Premium
A specific, low K m ADP‐ribose pyrophosphatase from rat liver
Author(s) -
Miró Asunción,
Costas María Jesús,
García-Díaz Miguel,
Hernández María Teresa,
Cameselle José Carlos
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81176-7
Subject(s) - pyrophosphatases , ribose , nad+ kinase , pyrophosphatase , biochemistry , hydrolysis , inorganic pyrophosphatase , nicotinamide , chemistry , cyclic adp ribose , enzyme , biology , pyrophosphate , microbiology and biotechnology , cd38 , stem cell , cd34
Two rat liver ADP‐ribose pyrophosphatases (ADPRibases) were partially purified. ADPRibase‐I hydrolyzed ADP‐ribose ( K m =0.5 μM) giving AMP as a product, required Mg 2+ or, less efficiently, Mn 2+ (Ca 2+ was not active), its activity changed little between pH 7 and 9, and was specific for ADP‐ribose as it did not hydrolyze ADP‐glucose, NAD + , NADH or diadenosine 5′,5″‐ P 1 , P n ‐ n ‐phosphates (Ap 2 A, Ap 3 A). ADPRibase‐II showed similar properties, except that the K m for ADP‐ribose was 50 μM and may be non‐specific, as the same preparation hydrolyzed ADP‐glucose, NADH and Ap 2 A. ADPRibase‐I fulfils the requirements of a specific turnover pathway consistent with a cellular role for free ADP‐ribose.