NAD(P)(+)-glycohydrolase (NADase, EC 3.2.2.6) was partially purified from microsomal membranes of human spleen after solubilization with Triton X-100. In addition to NAD(+) and NADP(+), the enzyme catalyzed the hydrolysis of several NAD(+) analogues and the pyridine base exchange reaction with conversion of NAD(+) into 3-acetylpyridine adenine dinucleotide. The enzyme also catalyzed the synthesis of cyclic ADP-ribose (cADPR) from NAD(+) and the hydrolysis of cADPR to adenosine diphosphoribose (ADPR). Therefore, this enzyme is a new member of multicatalytic NADases recently identified from mammals, involved in the regulation of intracellular cADPR concentration. Human spleen NADase showed a subunit molecular mass of 45 kDa, a pI of 4.9 and a K-m value for NAD(+) of 26 mu M. High activation of ADPR cyclase activity was observed in the presence of Ag+ ions, corresponding to NADase inhibition.

NAD(P)+-glycohydrolase from human spleen: a multicatalytic enzyme / Orsomando, Giuseppe; Polzonetti, V; Natalini, P.. - In: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. PART B, BIOCHEMISTRY & MOLECULAR BIOLOGY. - ISSN 1096-4959. - STAMPA. - 126:1(2000), pp. 89-98. [10.1016/S0305-0491(00)00170-X]

NAD(P)+-glycohydrolase from human spleen: a multicatalytic enzyme

ORSOMANDO, Giuseppe;
2000-01-01

Abstract

NAD(P)(+)-glycohydrolase (NADase, EC 3.2.2.6) was partially purified from microsomal membranes of human spleen after solubilization with Triton X-100. In addition to NAD(+) and NADP(+), the enzyme catalyzed the hydrolysis of several NAD(+) analogues and the pyridine base exchange reaction with conversion of NAD(+) into 3-acetylpyridine adenine dinucleotide. The enzyme also catalyzed the synthesis of cyclic ADP-ribose (cADPR) from NAD(+) and the hydrolysis of cADPR to adenosine diphosphoribose (ADPR). Therefore, this enzyme is a new member of multicatalytic NADases recently identified from mammals, involved in the regulation of intracellular cADPR concentration. Human spleen NADase showed a subunit molecular mass of 45 kDa, a pI of 4.9 and a K-m value for NAD(+) of 26 mu M. High activation of ADPR cyclase activity was observed in the presence of Ag+ ions, corresponding to NADase inhibition.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11566/34733
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