Hydrolysis of adenosine 5'-triphosphate: an isotope-labeling study

Autor:	James F. Marecek, Fausto Ramirez, Eugene S. Kuhn, Seymour Meyerson
Rok vydání:	1982
Předmět:	chemistry.chemical_classification Kinetics Inorganic chemistry chemistry.chemical_element General Chemistry Biochemistry Medicinal chemistry Adenosine Oxygen Catalysis Chemical kinetics Hydrolysis Colloid and Surface Chemistry Enzyme chemistry medicine Nucleotide Solvolysis medicine.drug
Zdroj:	Journal of the American Chemical Society. 104:7231-7239
ISSN:	1520-5126 0002-7863
DOI:	10.1021/ja00389a055
Popis:	A combination of /sup 18/O-labeling experiments and kinetic studies to clarify the nonenzymatic hydrolytic pathways of adenosine 5'-triphosphate (ATP) at pH values ranging from 0 to 8.3 has been used in this experiment. In 1 N and 0.1 N HCl, the data are consistent with the hypothesis that hydrolysis occurs by addition-elimination, with initial attack 93% ..gamma.. and 7% ..beta..; both lead only to ADP + P/sub i/. In the subsequent hydrolysis of the ADP to AMP + P/sub i/, attack is 83% ..beta.. and 17% ..cap alpha... At pH 8.3, the data are consistent with the hypothesis that hydrolsysis occurs by elimination-addition. Over the entire pH range studied, no oxygen exchange between water and ATP, ADP, or P/sub i/ was detected. Nonenzymatic hydrolysis and isotopic analysis of the resultant P/sub i/ comprise a preferred means of assaying the isotopic enrichment of (..gamma..-/sup 18/O)ATP to be used in studies of enzymatic processes.
Databáze:	OpenAIRE
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