Enzymatic regeneration of ATP: II. Equilibrium studies with acetate kinase and adenylate kinase
作者:
Robert S. Langer,
Colin R. Gardner,
Bruce K. Hamilton,
Clark K. Colton,
期刊:
AIChE Journal
(WILEY Available online 1977)
卷期:
Volume 23,
issue 1
页码: 1-10
ISSN:0001-1541
年代: 1977
DOI:10.1002/aic.690230102
出版商: American Institute of Chemical Engineers
数据来源: WILEY
摘要:
AbstractEquilibria of reactions catalyzed by acetate kinase and adenylate kinase were studied experimentally and theoretically. Nucleotide conversions in excess of 90% were obtained with reactants (acetyl phosphate and one nucleotide) in stoichiometric proportion for ATP regeneration from either ADP via acetate kinase or AMP via the coupled enzyme system. Observed equilibrium constants, measured as a function of [Mg2+] atpH 7.4, ranged from about 1 to 9 for the reaction catalyzed by adenylate kinase and from about 50 to 400 for the reaction catalyzed by acetate kinase. These results agreed well with prediction of a theoretical model for the multiple equilibria between all species present in solution. Theoretical calculations showed that magnesium ion complexes and totally dissociated anions are the predominant species in solution at\documentclass{article}\pagestyle{empty}\begin{document}$p{\rm H}\tilde>7{\rm and}[{\rm Mg}^{2 + } ]\tilde>10^{ - 3} {\rm M}$\end{document}.
点击下载:
PDF
(980KB)
返 回