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  • Title: Cytosolic adenylate kinase catalyzes the synthesis of thiamin triphosphate from thiamin diphosphate.
    Author: Shikata H, Koyama S, Egi Y, Yamada K, Kawasaki T.
    Journal: Biochem Int; 1989 May; 18(5):933-41. PubMed ID: 2551297.
    Abstract:
    An attempt was made to purify a porcine skeletal muscle enzyme catalyzing the formation of thiamin triphosphate (TTP) from thiamin diphosphate (TDP), requiring ATP, Mg2+ and a cofactor (creatine). As the purification proceeded, the reaction requirements for ATP and creatine were lost and then a requirement for ADP was manifested. The activity responsible for TTP synthesis from TDP, ADP, and Mg2+ was found to be copurified with adenylate kinase [EC 2.7.4.3] activity, and was finally purified to a single band on SDS-PAGE. Antiserum obtained against the purified enzyme preparation inhibited both adenylate kinase activity and the TTP-synthesizing activity to exactly the same extent. These results indicate that adenylate kinase catalyzes TTP formation from TDP in vitro.
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