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  • Title: Purification and some properties of liver adenylylsulfate kinase.
    Author: Hommes FA, Moss L, Touchton J.
    Journal: Biochim Biophys Acta; 1987 May 19; 924(2):270-5. PubMed ID: 3032273.
    Abstract:
    Adenylylsulfate kinase (ATP:adenylylsulfate 3'-phosphotransferase, EC 2.7.1.25) has been purified over 1300-fold from rat liver in 10% yield. The enzyme has a molecular weight of 58,000 and is composed of four subunits of equal molecular weight. ATP is an allosteric activator of adenylylsulfate kinase, with a Hill coefficient of 2.2 and a K0.5 of 2.5 mM. Adenosine phosphosulfate is a potent inhibitor of adenylylsulfate kinase, but the adenosine phosphosulfate concentration for maximal reaction is dependent on the ATP concentration. At the physiological levels of ATP the inhibition by adenosine phosphosulfate is not likely to play a role, while the allosteric regulation of adenylylsulfate kinase by ATP may be operative.
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