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Adenylate Deaminase (5′‐Adenylic Acid Deaminase, AMPDA)‐Catalyzed Deamination of 5′‐Deoxy‐5′‐Substituted and 5′‐Protected Adenosines: A Comparison with the Catalytic Activity of Adenosine Deaminase (ADA)
Author(s) -
Ciuffreda Pierangela,
Loseto Angela,
Alessandrini Laura,
Terraneo Giancarlo,
Santaniello Enzo
Publication year - 2003
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.200300435
Subject(s) - deamination , chemistry , amp deaminase , adenosine deaminase , adenylate kinase , catalysis , adenosine deaminase inhibitor , biochemistry , enzyme , adenosine , stereochemistry
The enzyme adenylate deaminase (AMPDA) is able to catalyze the hydrolytic deamination of 5′‐substituted and 5′‐protected 5′‐deoxyadenosines, whereas limited or no activity is shown by adenosine deaminase (ADA) towards the same substrates. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2003)