TAILIEUCHUNG - Báo cáo khoa học: A kinetic study of a ternary cycle between adenine nucleotides

In the present paper, a kinetic study is made of the behavior of a moiety-conserved ternary cycle between the adenine nucleotides. The system con-tains the enzymes S-acetyl coenzyme A synthetase, adenylate kinase and pyruvate kinase, and converts ATP into AMP, then into ADP and finally back to ATP. | iFEBS Journal A kinetic study of a ternary cycle between adenine nucleotides Edelmira Valero1 Ramon Varon1 and Francisco Garcia-Carmona2 1 Departamento de Quimica-Fisica Escuela Politecnica Superior de Albacete Universidad de Castilla-La Mancha Albacete Spain 2 Departamento de Bioquimica y Biologia Molecular A Facultad de Biologia Universidad de Murcia Spain Keywords enzymatic cycling enzyme kinetics moiety-conserved cycle pyruvate kinase S-acetyl coenzyme A synthetase adenylate kinase Correspondence E. Valero Departamento de Quimica-Fisica Escuela Politecnica Superior de Albacete Universidad de Castilla-La Mancha Campus Universitario E-02071-Albacete Spain Fax 34 967 599224 Tel 34 967 599200 E-mail The mathematical model described here has been submitted to the Online Cellular Systems Modelling Database and can be accessed at http database valero of charge Received 19 April2006 revised 22 May 2006 accepted 8 June 2006 In the present paper a kinetic study is made of the behavior of a moiety-conserved ternary cycle between the adenine nucleotides. The system contains the enzymes S-acetyl coenzyme A synthetase adenylate kinase and pyruvate kinase and converts ATP into AMP then into ADP and finally back to ATP. L-Lactate dehydrogenase is added to the system to enable continuous monitoring of the progress of the reaction. The cycle cannot work when the only recycling substrate in the reaction medium is AMP. A mathematical model is proposed whose kinetic behavior has been analyzed both numerically by integration of the nonlinear differential equations describing the kinetics of the reactions involved and analytically under steady-state conditions with good agreement with the experimental results being obtained. The data obtained showed that there is a threshold value of the S-acetyl coenzyme A synthetase adenylate kinase ratio above which the cycle stops because all the recycling substrate has been accumulated

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