Characterization of an ecto-5 ′-nucleotidase (EC 3.1.3.5) activity in intact cells of Trichomonas vaginalis
The enzymatic properties of an ecto-5 ′-nucleotidase were described in Trichomonas vaginalis. The enzyme hydrolyzes nucleoside monophosphates in optimum pH values of 7.5 and 6.5 for the 30236 strain and for the 30238 strain, respectively. Mg 2+ and Ca 2+ were activators of AMP hydrolysis in both str...
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Published in | Experimental parasitology Vol. 105; no. 2; pp. 167 - 173 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
San Diego, CA
Elsevier Inc
01.10.2003
Elsevier |
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Abstract | The enzymatic properties of an ecto-5
′-nucleotidase were described in
Trichomonas vaginalis. The enzyme hydrolyzes nucleoside monophosphates in optimum pH values of 7.5 and 6.5 for the 30236 strain and for the 30238 strain, respectively. Mg
2+ and Ca
2+ were activators of AMP hydrolysis in both strains. The apparent
K
m (Michaelis constant) values for Mg
2+-AMP were 111.4
±
28.1
μM (mean
±
SD,
n=3) for 30236 strain and 420.2
±
35.7
μM (mean
±
SD,
n=3) for 30238 strain. The ecto-5
′-nucleotidase activity was insensitive to levamisole and tetramisole, inhibitors of alkaline phosphatases, whereas α,β-methylene-ADP inhibited the enzymatic activity of both strains. Our results showed that the AMP hydrolysis presents differences in some kinetic parameters between the two strains investigated. An analysis of the enzymatic chain involved in the ATP hydrolysis to adenosine will contribute to understanding the biochemical aspects of the parasite and the mechanisms related to host–parasite interactions.
Index Descriptors and Abbreviations: Trichomonas vaginalis; Parasitic protozoan; Intact cells; Ecto-5
′-nucleotidase; Adenosine; ATP, adenosine 5
′-triphosphate; ADP, adenosine 5
′-diphosphate; AMP, adenosine 5
′-monophosphate; NTPDase1, nucleoside triphosphate diphosphohydrolase 1 (EC 3.6.1.5); NTPDase2, nucleoside triphosphate diphosphohydrolase 2 (EC 3.6.1.3); Ecto-5
′-nucleotidase (EC 3.1.3.5); CMP, cytidine 5
′-monophosphate; UMP, uridine 5
′-monophosphate; IMP, inosine 5
′-monophosphate; GMP, guanosine 5
′-monophosphate,
K
m, Michaelis constant;
V
max, maximum velocity; 3
′,5
′-cAMP, adenosine 3
′, 5
′-cyclic monophosphate; NAD
+, nicotinamide adenine dinucleotide; Ap
nA, diadenosine polyphosphates; AMPCP, α,β-methylene adenosine diphosphate. |
---|---|
AbstractList | The enzymatic properties of an ecto-5'-nucleotidase were described in Trichomonas vaginalis. The enzyme hydrolyzes nucleoside monophosphates in optimum pH values of 7.5 and 6.5 for the 30236 strain and for the 30238 strain, respectively. Mg(2+) and Ca(2+) were activators of AMP hydrolysis in both strains. The apparent K(m) (Michaelis constant) values for Mg(2+)-AMP were 111.4+/-28.1 microM (mean+/-SD, n=3) for 30236 strain and 420.2+/-35.7 microM (mean+/-SD, n=3) for 30238 strain. The ecto-5'-nucleotidase activity was insensitive to levamisole and tetramisole, inhibitors of alkaline phosphatases, whereas alpha,beta-methylene-ADP inhibited the enzymatic activity of both strains. Our results showed that the AMP hydrolysis presents differences in some kinetic parameters between the two strains investigated. An analysis of the enzymatic chain involved in the ATP hydrolysis to adenosine will contribute to understanding the biochemical aspects of the parasite and the mechanisms related to host-parasite interactions. The enzymatic properties of an ecto-5 ′-nucleotidase were described in Trichomonas vaginalis. The enzyme hydrolyzes nucleoside monophosphates in optimum pH values of 7.5 and 6.5 for the 30236 strain and for the 30238 strain, respectively. Mg 2+ and Ca 2+ were activators of AMP hydrolysis in both strains. The apparent K m (Michaelis constant) values for Mg 2+-AMP were 111.4 ± 28.1 μM (mean ± SD, n=3) for 30236 strain and 420.2 ± 35.7 μM (mean ± SD, n=3) for 30238 strain. The ecto-5 ′-nucleotidase activity was insensitive to levamisole and tetramisole, inhibitors of alkaline phosphatases, whereas α,β-methylene-ADP inhibited the enzymatic activity of both strains. Our results showed that the AMP hydrolysis presents differences in some kinetic parameters between the two strains investigated. An analysis of the enzymatic chain involved in the ATP hydrolysis to adenosine will contribute to understanding the biochemical aspects of the parasite and the mechanisms related to host–parasite interactions. Index Descriptors and Abbreviations: Trichomonas vaginalis; Parasitic protozoan; Intact cells; Ecto-5 ′-nucleotidase; Adenosine; ATP, adenosine 5 ′-triphosphate; ADP, adenosine 5 ′-diphosphate; AMP, adenosine 5 ′-monophosphate; NTPDase1, nucleoside triphosphate diphosphohydrolase 1 (EC 3.6.1.5); NTPDase2, nucleoside triphosphate diphosphohydrolase 2 (EC 3.6.1.3); Ecto-5 ′-nucleotidase (EC 3.1.3.5); CMP, cytidine 5 ′-monophosphate; UMP, uridine 5 ′-monophosphate; IMP, inosine 5 ′-monophosphate; GMP, guanosine 5 ′-monophosphate, K m, Michaelis constant; V max, maximum velocity; 3 ′,5 ′-cAMP, adenosine 3 ′, 5 ′-cyclic monophosphate; NAD +, nicotinamide adenine dinucleotide; Ap nA, diadenosine polyphosphates; AMPCP, α,β-methylene adenosine diphosphate. |
Author | Tasca, Tiana Bonan, Carla D Carli, Geraldo A.De Sarkis, João J.F Battastini, Ana M.O |
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Keywords | Characterization Trichomonas vaginalis Parasite Protozoa Activity Trichomonadida |
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Snippet | The enzymatic properties of an ecto-5
′-nucleotidase were described in
Trichomonas vaginalis. The enzyme hydrolyzes nucleoside monophosphates in optimum pH... The enzymatic properties of an ecto-5'-nucleotidase were described in Trichomonas vaginalis. The enzyme hydrolyzes nucleoside monophosphates in optimum pH... |
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SubjectTerms | 5'-Nucleotidase - antagonists & inhibitors 5'-Nucleotidase - metabolism Adenosine Monophosphate - metabolism Alkaline Phosphatase - antagonists & inhibitors Animals Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences Calcium - metabolism Experimental protozoal diseases and models Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolysis Infectious diseases Kinetics Magnesium - metabolism Medical sciences Parasitic diseases Protozoa Protozoal diseases Trichomonas vaginalis - enzymology |
Title | Characterization of an ecto-5 ′-nucleotidase (EC 3.1.3.5) activity in intact cells of Trichomonas vaginalis |
URI | https://dx.doi.org/10.1016/j.exppara.2003.12.001 https://www.ncbi.nlm.nih.gov/pubmed/14969694 https://search.proquest.com/docview/71535964 |
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