Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.5.1.4 (deaminase)
5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The apparent size (87.5 kDa) of the major polypeptide in freshly isolated chicken muscle AMP deaminase (AMPD.M) was comparable with that predicted from the sequences of the genes for the major muscle isoforms from human and rat. The size of the subunit of AMP deaminase from chicken muscle is indistinguishable from that of the rabbit enzyme. The peptide profiles of cyanogen bromide digests of AMPD.M from chicken and rabbit share a 17-kDa fragment, representing approximately 20% of the intact subunits of these enzymes. The first 25 residues of these fragments are 88.5% identical; the rabbit and chicken segments are greater than 92% and 84% identical, respectively, to the sequences predicted for residues 310-335 for AMPD.M from human and rat. Polyclonal rabbit antisera directed against AMPD.M from chicken breast recognize the full-length AMPD.M polypeptides on immunoblots of extracts of both avian and rabbit muscle, including an antiserum from the rabbit in which the antibody was prepared. The 17-kDa fragments, derived by incomplete cleavage of highly conserved internal segments of the deaminase subunit, share epitopes involved in the autorecognition of rabbit AMPD.M by rabbit polyclonal antibodies directed against the avian AMPD.M.
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PMID:AMP-deaminases from chicken and rabbit muscle: partial primary sequences of homologous 17-kDa CNBr fragments: autorecognition by rabbit anti-[chicken AMPD]. 911 97

A 14-year-old boy with exercise-related myalgia and cramps had several episodes of myoglobinuria since early childhood. An episode at 2 years of age caused acute renal failure. Histochemical and biochemical analysis of muscle showed a combined defect of phosphofructokinase (PFK) and adenosine monophosphate (AMP) deaminase. DNA analysis showed that the patient was homozygous for a G-to-C substitution at codon 39 of the PFK gene (previously described in an Italian patient) and for the common mutation found in AMP deaminase deficiency.
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PMID:Combined defects of muscle phosphofructokinase and AMP deaminase in a child with myoglobinuria. 944

Abnormal elevations in ammonia have been implicated in the pathogenesis of Alzheimer's disease. However, the biochemical mechanism(s) leading to increased ammonia in Alzheimer's disease have not yet been identified. A potential source of increased ammonia production is adenosine monophosphate (AMP) deaminase, an important enzyme in the regulation of the purine nucleotide cycle and adenylate energy charge. AMP deaminase activity is expressed in human brain and converts AMP to inosine monophosphate with the release of ammonia. We have investigated AMP deaminase activity in postmortem brain tissue from Alzheimer's disease subjects and age-matched controls. Compared to control brain, Alzheimer's disease brain AMP deaminase activity is 1.6- to 2.4-fold greater in the regions examined--the cerebellum, occipital cortex, and temporal cortex. Similar increases in AMP deaminase protein and mRNA levels are observed in Alzheimer's disease brain. These results suggest that increased AMP deaminase activity may augment ammonia levels in the brain in Alzheimer's disease.
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PMID:Elevated adenosine monophosphate deaminase activity in Alzheimer's disease brain. 988 40

Adenosine monophosphate deaminase (AMPD; EC 3.5.4.6) catalyses the hydrolysis of adenosine monophosphate (AMP) to commensurate amounts of inosine monophosphate (IMP) and ammonia. The production of AMP deaminase in Candida albicans was measured in Lee's medium grown cultures. The highest AMPD activity was observed at 24 h of growth. The enzyme had an optimum pH and temperature at 6-7 and 28 degrees C, respectively. This enzyme was inhibited under iron-limited growth conditions as well as by protease inhibitors. The AMPD of C. albicans showed a moderate increase in activity when cultures were grown in the presence of the divalent cations Mg2+, Ca2+, and Zn2+. Moreover, ADP, ATP, adenine, adenosine, deoxyribose and hypoxanthine increased the enzyme activity. Cultures grown in trypticase soy broth exhibited maximum AMPD activity compared with those grown in Sabouraud dextrose broth or Lee's medium.
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PMID:Properties of adenosine monophosphate deaminase of Candida albicans. 1039 42

Slices of rat hippocampus can be induces to generate spontaneous interictal-like bursts of action potentials when perfused with a with a medium containing no added magnesium and 4-aminopyridine (4AP). The frequency of these bursts is depressed by adenosine 5'triphosphate (ATP) and this effect can be prevented by cyclopentyltheophylline but not by adenosine deaminase. AMP (50 microM) had a similar action to reduce discharge rate. At 10 microM, adenosine, diadenosine tetraphosphate and diadenosine pentaphosphate all decreased the burst frequency. Adenosine deaminase (0.2 U ml-1) totally annulled the inhibition of epileptiform activity produced by 10 microM adenosine but reduced only the later components of the inhibition by 10 microM diadenosine tetraphosphate and diadenosine pentaphosphate. Cyclopentyltheophylline prevented the depression of burst discharges by diadenosine tetraphosphate. 5'-adenylic acid deaminase (AMPPase) did not significantly alter the discharge rate over the 10 min superfusion period used for drum application but did prevent the depressant effect of AMP and ATP. AMP deaminase did not prevent the inhibitory effects of diadenosine tetraphosphate. The results suggests that in the CA3 region of the hippocampus, diadenosine tertraphosphate and diadenosine pentaphosphate act partly by stimulating xanthine sensitive receptors directly and partly via metabolism to adenosine, and that AMP may be responsible for the inhibitory effects of ATP on epileptiform activity.
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PMID:Nucleotide and dinucleotide effects on rates of paroxysmal depolarising bursts in rat hippocampus. 1055 Oct 2

Because micromolar concentrations of adenosine (Ado) have been documented recently in the interstitial fluid of carcinomas growing in animals, we examined the effects of low concentrations of Ado on the growth of cultured human carcinoma cells. Ado alone had little effect upon cell growth. In the presence of one of a number of Ado deaminase (ADA) inhibitors, Ado led to significant growth inhibition of all cell lines tested. Similar effects were found when ATP, ADP, or AMP was substituted for Ado. Surprisingly, the ADA inhibitor coformycin (CF) had a much greater potentiating effect than did 2'-deoxycoformycin (DCF), although DCF is a more potent ADA inhibitor. The growth inhibition of the Ado/CF combination was not abrogated by pyrimidines or caffeine, a nonspecific Ado receptor blocker. Toxicity was prevented by the addition of the Ado transport inhibitor dipyridamole or the Ado kinase inhibitor 5'-amino 5'-deoxyadenosine. S-Adenosylhomocysteine hydrolase is not involved because neither homocysteine thiolactone nor an S-adenosylhomocysteine hydrolase inhibitor (adenosine dialdehyde) potentiated toxicity of the Ado/CF combination. Unexpectedly, substitution of 2'-deoxyadenosine (the toxic moiety in congenital ADA deficiency) for Ado, did not lead to equivalent toxicity. The Ado/CF combination inhibited DNA synthesis and brought about morphological changes consistent with apoptosis. Together, these findings indicate that the Ado-mediated killing proceeds via an intracellular route that requires the action of Ado kinase. The enhanced cofactor activity of CF may be attributable to its being a more potent inhibitor of AMP deaminase than is DCF.
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PMID:Adenosine-mediated killing of cultured epithelial cancer cells. 1076 76

The dry powdered of Sinapis arvensis, Thymelaea hirsuta, Callistemon lanceolatus and Peganum harmala showed molluscicidal activity against Biomphalaria alexandrina, specific intermediate hosts to Schistosoma mansoni. Effect of LC25 of dry powdered plant molluscicides on hexokinase (HK), glucose phosphate isomerase (GPI), AMP deaminase, adenosine deaminase and phenol oxidase (PO) of B. alexandrina was traced. C. lanceolatus showed the highest molluscicidal activity as it has the lowest LC50 compared to S. arvensis, T. hirsuta, and P. harmala. LC25 of the latter three plants resulted in more significant inhibition of HK, GPI, AMP-deaminase and PO than C. lanceolatus. Treatment of snails with LC10 of these plants markedly affected compatibility of B. alexandrina to S. mansoni infection. Significant decrease in cercarial production recorded in snails treated with sublethal concentrations of S. arvensis, T. hirsuta, and P. harmala. Remarkable impairment of the egg laying capacity of molluscicide-treated snails was also recorded. Correlation between activity levels of HK, GPI and AMP deaminase and compatibility to parasitic infection and role of PO in the egglaying capacity of these snail species were discussed.
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PMID:In vivo, attenuation of schistosome cercarial development and disturbance of egg laying capacity in Biomphalaria alexandrina using sublethal concentrations of plant molluscicides. 1177 93

Blood lymphocyte activities of 5'-nucleotidases, adenosine deaminase and AMP deaminase have been investigated for evaluation of immune system state of albino rats under normal conditions, immobilization stress and effect of radiation. Stress-induced reactions were characterized by changes of activities of these enzymes. However the ratios of activities 5'- nucleotidase/AMP-deaminase (coefficient A) and adenosine-deaminase/AMP-deaminase (coefficient B) were even more informative than separate analysis of these enzymes.
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PMID:[Enzymes of purine nucleotide metabolism in assessment of the functional competence of the immune system]. 1594 54

Adenosine deaminase (ADA) is a well-characterized enzyme involved in the depletion of adenosine levels. A group of proteins with similarity to ADA, the adenosine deaminase-related growth factors (ADGF; known as CECR1 in vertebrates), has been described recently in various organisms. We have determined the phylogenetic relationships of various gene products with significant amino acid similarity to ADA using parsimony and Bayesian methods, and discovered a novel paralogue, termed ADA-like (ADAL). The ADGF proteins share a novel amino acid motif, "MPKG," within which the proline and lysine residues are also conserved in the ADAL and ADA subfamilies. The significance of this new domain is unknown, but it is located just upstream of two ADA catalytic residues, of which all eight are conserved among the ADGF and ADAL proteins. This conservation suggests that ADGF and ADAL may share the same catalytic function as ADA, which has been proven for some ADGF members. These analyses also revealed that some genes previously thought to be classic ADAs are instead ADAL or ADGFs. We here define the ADGF, ADAL, ADA, adenine deaminase (ADE), and AMP deaminase (AMPD) groups as subfamilies of the adenyl-deaminase family. The availability of genomic data for the members of this family allowed us to reconstruct the intron evolution within the phylogeny and strengthen the introns-late hypothesis of the synthetic introns theory. This study shows that ADA activity is clearly more complex than once thought, perhaps involving a delicately balanced pattern of temporal and spatial expression of a number of paralogous proteins.
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PMID:Phylogenetic analysis reveals a novel protein family closely related to adenosine deaminase. 1624 11

Embryonic factor 1 (FAC1) is one of the earliest expressed plant genes and encodes an AMP deaminase (AMPD), which is also an identified herbicide target. This report identifies an N-terminal transmembrane domain in Arabidopsis FAC1, explores subcellular fractionation, and presents a 3.3-A globular catalytic domain x-ray crystal structure with a bound herbicide-based transition state inhibitor that provides the first glimpse of a complete AMPD active site. FAC1 contains an (alpha/beta)(8)-barrel characterized by loops in place of strands 5 and 6 that places it in a small subset of the amidohydrolase superfamily with imperfect folds. Unlike tetrameric animal orthologs, FAC1 is a dimer and each subunit contains an exposed Walker A motif that may be involved in the dramatic combined K(m) (25-80-fold lower) and V(max) (5-6-fold higher) activation by ATP. Normal mode analysis predicts a hinge motion that flattens basic surfaces on each monomer that flank the dimer interface, which suggests a reversible association between the FAC1 globular catalytic domain and intracellular membranes, with N-terminal transmembrane and disordered linker regions serving as the anchor and attachment to the globular catalytic domain, respectively.
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PMID:Membrane association, mechanism of action, and structure of Arabidopsis embryonic factor 1 (FAC1). 1654 43


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