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)

Chromatography on phosphocellulose P-11 under conditions different from those applicable for deaminases specific to 5' AMP resulted in homogeneous preparation of snail foot muscle enzyme. Snail deaminase is a tetramer with molecular weight of 240,000, composed of four apparently identical subunits. Its amino acid composition is remarkably different from deaminases of higher animals, it was not inhibited by EDTA, but zinc became inhibitory to the snail enzyme. Unlike deaminases specific to 5' AMP, nonspecific deaminase is not a zinc-containing enzyme. It was adopted further for the preparation of hypoxanthine derivatives of adenosine-containing nucleotides such as NAD, NADH, AMP-P(NH)P, AMP, ADP and ATP.
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PMID:Nonspecific snail muscle adenylate deaminase: simplified purification, characterization and use for the preparation of deamino derivatives of NAD, NADH and AMP-P(NH)P. 380 47

The OA-6129 group of carbapenem antibiotics were phosphorylated with ATP by Brevibacterium ammoniagenes at the primary hydroxyl group of the C-3 pantetheinyl side chain. The phosphorylation resulted in the reduced antimicrobial activity against some Gram-positive bacteria, and the improved activity against some Gram-negative microbes. The increased resistance of the OA-6129 carbapenems due to phosphorylation was significant to mouse renal dehydropeptidase and moderate to the human enzyme. OA-6129A and B2 phosphates were found to be unsusceptible to A933 acylase, while OA-6129A and B2 were depantothenylated.
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PMID:Microbial phosphorylation of the OA-6129 group of carbapenem compounds. 383 25

In adipocytes, adenylate cyclase is positively regulated by beta-adrenergic agents and negatively regulated by adenosine. Incubation of adipocytes with adenosine deaminase relieves the inhibition of adenylate cyclase by destroying the adenosine that the cells release into the medium. When adipocytes are incubated with adenosine deaminase and the beta-adrenergic agent isoproterenol, most of their ATP is converted to AMP in 5 min. Either isoproterenol or adenosine deaminase alone has little or no effect. In the additional presence of the phosphodiesterase inhibitor 4-(3-butoxy-4-methoxybenzyl)imidazolidin-2-one (Ro 20-1724) cAMP accumulates instead of AMP. Under these conditions, cAMP represents 40-50% of the total intracellular adenine nucleotides, and ATP only 5%. N6-(L-2-phenylisopropyl)adenosine, a deaminase-resistant adenosine agonist, prevents beta-adrenergic stimulation. 8-(p-Sulfophenyl)theophylline and 3-isobutyl-1-methylxanthine are both adenosine antagonists that can replace the deaminase in permitting beta-adrenergic stimulation of adenylate cyclase, but only the latter also inhibits the phosphodiesterase and causes accumulation of cAMP. When the ATP-depleted adipocytes are washed with fresh medium, the nucleoside triphosphate level can be restored within 5 min. The ATP-restored adipocytes can respond rapidly to a second dose of isoproterenol and adenosine antagonist. These findings point out the important role of adenosine in controlling adenylate cyclase activity and the possible involvement of adenylate cyclase in the control of energy flow in rat adipocytes.
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PMID:Extensive but reversible depletion of ATP via adenylate cyclase in rat adipocytes. 385 40

In beef heart AMP-deaminase (EC 3.5.4.6.), 7 SH-groups out of 26 half-cysteine residues in the protein molecule have been shown to be accessible to alkylation by DTNB in the absence of ATP. The addition of ATP showed that only 6 SH-groups were accessible. DTNB-modified enzyme showed about 30% of the native catalytic activity but no sensitivity to the ATP-activating effect. Almost full reactivation of the modified enzyme and the restoration of the activatory effect of ATP could be achieved by exhaustive dialysis against mercaptoethanol.
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PMID:Modification of the catalytic and regulatory properties of beef heart AMP-deaminase by DTNB treatment. 399 29

Four thoroughbred horses performed 4 gallops (G1-G4) with intervals of 5 min. With one exception, gallops were sustained at maximal speed over 620 m. Muscle biopsy samples of the middle gluteal and brachiocephalicus were taken before, during, and after exercise and assayed for ATP and intermediary metabolites. The results showed a major involvement of the brachiocephalicus, in addition to the middle gluteal, during galloping. In three horses, who were clearly fatigued, muscle ATP decreased by up to 50% by the end of G4. This was matched by an equal rise in inosine 5'-monophosphate. Pronounced accumulations of glycerol 3-phosphate, glycerol, and lactate (up to 204 mmol X kg dry muscle-1) occurred with exercise. In the fourth horse, which was less fatigued, a decrease in ATP and increases in intermediary metabolites were much less. Postexercise there was little or no recovery in muscle ATP or lactate during 30 min. The decreases in ATP are consistent with a high activity of adenosine 5'-monophosphate deaminase in horse muscle and indicative also of the high level of anaerobic stress of the exercise program. There was evidence to suggest that the increase in muscle glycerol resulted from hydrolysis of glycerol 3-phosphate and not from the utilization of triglyceride.
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PMID:Metabolic response of equine muscle to intermittent maximal exercise. 399 31

The binding of the fluorescent probe 4,4'-bis[8-(phenylamino)naphthalene-1-sulfonate] (bis-ANS) to human alpha- and gamma-thrombins was investigated. Bis-ANS binds in a 1:1 complex to both forms of the enzyme, with Kd = 14.8 +/- 2.2 microM and 5.8 +/- 1.0 microM for alpha- and gamma-thrombin, respectively, at pH 7.0 [25 mM tris(hydroxymethyl)aminomethane, 0.15 M NaC1]. Fluorescence changes upon complexation included a considerable (approximately 30-nm) blue shift in the fluorescence emission maximum as well as a dramatic increase in the fluorescence emission intensity: a 70-fold enhancement was observed with alpha-thrombin vs. a approximately 220-fold enhancement with gamma-thrombin. Proflavin was not displaced upon bis-ANS binding. The unknown thrombin effectors ATP, Ca(II)ATP, Co(III)ATP, phosphate, and pyrophosphate bound with enhancement of the fluorescence of the bis-ANS-alpha-thrombin complex. The two inhibitors benzamidine and p-chlorobenzylamine as well as heparin caused decreases in bis-ANS-thrombin fluorescence: valerylamidine had no effect on the fluorescence of the bis-ANS-thrombin complex. Kinetic measurements with two chromogenic substrates, S-2238 and S-2160, indicated that bis-ANS acts as a partial noncompetitive inhibitor of thrombin amidase activity. The kinetic evidence combined with the ligand binding results suggests that bis-ANS does not overlap the catalytic site. The fluorophore ANS complexed with equal affinity to both alpha- and gamma-thrombins (Kd = 24 +/- 4 microM); however, the gamma-thrombin-ANS complex emission at 470 nm was enhanced 26% more than that for the alpha form.
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PMID:4,4'-Bis[8-(phenylamino)naphthalene-1-sulfonate] binding to human thrombins: a sensitive exo site fluorescent affinity probe. 401 98

1. Pseudomonas sp. N.C.I.B. 8858 grew well on d- and l-1-aminopropan-2-ol and on aminoacetone. 2. Cell-free extracts possessed high activities of inducibly formed l-1-aminopropan-2-ol-NAD(+) oxidoreductase, amino alcohol-ATP phosphotransferase, dl-1-aminopropan-2-ol O-phosphate phospho-lyase and aldehyde-NAD(+) oxidoreductase, but no 1-aminopropan-2-ol racemase or d-1-aminopropan-2-ol-NAD(+) oxidoreductase. 3. The amino alcohol kinase (activated by ADP) was non-stereospecific towards 1-aminopropan-2-ol and was one-third as active with ethanolamine. The phospho-lyase was active with l- and d-1-aminopropan-2-ol O-phosphate, but ethanolamine O-phosphate was only one-tenth as active as its higher homologues. The purified aldehyde dehydrogenase was active with propionaldehyde, acetaldehyde and also with methylglyoxal. The previously observed 2-oxo aldehyde dehydrogenase activity was considered to be due to the broadly specific aldehyde dehydrogenase. 4. Mutants of Pseudomonas sp. N.C.I.B. 8858 deficient in 1-aminopropan-2-ol kinase, 1-aminopropan-2-ol O-phosphate phospho-lyase, aldehyde dehydrogenase or an enzyme involved in propionate metabolism were incapable of growth on aminoacetone or 1-aminopropan-2-ol as carbon source, although all except the kinase- or phospho-lyasedeficient mutants could use these compounds and ethanolamine as nitrogen sources. The aldehyde dehydrogenase-deficient mutants produced copious amounts of propionaldehyde and acetaldehyde during growth on the corresponding amino alcohols. 5. The path of aminoacetone metabolism in Pseudomonas sp. N.C.I.B. 8858 was concluded to involve l-1-aminopropan-2-ol, the O-phosphate ester of this compound, propionaldehyde and propionate as obligatory intermediates. d-1-Aminopropan-2-ol was metabolized by the same route as the l-isomer, gratuitously inducing formation of the stereospecific l-1-aminopropan-2-ol dehydrogenase. 6. Extracts of the pseudomonad grown with ethanolamine as the nitrogen source were devoid of 1-aminopropan-2-ol dehydrogenase, the kinase and the phospho-lyase, but exhibited cobamide coenzyme-dependent deaminase activity. Mutants deficient in kinase or phospho-lyase (deaminating) grew well on ethanolamine as the nitrogen source. Ethanolamine deaminase was inactive with, but inhibited by, 1-aminopropan-2-ol.
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PMID:Microbial metabolism of amino alcohols. Aminoacetone metabolism via 1-aminopropan-2-ol in Pseudomonas sp. N.C.I.B. 8858. 436 43

1. A method is described for detecting and determining the products of metabolism of ADP added to plasma at initial concentrations of about 1mum-ADP. 2. ATP, ADP, AMP, adenosine, inosine and hypoxanthine were detected in human platelet-rich plasma after incubation with ADP and in the presence of either heparin or heparin-citrate. 3. The products of incubation of ADP with human platelet-poor plasma in the presence of heparin were the same as with platelet-rich plasma, except that, when the initial concentration of ADP was 1.5mum, little or no ATP was detected. 4. The ATP detected in platelet-rich plasma when 1.5mum-ADP was initially incubated was present in the platelets and not in the plasma. 5. The time for 50% decay of ADP in either platelet-rich or platelet-poor plasma in the presence of heparin was about 20min. when the initial concentration of ADP was 200mum, but was 6-9min. when the initial ADP concentration was 1.5-2.5mum. The corresponding values in the presence of heparin-citrate were about 45min. and about 9-12min. respectively. 6. Hypoxanthine accumulated to a greater extent in platelet-rich than in platelet-poor plasma after the addition of ADP. 7. After incubation for 15-20min. of either platelet-rich plasma or suspensions of washed platelets in saline with adenosine at an initial concentration of about 3-4mum, ATP, ADP and AMP were detected in the platelets. Similar incubations of washed platelets with inosine also showed the formation of these substances, but to a much less extent. 8. After the addition of adenosine to suspensions of washed platelets in saline, inosine and hypoxanthine were detected in the incubation mixture. After the addition of inosine, hypoxanthine was detected. 9. When ADP at an initial concentration of 1.5mum was added to platelet-rich plasma containing adenosine deaminase, no adenosine was detected in the incubation mixture. There was no difference in the rate of decay of ADP in the presence or absence of the deaminase, but ATP formation was decreased in its presence.
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PMID:Detection and determination of adenosine diphosphate and related substances in plasma. 594 46

The activities of adenylate kinase, AMP-deaminase and 5'-nucleotidase in various tissues of the rat were studied. The activity of the forward adenylate kinase reaction (ATP + AMP----2 ADP) against the back one (2 ADP----ATP + AMP) was predominant. The liver was shown to contain two, while the blood serum--three adenylate kinase isoenzymes. In the skeletal muscles, the catabolism of adenylic acid involving AMP-deaminase and 5'-nucleotidase predominantly occurred via deamination, in the liver--via dephosphorylation, while in the leucocytes, erythrocytes and blood serum the activity of these processes was essentially the same. In vitro, ATP enhanced the activity of AMP-deaminase in the liver, leucocytes and erythrocytes and decreased it in the blood serum. Under effects of ATP, the activity of 5'-nucleotidase in the leucocytes and blood serum was markedly elevated, that in the liver and erythrocytes was unaffected.
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PMID:[Role of adenylate kinase, AMP deaminase and 5'-nucleotidase in the metabolism of adenylic nucleotides]. 609 96

The substrate (AMP) and co-factor (ATP)-dependent kinetic parameters of AMP-deaminase have been studied in the contralateral and denervated gastrocnemius muscles of frog, Rana hexadactyla. An increasing in apparent affinity (Km) and maximal velocity (V) were found with denervated muscle enzyme as compared to the contralateral muscle enzyme. The activation energy (delta E) values were found to be decreased on denervation suggesting increased catalytic efficiency of denervated muscle enzyme.
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PMID:AMP-deaminase activity in denervation atrophy of the amphibian skeletal muscle. 616 65


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