIVE SITES; GLYCOLALDEHYDE; H NMR SPECTROSCOPY; HYDRON TRANSFER; INTRAMOLECULAR TRANSFER; INTRINSIC BINDING; ISOMERIZATION REACTION; PRODUCT DISTRIBUTIONS; PROTEIN SURFACE; TRIOSEPHOSPHATE ISOMERASE;

ALDEHYDES; BINDING ENERGY; BIOCHEMISTRY; DEUTERIUM; ELECTRON TRANSITIONS; ENZYMES; HYDROGEN; ISOMERIZATION; ISOMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; TECHNOLOGICAL FORECASTING; THERMAL INSULATING MATERIALS;

GENETIC ALGORITHMS;

DEUTERIUM; PHOSPHITE; TRIOSEPHOSPHATE ISOMERASE;

ARTICLE; CATALYSIS; CHEMICAL REACTION; ENERGY; ENZYME ACTIVE SITE; ISOMERIZATION; NONHUMAN; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; RABBIT;

ACETALDEHYDE; ANIMALS; CATALYSIS; CHICKENS; DEUTERIUM; DEUTERIUM EXCHANGE MEASUREMENT; KINETICS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHITES; RABBITS; STEREOISOMERISM; TRIOSE-PHOSPHATE ISOMERASE;

EID: 67649214131     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900636c     Document Type: Article

References (44)

1. Knowles, J. R., and Albery, W. J. (1977) Perfection in enzyme catalysis: the energetics of triosephosphate isomerase. Acc. Chem. Res. 10, 105-111.
2. Rieder, S. V., and Rose, I. A. (1959) Mechanism of the triose phosphate isomerase reaction. J. Biol. Chem. 234, 1007-1010.
3. Shonk, C. E., and Boxer, G. E. (1964) Enzyme patterns in human tissues. I. Methods for the determination of glycolytic enzymes. Cancer. Res. 24, 709-721.
4. Gerlt, J. A., and Gassman, P. G. (1993) Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters. Biochemistry 32, 11943-11952. (Pubitemid 23353629)
5. Amyes, T. L., and Richard, J. P. (2007) Proton transfer to and from carbon in model systems, in Hydrogen-Transfer Reactions, Vol.3, Biological Aspects I-II (Hynes, J. T., Klinman, J. P., Limbach, H.-H., and Schowen, R. L., Eds.) pp 949-973, Wiley-VCH, Weinheim.
6. Xiang, J., Jung, J.-y., and Sampson, N. S. (2004) Entropy effects on protein hinges: The reaction catalyzed by triosephosphate isomerase. Biochemistry 43, 11436-11445.
7. Jogl, G., Rozovsky, S., McDermott, A. E., and Tong, L. (2003) Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2 Å resolution. Proc. Natl. Acad. Sci. U.S.A. 100, 50-55.
8. Loria, J. P., Berlow, R. B., and Watt, E. D. (2008) Characterization of enzyme motions by solution NMR relaxation dispersion. Acc. Chem. Res. 41, 214-221.
9. Blacklow, S. C., Raines, R. T., Lim, W. A., Zamore, P. D., and Knowles, J. R. (1988) Triosephosphate isomerase catalysis is diffusion controlled. Biochemistry 27, 1158-1165.
10. Amyes, T. L., O'Donoghue, A. C., and Richard, J. P. (2001) Contribution of phosphate intrinsic binding energy to the enzymatic rate acceleration for triosephosphate isomerase. J. Am. Chem. Soc. 123, 11325-11326.
11. Richard, J. P. (1984) Acid-base catalysis of the elimination and isomerization reactions of triose phosphates. J. Am. Chem. Soc. 106, 4926-4936.
12. Pompliano, D. L., Peyman, A., and Knowles, J. R. (1990) Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase. Biochemistry 29, 3186-3194. (Pubitemid 20131455)
13. Sampson, N. S., and Knowles, J. R. (1992) Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase. Biochemistry 31, 8482-8487.
14. Sampson, N. S., and Knowles, J. R. (1992) Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase. Biochemistry 31, 8488-8494.
15. Sun, J., and Sampson, N. S. (1999) Understanding protein lids: kinetic analysis of active hinge mutants in triosephosphate isomerase. Biochemistry 38, 11474-11481. (Pubitemid 129516725)
16. Xiang, J., Sun, J., and Sampson, N. S. (2001) The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase. J. Mol. Biol. 307, 1103-1112.
17. Kursula, I., Salin, M., Sun, J., Norledge, B. V., Haapalainen, A. M., Sampson, N. S., and Wierenga, R. K. (2004) Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase. Protein Eng., Des. Sel. 17, 375-382. (Pubitemid 39093518)
18. Sun, J., and Sampson, N. S. (1998) Determination of the amino acid requirements for a protein hinge in triosephosphate isomerase. Protein Sci. 7, 1495-1505. (Pubitemid 28331268)
19. Amyes, T. L., and Richard, J. P. (2007) Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion. Biochemistry 46, 5841-5854. (Pubitemid 46764132)
20. +) by phosphite dianion. Biochemistry 47, 4575-4582.
21. Jencks, W. P. (1975) Binding energy, specificity and enzymic catalysis: the Circe effect. Adv. Enzymol. Relat. Areas Mol. Biol. 43, 219-410.
22. O'Donoghue, A. C., Amyes, T. L., and Richard, J. P. (2005) Hydron transfer catalyzed by triosephosphate isomerase. Products of isomerization of (R)-glyceraldehyde 3-phosphate in D2O. Biochemistry 44, 2610-2621. (Pubitemid 40279565)
23. O'Donoghue, A. C., Amyes, T. L., and Richard, J. P. (2005) Hydron transfer catalyzed by triosephosphate isomerase. Products of isomerization of dihydroxyacetone phosphate in D2O. Biochemistry 44, 2622-2631. (Pubitemid 40279566)
24. Albery, W. J., and Knowles, J. R. (1976) Free-energy profile for the reaction catalyzed by triosephosphate isomerase. Biochemistry 15, 5627-5631. (Pubitemid 8004279)
25. Hermes, J. D., Parekh, S. M., Blacklow, S. C., Koster, H., and Knowles, J. R. (1989) A reliable method for random mutagenesis: the generation of mutant libraries using spiked oligodeoxyribonucleotide primers. Gene 84, 143-151. (Pubitemid 20028469)
26. Straus, D., and Gilbert, W. (1985) Chicken triosephosphate isomerase complements an Escherichia coli deficiency. Proc. Natl. Acad. Sci. U.S.A. 82, 2014-2018.
27. Putman, S. J., Coulson, A. F. W., Farley, I. R. T., Riddleston, B., and Knowles, J. R. (1972) Specificity and kinetics of triose phosphate isomerase from chicken muscle. Biochem. J. 129, 301-310.
28. Glasoe, P. K., and Long, F. A. (1960) Use of glass electrodes to measure acidities in deuterium oxide. J. Phys. Chem. 64, 188-190.
29. Collins, G. C. S., and George, W. O. (1971) Nuclear magnetic resonance spectra of glycolaldehyde. J. Chem. Soc. B, 1352-1355.
30. Plaut, B., and Knowles, J. R. (1972) pH-dependence of the triose phosphate isomerase reaction. Biochem. J. 129, 311-320.
31. Amyes, T. L., and Richard, J. P. (1992) Generation and stability of a simple thiol ester enolate in aqueous solution. J. Am. Chem. Soc. 114, 10297-10302.
32. a of ethyl acetate: Broensted correlation for deprotonation of a simple oxygen ester in aqueous solution. J. Am. Chem. Soc. 118, 3129-3141.
33. Richard, J. P., Williams, G., O'Donoghue, A. C., and Amyes, T. L. (2002) Formation and stability of enolates of acetamide and acetate anion: an eigen plot for proton transfer at α-carbonyl carbon. J. Am. Chem. Soc. 124, 2957-2968.
34. 2O. Org. Biomol. Chem. 6, 391-396.
35. Komives, E. A., Chang, L. C., Lolis, E., Tilton, R. F., Petsko, G. A., and Knowles, J. R. (1991) Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95. Biochemistry 30, 3011-3019.
36. Lodi, P. J., and Knowles, J. R. (1991) Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implications. Biochemistry 30, 6948-6956.
37. Nickbarg, E. B., Davenport, R. C., Petsko, G. A., and Knowles, J. R. (1988) Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism. Biochemistry 27, 5948-5960.
38. Harris, T. K., Abeygunawardana, C., and Mildvan, A. S. (1997) NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase. Biochemistry 36, 14661-14675. (Pubitemid 27524386)
39. Harris, T. K., Cole, R. N., Comer, F. I., and Mildvan, A. S. (1998) Proton transfer in the mechanism of triosephosphate isomerase. Biochemistry 37, 16828-16838. (Pubitemid 28543945)
40. Hine, J. (1978) Bifunctional catalysis of α-hydrogen exchange of aldehydes and ketones. Acc. Chem. Res. 11, 1-7.
41. 6 by conformationally constrained derivatives of N,N-dimethyl-1,3-propanediamine. J. Am. Chem. Soc. 98, 3287-3294.
42. Alber, T., Banner, D. W., Bloomer, A. C., Petsko, G. A., Phillips, D., Rivers, P. S., and Wilson, I. A. (1981) On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase. Philos. Trans. R. Soc. London, Ser. B 293, 159-171.
43. Lolis, E., and Petsko, G. A. (1990) Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-Å resolution: implications for catalysis. Biochemistry 29, 6619-6625. (Pubitemid 20223556)
44. Davenport, R. C., Bash, P. A., Seaton, B. A., Karplus, M., Petsko, G. A., and Ringe, D. (1991) Structure of the triosephosphate isomerase- phosphoglycolohydroxamate complex: an analog of the intermediate on the reaction pathway. Biochemistry 30, 5821-5826.