Characterization and purification of adenosine deaminase 1 from human and chicken liver

Iwaki-Egawa, Sachiko; Watanabe, Yasuhiro

doi:10.1016/s1096-4959(02)00122-7

Cited by 13 publications

(14 citation statements)

References 32 publications

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“…These results reflect that ADAII activity can be modulate by various modulators including substrate analog which may used for controlling the enzyme activity. These results are similar to the substrate specificities of adenosine deaminase from human and Chicken liver (Iwaki-Egawa and Watanabe, 2002), bovine brain (Lupidi et al 1992), rate brain (Centelles et al 1988), san fly Lutzomyia longipalepis, mice intestine (Singh and Sharma 2000) and camel skeletal muscle (Alrokayan 2002).…”

Section: Discussionsupporting

confidence: 74%

Adenosine deaminase from camel tick Hyalomma dromedarii: purification and characterization

Mohamed

2006

Exp Appl Acarol

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Adenosine deaminase is involved in purine metabolism and is a key enzyme for the control of the cellular levels of adenosine. Adenosine deaminase activity showed significant changes during embryogenesis of the camel tick Hyalomma dromedarii. From the elution profile of chromatography on DEAE-sepharose, three forms of enzyme (ADAI, ADAII and ADAIII) were separated. ADAII was purified to homogeneity after chromatography on Sephacryl S-200. The molecular mass of adenosine deaminase ADAII was 42 kDa for the native enzyme and represented a monomer of 42 kDa by SDS-PAGE. The enzyme had a pH optimum at 7.5 and temperature optimum at 40 degrees C with heat stability up to 40 degrees C. ADAII had a K (m) of 0.5 mM adenosine with higher affinity toward deoxyadenosine and adenosine than other purines. Ni(2+), Ba(2+), Zn(2+), Li(2+), Hg(2+) and Mg(2+) partially inhibited the ADAII. Mg(2+) was the strongest inhibitor by 91% of the enzyme's activity.

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Section: Discussionsupporting

confidence: 74%

Adenosine deaminase from camel tick Hyalomma dromedarii: purification and characterization

Mohamed

2006

Exp Appl Acarol

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“…Pairwise alignments of the L. donovani AAH primary structure with each of the Leishmania and S. cerevisiae counterparts revealed 94 and 38% amino acid identities with the other leishmanial and the S. cerevisiae Aah1p AAH sequences, respectively. Comparison of the L. donovani AAH with functionally characterized ADA proteins from Plasmodium falciparum, P. vivax (75), E. coli (76), Mus musculus (38,77), and Homo sapiens (78,79) demonstrated that the AAH from L. donovani was 23-25% identical to the two Plasmodium ADAs, 27% identical to the E. coli ADA, and 23-24% identical to the two mammalian ADAs.…”

Section: Multiple Sequence Alignment Of L Donovani Aah-the Lmentioning

confidence: 99%

Adenine Aminohydrolase from Leishmania donovani

Boitz

Strasser

Hartman

et al. 2012

Journal of Biological Chemistry

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Background: Purine salvage in Leishmania is an indispensable nutritional process. Results: Adenine aminohydrolase, a key purine enzyme in Leishmania, has been characterized biochemically and genetically. Conclusion: Adenine aminohydrolase is a unique enzyme in purine salvage that converts 6-aminopurines into 6-oxypurines. Significance: Functional characterization of key enzymes is crucial for understanding purine salvage and ultimately for targeting the pathway with drugs.

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“…The kinetic data obtained in this study are in accordance with other studies related to ADA activity, although there are some variations of K M among different ADA members. The K M value of H. dromedarii ADA2 was estimated to 0.5 mM adenosine (Mohamed, 2006), which is relatively close to several ADAs from different sources, such as rat brain (0.45 mM) (Centelles et al ., 1988), bovine brain (0.4 mM) (Lupidi et al ., 1992), human (0.46 mM) and chicken liver (0.33 mM) (Iwaki‐Egawa & Watanabe, 2002). However, lower K M values were reported for ADA activity from mice intestine (0.023 mM) (Singh & Sharma, 2000) and from the sand fly Lutzomyia longipalpis (0.01 mM) (Charlab et al ., 2000).…”

Section: Discussionmentioning

confidence: 99%

Kinetic characterization and gene expression of adenosine deaminase in intact trophozoites of Trichomonas vaginalis

Weizenmann¹,

Frasson²,

Barros³

et al. 2011

FEMS Microbiology Letters

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Trichomonas vaginalis is a parasite that resides in the human urogenital tract and causes trichomonosis, the most prevalent nonviral sexually transmitted disease. Nucleoside triphosphate diphosphohydrolase (NTPDase), which hydrolyzes extracellular di- and triphosphate nucleotides, and ecto-5'-nucleotidase, which hydrolyzes AMP, have been characterized in T. vaginalis. The aim of this study was to characterize the adenosine deaminase (ADA) activity in intact trophozoites of T. vaginalis. A strong inhibition in adenosine deamination was observed in the presence of calcium and magnesium, which was prevented by EDTA. The apparent K(M) value for adenosine was 1.13 ± 0.07mM. The calculated V(max) was 2.61 ± 0.054 nmol NH(3) min(-1) mg(-1) protein. Adenosine deamination was inhibited in the presence of erythro-9-(2-hydroxy-3-nonyl)adenine. Semi-quantitative reverse transcriptase-PCR experiments were performed and both ADA-related genes ada(125) and ada(231) mRNA were expressed, although ada(231) in higher quantity when compared with the ada(125) : α-tubulin ratio. Furthermore, a phylogenetic analysis showed that the T. vaginalis sequences formed a clade with Entamoeba histolytica and Dictyostelium discoideum sequences, and it strongly suggests homologous functions in the T. vaginalis genome. The presence of ADA activity in T. vaginalis may be important to modulate the adenosine/inosine levels during infection and, consequently, to maintain the anti-inflammatory properties through different nucleoside-signalling mechanisms.

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Characterization and purification of adenosine deaminase 1 from human and chicken liver

Cited by 13 publications

References 32 publications

Adenosine deaminase from camel tick Hyalomma dromedarii: purification and characterization

Adenosine deaminase from camel tick Hyalomma dromedarii: purification and characterization

Adenine Aminohydrolase from Leishmania donovani

Kinetic characterization and gene expression of adenosine deaminase in intact trophozoites of Trichomonas vaginalis

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