Spontaneous hydrolysis of ionized phosphate monoesters and diesters and the proficiencies of phosphatases and phosphodiesterases as catalysts

Journal of the American Chemical Society

Volumn 120, Issue 4, 1998, Pages 833-834

  Wolfenden, Richard ^a   Ridgway, Caroline ^a   Young, Gregory ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATASE; PHOSPHATE; PHOSPHODIESTERASE;

ARTICLE; CATALYST; CONTROLLED STUDY; DISSOCIATION CONSTANT; DRUG SYNTHESIS; ENZYME ACTIVITY; HYDROLYSIS; NONHUMAN;

EID: 0032481372     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9733604     Document Type: Article

References (17)

1. Radzicka, A.; Wolfenden, R. Science 1995, 267, 90-93.
2. Wolfenden, R. Annu. Rev. Biophys. Bioeng. 1976, 5, 271-306.
3. Bearne, S. L.; Wolfenden, R. Biochemistry 1997, 36, 1646-1656.
4. The acidities of substrates, buffers, and solvent water vary with temperature (ref 5). These complications are not expected to interfere with determination of the rates of the uncatalyzed reactions, which are pH-independent.
5. Edsall, J. T.; Wyman, J. Biophysical Chemistry; Academic Press: New York, 1958; pp 452-453.
6. Bunton, C. A.; Llewellyn, D. R.; Oldham, K. G.; Vernon, C. A. J. Chem. Soc. 1958, 3574-3587.
7. Butcher, W. W.; Westheimer, F. H. J. Am. Chem. Soc. 1955, 77, 2420-2423.
8. Kirby, A. J.; Varvoglis, A. G. J. Am. Chem. Soc. 1967, 89, 415-423.
9. Williams, A.; Naylor, R. A. J. Chem. Soc. B 1971, 1973-1979. The reaction catalyzed by alkaline phosphatase is not ideal for this comparison, as it proceeds through a covalent intermediate. Qualitatively, this comparison seems justified to the extent that an active site serine side chain may resemble a bound water molecule in its inherent chemical reactivity.
10. Labow, B. I.; Herschlag, D.; Jencks, W. P. Biochemistry 1993, 32, 8737-8741.
11. Hengge, A. C.; Edens, W. A.; Elsing, H. J. Am. Chem. Soc. 1994, 116, 5045-5049.
12. Simopoulos, T. T.; Jencks, W. P. Biochemistry 1994, 33, 3, 10375-10380.
13. Bunton, C. A.; Mhala, M. M.; Oldham, K. G.; Vernon, C. A. J. Chem. Soc. 1960, 3293-3301.
14. Dimethyl phosphate cleavage is subject to catalysis by KOH (refs 7 and 15), and preliminary experiments indicate that, in strong alkali, the heat of activation is substantially less positive than the heat of activation for water attack on the dimethyl phosphate anion. Under those conditions (>0.3 M KOH), methyl phosphate accumulates in measurable quantities during the hydrolysis of dimethyl phosphate.
15. Haake, P. C.; Westheimer, F. H. J. Am. Chem. Soc. 1961, 83, 1102-1109.
16. Because of major differences in energy of activation, dimethyl phosphate anion is more rapidly hydrolyzed than methyl phosphate dianion at temperatures below 50°C. These rates of reaction are too low to be of practical value in the preparation of monoesters, but see footnote 14 above.
17. Serpersu, E. H.; Shortle, D.; Mildvan, A. S. Biochemistry 1986, 25, 5, 68-77.