Cytosolic adenylate kinase catalyzes the synthesis of thiamin triphosphate from thiamin diphosphate.
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.
Shikata
H
H
Department of Biochemistry, Hiroshima University School of Medicine, Japan.
Koyama
S
S
Egi
Y
Y
Yamada
K
K
Kawasaki
T
T
D000263:Adenylate Kinase / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D003600:Cytosol / Q000201:enzymology*; D005779:Immunodiffusion; D009132:Muscles / Q000201:enzymology; D010770:Phosphotransferases / Q000378:metabolism*; D013552:Swine; D013835:Thiamine Pyrophosphate / Q000378:metabolism*; D013838:Thiamine Triphosphate / Q000096:biosynthesis
D013838:Thiamine Triphosphate; D010770:Phosphotransferases; D000263:Adenylate Kinase; D013835:Thiamine Pyrophosphate