Inhibition of adenosine deaminase from several sources by deaza derivatives of adenosine and EHNA.

doi:10.3109/14756368509031283

Paper

Inhibition of adenosine deaminase from several sources by deaza derivatives of adenosine and EHNA.

Published 1985 · G. Lupidi, G. Cristalli, F. Marmocchi

Journal of enzyme inhibition

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18

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Abstract

Deaza analogues of adenosine and EHNA were tested as inhibitors of the enzyme adenosine deaminase (ADA) obtained from several sources including human erythrocytes, calf intestine, Saccaromices cerevisiae, Escherichia coli and Takadiastase. Ki values of the inhibitors suggest differences among the enzymes both at purine and erythro-nonyl binding site. Among the ribofuranosyl derivatives, 1-deazaadenosine is the best inhibitor, its Ki ranging between 3.5 x 10(-7) and 4 x 10(-5) M for ADA from erythrocytes and Takadiastase respectively. Only ADA from erythrocytes and calf intestine bind EHNA and some of deazaEHNA analogues; 3-deazaEHNA behaves very similarly to EHNA both in affinity and slow binding mechanism, whereas 1-deazaEHNA, though less potent, is a good inhibitor.

In Vitro Study

Study Snapshot

1-deazaadenosine is the best inhibitor of adenosine deaminase from various sources, with 3-deazaEHNA acting similarly to EHNA in affinity and slow binding mechanism.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Inhibition of adenosine deaminase from several sources by deaza derivatives of adenosine and EHNA.

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References

A general method of purification of adenosine deaminase by affinity chromatography.

Affinity chromatography effectively purifies adenosine deaminase from various sources, yielding homogeneous enzyme preparations with high yields and maintaining the same number of multiple enzyme forms as in the crude extract.

Deaza analogues of adenosine as inhibitors of blood platelet aggregation.

Deaza analogues of adenosine with 6-amino group and nitrogen atoms at positions 3 and 7 effectively inhibit platelet aggregation induced by ADP and collagen.

Adenosine deaminase inhibitors. Synthesis of deaza analogues of erythro-9-(2-hydroxy-3-nonyl)adenine.

3-deaza-EHNA and 1-deaza-EHNA show comparable inhibitory activity against adenosine deaminase, with 1-deaza-EHNA being a semitight inhibitor.

Human malaria parasite adenosine deaminase. Characterization in host enzyme-deficient erythrocyte culture.

In vitro culture of adenosine deaminase-deficient human erythrocytes with 8% parasitemia reveals a unique increase in adenosine deaminase activity, providing insights into the purine metabolism of the intraerythrocytic malaria parasit

Conversion of 2,6-diamino-9-(2-hydroxyethoxymethyl)purine to acyclovir as catalyzed by adenosine deaminase.

Adenosine deaminase catalyzes the conversion of 2,6-diamino-9-(2-hydroxyethoxymethyl)purine to acyclovir, with various enzymes showing different substrate efficiencies and inhibitory effects.

Citations

Therapeutic Perspectives of Adenosine Deaminase Inhibition in Cardiovascular Diseases

Inhibiting adenosine deaminase (ADA) may be a promising therapeutic target for cardiovascular diseases like atherosclerosis, hypertension, thrombosis, and diabetes.

Moonlighting Adenosine Deaminase: A Target Protein for Drug Development

Moonlighting adenosine deaminase (ADA) plays multiple roles in medicine, and drugs modulating ADA properties may have potential medical interest.

Extracellular guanosine regulates extracellular adenosine levels.

Extracellular guanosine slows the disposition of extracellular adenosine in various cell types, potentially impacting adenosine metabolism and cellular adenosine levels.

Adenosine deaminase in the modulation of immune system and its potential as a novel target for treatment of inflammatory disorders.

ADA plays a crucial role in regulating immune system activity and inflammatory diseases, making it a potential target for developing novel treatments.

Theoretical Study of the Structure of Adenosine Deaminase Complexes with Adenosine Analogues: I. Aza-, Deaza-, and Isomeric Azadeazaanalogues of Adenosine

The optimal conformation of adenosine deaminase in the absence of bound ligand is similar to the structure of the ADA complex with 1-deazaadenosine (1ADD), which correlates with its enzymatic activity towards corresponding nucleosides.