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Results for “Nucleoside Deaminases”

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At least 19 recordsLinked to original sources
PubMed1970

Nucleoside deaminase: an enzymatic marker for stress erythropoiesis in the mouse.

The level of nucleoside deaminase was determined in extracts of mouse tissues obtained during a period of accelerated erythropoiesis induced by hypoxia, hemorrhage, or the injection of phenylhydrazine. Under these conditions a striking (10- to 100-fold) elevation of the enzyme activity occurred in the spleen. Similar results were obtained with the injection of purified erythropoietin. In control animals, only a trace of nucleoside deaminase activity was detected in the blood. During the reticulocyte response which followed erythropoietic stimulation, there was a sharp increase in the blood level of nucleoside deaminase, which rose up to 120 times that of control animals. By differential centrifugation, the enzyme was localized to the reticulocyte-rich fraction. Erythrocyte nucleoside deaminase remained elevated even after the reticulocyte count had fallen to normal in the phenylhydrazine-treated mice or to zero after the cessation of hypoxia. There was a very gradual decline in the enzyme activity in the blood which fell to the barely detectable control levels about 45 days after the initial reticulocyte response, a time period which corresponds to the survival of the mouse red blood cell. The persistence of high levels of nucleoside deaminase for the full life span of a generation of erythrocytes formed during stress, viewed in contrast to the virtual absence of the enzyme from normal erythrocytes of all ages, represents an enzymatic difference between the normal red blood cell and the cell produced under conditions of accelerated erythropoiesis.

Aminohydrolases↗
PubMed1991

The measurement of nucleoside deaminases by high performance liquid chromatography and their use in clinical chemistry.

The measurement of the nucleoside deaminases--cytidine deaminase, guanosine deaminase and adenosine deaminase--by reversed phase high performance liquid chromatography is reviewed. The clinical value of assaying the enzyme activity is discussed for each of these enzymes. Both cytidine deaminase and adenosine deaminase measurements have proven clinical value, although the use of the assay of cytidine deaminase in the diagnosis of pre-eclampsia is probably not helpful.

Adenosine Deaminase↗
PubMedDate not supplied

Adenosine deaminase, nucleoside phosphorylase and hypoxanthine-guanine phosphoribosyltransferase activity in normal lymphocyte subpopulations.

Adenosine deaminase (ADA), purine nucleoside phosphorylase (PNP), and hypoxanthine-guanine phosphoribosyltransferase (HGPRT) activities were measured in normal human B lymphocytes, T lymphocytes, and T gamma and T mu lymphocyte subsets. Total ADA activity in T cells was 5.5U, activity in T gamma and T mu cells was 3.7U and 5.3U, respectively; B cell ADA levels were 3.3U. PNP activity in T cells was 119U, activity in T gamma and T mu cells was 75U and 155U, respectively. B cell PNP activity was 88U. HGPRT activity in T cells was 20.9U; T gamma and T mu HGPRT levels were 13.0U and 52U respectively. B cell HGPRT levels were 46.8U. These data provides further evidence for the biochemical heterogeneity of normal human lymphocytes.

Adenosine Deaminase↗
PubMed1976

Correlation analysis of Baker's studies on enzyme inhibition. 2. Chymotrypsin, trypsin, thymidine phosphorylase, uridine phosphorylase, thymidylate synthetase, cytosine nucleoside deaminase, dihydrofolate reductase, malate dehydrogenase, glutamate dehydrogenase, lactate dehydrogenase, and glyceraldehyde-phosphate dehydrogenase.

The inhibitory activity of 1058 inhibitors of the title enzymes has been formulated in 13 equations correlating chemical structure with inhibitory potency. Two types of regions in enzymes have been defined by means of pi and molar refractivity constants. The use of indicator variables has been extensively developed to suggest special enzyme-ligand interactions. Several examples are given of the use of correlation equations in comparing structural features of different systems.

Animals↗
PubMed1978

Deoxycytidine kinase and cytosine nucleoside deaminase activities in synchronized cultures of normal rat kidney cells.

Previous work has suggested that 1-beta-D-arabinofuranosylcytosine 5'-triphosphate is the active metabolite of 1-beta-D-arabinofuranosylcytosine. The amount of 1-beta-D-arabinofuranosylcytosine 5'-triphosphate formed in tissues has been shown to be influenced by the relative levels of deoxycytidine kinase and cytosine deaminase. In this study we have measured the intracellular levels of deoxycytidine kinase and cytosine deaminase activities in synchronized cultures of normal rat kidney cells. The deoxycytidine kinase activity was found to be cell cycle related with a minor peak of activity in early G1 phase and a major peak of activity in middle and late S phase. The cytosine deaminase activity was also found to be cycle dependent with a peak of activity at G1 phase and another at S phase of the cell cycle. Similar results were obtained when cytosine deaminase activities were measured with cytidine, deoxycytidine, or 1-beta-D-arabinofuranosylcytosine as substrate. Present studies also confirmed earlier studies by other workers that the main effect of 1-beta-D-arabinofuranosylcytosine is in the late S phase of the cell cycle.

Cell Cycle↗
PubMed1995

The nucleoside deaminases for cytidine and adenosine: structure, transition state stabilization, mechanism, and evolution.

Enzymatic deamination of cytidine and adenosine bases in RNA have recently been shown to be mechanisms for changing the coding specificity of messenger and transfer RNAs. The structures of the enzymes that carry out deamination of the corresponding nucleosides have been analyzed by X-ray crystallography. They are quite different from one another in most respects, including quaternary and tertiary structure, but they have similar chemical groups in their active sites. Both enzymes envelope their nucleoside substrates completely, perhaps accounting for the fact that they are inactive on RNA substrates. Much has been learned about catalytic mechanisms from the structures of the enzymes and their complexes with transition state analog inhibitors. Catalysis proceeds with the activation by zinc of a bound water molecule, presumably to hydroxide ion, which attacks the appropriate carbon to generate a tetrahedral intermediate. The detailed stereochemistry of the two resulting chiral centers is diastereoisomeric. Details of the ensuing proton transfer steps necessary to generate and release the products are also apparently different in the two enzymes. Thus, the active site similarities are probably the result of convergent evolution.

Adenosine Deaminase↗
PubMed1993

Are there limits to enzyme-inhibitor binding discrimination? Inferences from the behavior of nucleoside deaminases.

An enzyme can enhance the rate of a reaction only to the extent that it binds the altered substrate in the transition state (S not equal to) more tightly than it binds the substrate in the ground state. Inhibitors that resemble S not equal to can be used to stop an enzyme from working, probe its mechanism of action and obtain exact structural information about intermediates in catalysis. In S not equal to analog inhibitors of adenosine and cytidine deaminases, a single hydroxyl group appears to make extremely large contributions to binding affinity. The magnitude of this contribution becomes even more striking when differences in free energy of solvation by water are taken into account. Other results, obtained by deleting individual binding determinants, indicate the operation of remarkable levels of cooperativity and suggest that if every group is in exactly the right position and is part of an inflexible structure, then a single substituent or H-bond can produce very large increases in binding affinity. Some implications for inhibitor design are considered.

Aminohydrolases↗