2006Nucleosides Nucleotides & Nucleic AcidsRequires access

Deamination of 2′,3′-O-Isopropylideneadenosine-5′- Carboxylic Acid Catalyzed by Adenosine Deaminase (ADA) and Adenylate Deaminase (AMPDA): Influence of Substrate Ionization on the Activity of the Enzymes

Pierangela Ciuffreda, Laura Alessandrini, Radmila Pavlović, Enzo Santaniello

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Abstract

Adenosine deaminase (ADA) and adenylate deaminase (AMPDA) catalyze the deamination of 2 ',3 '-O-isopropylideneadenosine-5'-carboxylic acid to the corresponding inosine derivative and dependence of the rate of enzymatic reaction on the ionization degree of the substrate has been studied at different pH values.

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What this paper is about

Adenosine deaminase (ADA) and adenylate deaminase (AMPDA) catalyze the deamination of 2 ',3 '-O-isopropylideneadenosine-5'-carboxylic acid to the corresponding inosine derivative and dependence of the rate of enzymatic reaction on the ionization degree of the substrate has been studied at different pH values.

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OpenAlex reports 6 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

Adenosine deaminase (ADA) and adenylate deaminase (AMPDA) catalyze the deamination of 2 ',3 '-O-isopropylideneadenosine-5'-carboxylic acid to the corresponding inosine derivative and dependence of the rate of enzymatic reaction on the ionization degree of the substrate has been studied at different pH values.

Key concepts: Deamination, Inosine, Adenosine deaminase, Substrate (aquarium), AMP deaminase, Chemistry, Enzyme, Adenylate kinase

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Deamination of 2′,3′-O-Isopropylideneadenosine-5′- Carboxylic Acid Catalyzed by Adenosine Deaminase (ADA) and Adenylate Deaminase (AMPDA): Influence of Substrate Ionization on the Activity of the Enzymes — Research Paper | ScholarLens