2003European Journal of Organic ChemistryRequires access

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)

Pierangela Ciuffreda, Angela Loseto, Laura Alessandrini, Giancarlo Terraneo, Enzo Santaniello

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Abstract

Abstract 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)

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Abstract 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)

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Available abstract

Abstract 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)

Key concepts: Deamination, Chemistry, AMP deaminase, Adenosine deaminase, Adenylate kinase, Catalysis, Enzyme, Biochemistry

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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) — Research Paper | ScholarLens