Activity of Adenosine Deaminase (ADA) and Adenylate Deaminase (AMPDA) Towards 6‐Chloropurine Nucleosides Modified in the Ribose Moiety | Zendy

Ciuffreda Pierangela | Zendy; Buzzi Benedetta | Zendy; Alessandrini Laura | Zendy; Santaniello Enzo | Zendy

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Activity of Adenosine Deaminase (ADA) and Adenylate Deaminase (AMPDA) Towards 6‐Chloropurine Nucleosides Modified in the Ribose Moiety

Author(s) -

Ciuffreda Pierangela,

Buzzi Benedetta,

Alessandrini Laura,

Santaniello Enzo

Publication year - 2004

Publication title -

european journal of organic chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.825

H-Index - 155

eISSN - 1099-0690

pISSN - 1434-193X

DOI - 10.1002/ejoc.200400380

Subject(s) - adenosine deaminase , chemistry , amp deaminase , adenylate kinase , moiety , ribose , riboside , adenosine , hydrolysis , biochemistry , enzyme , derivative (finance) , stereochemistry , financial economics , economics

The enzymes adenosine deaminase (ADA) and adenylate deaminase (AMPDA) are able to catalyze the hydrolytic dechlorination of 6‐chloropurine riboside and the corresponding 2′,3′‐ O ‐isopropylidene derivative, but show no activity towards the 3,4‐ O ‐isopropylidene‐1‐methylriboside of 6‐chloropurine and adenine. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2004)

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