Cytosolic adenylate kinase catalyzes the synthesis of thiamin triphosphate from thiamin diphosphate.
Biochem Int
; 18(5): 933-41, 1989 May.
Article
en En
| MEDLINE
| ID: mdl-2551297
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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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosfotransferasas
/
Tiamina Pirofosfato
/
Adenilato Quinasa
/
Citosol
Límite:
Animals
Idioma:
En
Revista:
Biochem Int
Año:
1989
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Australia