Adenosine Deaminase in Nucleoside Synthesis. A Review

2006 ◽  
Vol 71 (6) ◽  
pp. 769-787 ◽  
Author(s):  
Mukta Gupta ◽  
Vasu Nair
Keyword(s):  
Adenosine Deaminase ◽  
Enzymatic Synthesis ◽  
Salvage Pathway ◽  
Purine Salvage ◽  
Adenosine Analogues ◽  
Nucleoside Synthesis ◽  
Synthetic Utility

Adenosine deaminase (ADA) is an enzyme in the purine salvage pathway that catalyzes the deamination of adenosine and deoxyadenosine to inosine and deoxyinosine, respectively. This deamination is an important factor in limiting the usefulness of adenosine analogues in chemotherapy. However, the biocatalysis by ADA is also a useful transformation in enzymatic synthesis. In this review, examples from both the principal investigator's laboratory and from the literature, which depict the synthetic usefulness of this enzyme in deamination, dehalogenation, demethoxylation reactions and in diastereoisomeric resolution, are presented. It is not the intent of this review to comprehensively list all of the biotransformations induced by adenosine deaminase, but rather to present representative examples to highlight the powerful synthetic utility of this enzyme. A review with 72 references.

scholarly journals Evaluation of adenosine deaminase and other purine salvage pathway enzymes in horses with combined immunodeficiency.

1976 ◽  
Vol 13 (3) ◽  
pp. 995-997 ◽  
Author(s):  
T C McGuire ◽  
B Pollara ◽  
J J Moore ◽  
M J Poppie
Keyword(s):  
Adenosine Deaminase ◽  
Combined Immunodeficiency ◽  
Salvage Pathway ◽  
Purine Salvage

scholarly journals Adenosine Deaminase 1 as a Biomarker for Diagnosis and Monitoring of Patients with Acute Lymphoblastic Leukemia

2018 ◽  
Vol 37 (2) ◽  
pp. 128-133 ◽  
Author(s):  
Mina Ebrahimi-Rad ◽  
Shohreh Khatami ◽  
Shahla Ansari ◽  
Shohreh Jalylfar ◽  
Shirin Valadbeigi ◽  
...  
Keyword(s):  
Acute Lymphoblastic Leukemia ◽  
Adenosine Deaminase ◽  
Healthy Subjects ◽  
Lymphoblastic Leukemia ◽  
Salvage Pathway ◽  
Purine Salvage ◽  
Pediatric Malignancy ◽  
Sds Page ◽  
Human T Lymphocyte ◽  
Relapsed Disease

SummaryBackground:Acute lymphoblastic leukemia (ALL) is known as the most prevalent pediatric malignancy all around the world. Identification of specific biomarker is necessary for early diagnosis and effective therapy. It is believed that Adenosine deaminase (ADA) as an enzyme involved in the purine salvage pathway increases in ALL patients. Herein, the quantity and pattern of ADA isoenzymes were surveyed among ALL patients in comparison to healthy subjects.Methods:Serum and RBC samples of three different groups of ALL patients, including newly diagnosed cases without any drugs administration, subjects with the relapsed disease, patients in the remission stage after therapy, and the healthy subjects were enrolled in the study. Then, the activity and pattern of ADA1, ADA2 and ADA1+cp were determined using ADA kit and electrophoresis on SDS-PAGE, respectively. To confirm the presence of ADA enzyme, the fresh serums, extractions from erythrocytes, JM cell line as a human T lymphocyte line and J774 A.1 as mouse monocyte line were electrophoresed on 1.2% agarose gel and stained with the specific dye.Results:The activities of ADA1 isoenzyme and total ADA in new cases and subjects with the relapsed disease were significantly higher than their activities in the patients in the remission stage and healthy controls (p<0.001). The unbounded ADA1 isoenzyme was found to exist in the erythrocyte, lymphocyte and monocyte. But in serum, all the ADA1 was bounded to the cp protein.Conclusions:ADA1 is the key isoenzyme elevating in ALL patients, therefore this isoenzyme could be a useful biomarker to diagnose ALL patients and monitor their therapies.

scholarly journals Metabolic Fate of Fumarate, a Side Product of the Purine Salvage Pathway in the Intraerythrocytic Stages ofPlasmodium falciparum

2011 ◽  
Vol 286 (11) ◽  
pp. 9236-9245 ◽  
Author(s):  
Vinay Bulusu ◽  
Vijay Jayaraman ◽  
Hemalatha Balaram
Keyword(s):  
Side Product ◽  
Salvage Pathway ◽  
Metabolic Fate ◽  
Purine Salvage ◽  
Ofplasmodium Falciparum

scholarly journals Purine nucleoside phosphorylase in chronic lymphocytic leukemia (CLL)

Blood ◽  
1978 ◽  
Vol 52 (5) ◽  
pp. 886-895 ◽  
Author(s):  
M Borgers ◽  
H Verhaegen ◽  
M De Brabander ◽  
J De Cree ◽  
W De Cock ◽  
...  
Keyword(s):  
Chronic Lymphocytic Leukemia ◽  
Healthy Subjects ◽  
Purine Nucleoside Phosphorylase ◽  
Peripheral Blood Lymphocytes ◽  
Lymphocytic Leukemia ◽  
Purine Nucleoside ◽  
Salvage Pathway ◽  
Purine Salvage ◽  
Nucleoside Phosphorylase ◽  
A Minor

Abstract Purine nucleoside phosphorylase (PNP), the enzyme schematically next to adenosine deaminase in the purine salvage pathway, has been demonstrated cytochemically in peripheral blood lymphocytes of healthy subjects and chronic lymphocytic leukemia (CLL) patients. The enzyme activity is confined to the cytosol. In healthy subjects the majority of lymphocytes are strongly reactive for PNP, whereas the rest are devoid of cytochemically demonstrable activity. The percentage of PNP- positive cells largely corresponds to the number of E rosette-forming cells and is inversely proportional to the number of Ig-bearing cells. In six of seven CLL patients studied only a minor percentage of the lymphocytes showed strong PNP activity, whereas the large majority (88%- -98%) possessed trace activity. Such patients have a high number of Ig- bearing cells and a low number of E rosette-forming cells. A different pattern of markers was found in the lymphocytes of the seventh CLL patient: 66% were strongly reactive for PNP, an important number formed E rosettes, and a minor percentage were Ig bearing. These data indicate that PNP can be useful as a “nonmembrane” marker in the differentiation of the B and T cell origin in CLL and deserves to be studied in other lymphoproliferative disorders.

Identification of a novel putative inhibitor of the Plasmodium falciparum purine nucleoside phosphorylase: exploring the purine salvage pathway to design new antimalarial drugs

2017 ◽  
Vol 21 (3) ◽  
pp. 677-695 ◽  
Author(s):  
Luciano Porto Kagami ◽  
Gustavo Machado das Neves ◽  
Ricardo Pereira Rodrigues ◽  
Vinicius Barreto da Silva ◽  
Vera Lucia Eifler-Lima ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Purine Nucleoside Phosphorylase ◽  
Antimalarial Drugs ◽  
Purine Nucleoside ◽  
Salvage Pathway ◽  
Purine Salvage ◽  
Nucleoside Phosphorylase

A KINETIC STUDY OF THE DEAMINATION OF SOME ADENOSINE ANALOGUES: SUBSTRATE SPECIFICITY OF ADENOSINE DEAMINASE

1966 ◽  
Vol 44 (3) ◽  
pp. 331-337 ◽  
Author(s):  
J. Lyndal York ◽  
G. A. LePage
Keyword(s):  
Substrate Specificity ◽  
Kinetic Study ◽  
Adenosine Deaminase ◽  
Competitive Inhibitor ◽  
Kinetic Constants ◽  
Glycosidic Linkage ◽  
Adenosine Analogues ◽  
Substrate Complex ◽  
Enzyme Substrate ◽  
Marked Dependence

The kinetic constants Km and Vmax were determined for the deamination by adenosine deaminase of a series of analogues of adenosine containing "fraudulent" sugars. The configuration of the 2′-hydroxyl was found to be important for the binding of enzyme and substrate. The largest effect of changes in sugar structure was on the rate of breakdown of the enzyme–substrate complex to form products, i.e. Vmax. The nature of the configuration in the 3′-position was not important if the 2′-hydroxyl was trans to the glycosidic linkage; however, if the steric arrangement of the 2′-hydroxyl was cis to the glycosidic linkage, then Vmax showed a marked dependence on the nature of the 3′-substituent and its configuration. For instance, Vmax values were for arabinosyl adenine < 3′-deoxyarabinosyl adenine <lyxosyl adenine. 6-N-methyladenosine was found to be a competitive inhibitor of adenosine deaminase, with a Ki of 2 × 10−6M.

scholarly journals Transport of purines and purine salvage pathway inhibitors by the Plasmodium falciparum equilibrative nucleoside transporter PfENT1

2010 ◽  
Vol 169 (1) ◽  
pp. 40-49 ◽  
Author(s):  
Paul M. Riegelhaupt ◽  
María B. Cassera ◽  
Richard F.G. Fröhlich ◽  
Keith Z. Hazleton ◽  
Jonathan J. Hefter ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Nucleoside Transporter ◽  
Salvage Pathway ◽  
Purine Salvage ◽  
Equilibrative Nucleoside Transporter
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