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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)