A specific, low K m ADP‐ribose pyrophosphatase from rat liver

FEBS Letters

Hernández, María Teresa²  Cameselle, José Carlos²  Miró, Asunción¹  García-Díaz, Miguel²  Costas, María Jesús² 

[1] Departamento de Patología y Clinicas Humanas (Médicas), Facultad de Medicina, Universidad de Extremadura, Instituto de Investigaciones Biomédicas del Consejo Superior de Investigaciones Científicas, E-06080 Badajoz, Spain;Departamento de Bioquímica y Biología Molecular y Genética, Facultad de Medicina, Universidad de Extremadura, Instituto de Investigaciones Biomédicas del Consejo Superior de Investigaciones Científicas, E-06080 Badajoz, Spain

关键词: ADP-ribose pyrophosphatase;    ADP-ribose;    free;    ADP-ribose turnover;    ADP-ribosylation;    (Liver);    ADPGlc;    ADP-glucose;    ADPRib;    ADP-ribose;    ADPRibase;    ADP-ribose pyrophosphatase;    Ap n A;    diadenosine 5′;    5‴-P 1;    Pn -n-phosphate;    UDPGlc;    UDP-glucose;   

DOI  :  10.1016/0014-5793(89)81176-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Mg²⁺ or, less efficiently, Mn²⁺ (Ca²⁺ 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 (Ap₂A, Ap₃A). 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 Ap₂A. ADPRibase-I fulfils the requirements of a specific turnover pathway consistent with a cellular role for free ADP-ribose.

【 授权许可】

Unknown