Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.4.1 (phosphodiesterase)
 18,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Methionyl adenylate (Met-AMP) inhibits protein synthesis by interacting with methionyl-tRNA synthetase. Addition of 1--3 mM inhibitor to chick embryo fibroblasts rapidly stops protein synthesis and DNA synthesis but not RNA synthesis. These effects can be reversed by renewal of the medium. The extent and reversibility of protein and DNA syntheses depend on the concentration of MetAMP in the cultures, the length of exposure and the cellular density. MetAMP is recognised by several enzymes as substrate and/or as inhibitor. MetAmp is degraded to methionol plus 5'-adenylic acid by 5'-phosphodiesterase. Adenosine deaminase, adenylic acid deaminase and 3':5'-phosphodiesterase cannot use MetAMP as substrate but the last enzyme is inhibited. The presence of MetAMP in cultures provokes a small but reproducible increase in the level of methionyl-tRNA synthetase and 5'-phosphodiesterase.
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PMID:Further studies of the action of methionyl adenylate on chick embryo fibroblasts. 19 96

Decrease in monoamine oxidase and increase in diamine oxidase and adenylate deaminating activities were found in rat liver mitochondrial fractions after repeated injections of ethanol. A monoamine oxidase inhibitor pargyline and an inhibitor of phosphodiesterase theophylline prevented the increase in adenylate deaminating activity in a subfraction of mitochondrial membranes in the ethanol intoxicated rats. In a subfraction of soluble mitochondrial proteins pargyline did not affect but theophylline prevented completely the increase in adenylate deaminating activity. The stimulation of adenylate deaminating activity in mitochondrial fractions of rat liver in ethanol intoxication might be caused by: 1) transformation of mitochondrial monoamine oxidases (in the subfraction of mitochondrial membranes) and 2) activation (or increased biosynthesis) of the adenylate deaminase in the subfraction of soluble mitochondrial proteins. The adenylate cyclase system is probably involved in the latter process.
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PMID:[Monoamine oxidase and adenylate deaminase activity of mitochondrial fractions of the rat liver in alcoholic intoxication]. 82 6

Chemical phosphorylation with sodium trimetaphosphate (STMP) as a modifying agent was used to prepare functional protein isolate and dissociated nucleic acid (mostly RNA) from baker's yeast. The majority of protein-RNA complex in the disintegrated yeast cells was first extracted with an aqueous alkaline solution (pH 12, 40 degrees C) followed by phosphorylation with STMP under the same condition for 6 hrs. An apparent dissociation of protein-RNA complex occurred due to the covalent attachment of anionic phosphate groups onto yeast protein molecules. The nucleic acid residued in the supernatant after removal of modified protein isolate by isoelectric precipitation was recovered by reprecipitating at pH 2 followed by converting it to 5'-nucleotides with malt rootlets 5'-phosphodiesterase as well as red marine algal adenylate deaminase. This coherent process provided a preparation of food-usable functional protein isolate and 5'-nucleotides from baker's yeast.
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PMID:Enzymatic preparation of seasoning 5'-nucleotides from baker's yeast. 610 Sep 35

The effects of S-adenosylhomocysteine and S-adenosylmethionine on some purine- and pyrimidine-metabolizing systems have been examined. Both compounds were capable of acting as relatively good inhibitors of adenosine deaminase, nucleoside phosphorylase, and adenylate deaminase activities but as relatively poor inhibitors of myokinase and nucleoside monophosphate kinase. The inhibitory effects were freely reversible. 5'-Nucleotidase, orotidine 5'- phosphate, and phosphodiesterase were unaffected. Nucleoside phosphorylase was competitively inhibited by both compounds, whereas mixed inhibitory effects occurred with adenosine deaminase.
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PMID:The effects of S-adenosylhomocysteine and S-adenosylmethionine on some purine- and pyrimidine-metabolizing systems. 629 1

The effect of intramuscularly administered immunomodulator, adenylate deaminase (E.C. 3.5.4.6), from Penicillium lanoso-viride on the clinical score of acute experimental autoimmune encephalomyelitis (EAE), a T cell-mediated autoimmune disease, was examined by inoculation of guinea pigs with rabbit brain and spinal cord homogenate (encephalitogen) and complete Freund's adjuvant. Adenylate deaminase (ADA) was effective in delaying the onset of clinical disease. ADA inhibited the severity of EAE. There was a significant decrease in clinical signs. A decrease in the number of morbid and dead animals was observed. Of ADA treated animals, 50-80% developed no clinical manifestations of EAE. The optimal version of treatment was a single preventive injection of ADA 1 day before the sensitization and then every second day after immunization for 20 days. ADA treatment of immunized animals diminished the activity of 2', 3'-cyclic nucleotide 3'-phosphodiesterase in the cerebrospinal fluid, as well the amount of complement fixing antiencephalitogenic antibodies in the blood serum. The mechanism of ADA cerebroprotective action is discussed. Significant skin-allergic cross-reaction of delayed-type hypersensitivity between ADA and encephalitogen was observed.
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PMID:Treatment of experimental autoimmune encephalomyelitis with adenylate deaminase from Penicillium lanoso-viride. 1067 41

Improved yields of 5'-nucleotides from yeast extract for food flavouring purposes is possible through use of microbial nucleotidases, which will be available to food processors as the flavour enhancer Aromild. The safety of these enzymes, 5'-phosphodiesterase (RP-1) and the 5'-adenylic deaminase (DN-50000) was investigated in male and female rats. Feeding rats a diet admixed with 500, 2000 and 8000 mg/kg body weight of DN-50000 for 35 days resulted in no significant dose-related changes in body weight, water consumption, urinalysis, haematological profiles, blood chemistry or histopathological profiles of either male or female rats from consumption of the enzyme preparation. There was an increase in the absolute and/or relative organ weights of the submaxillary (salivary) glands in both sexes at 8000 mg/kg. The no-observed-effect level (NOEL) for DN-50000 was clearly evident at 2000 mg/kg. Consumption of RP-1 enzyme for 35 days at dietary levels of 500, 2000 and 8000 mg/kg body weight resulted in no significant changes in the above mentioned parameters, which could be directly attributed to a dose-related effect, with the exception of an increase in the absolute and relative weights of submaxillary glands of both male and female rats in the 2000 and 8000 mg/kg groups. The increase in weight of the submaxillary glands was associated with histological evidence of acinar cell hypertrophy. The NOEL for dietary consumption of RP-1 was clearly evident at 500 mg/kg. In a follow-up study in which rats were gavaged with 2000 mg/kg RP-1, submaxillary gland hypertrophy did not occur. These studies suggest that DN-50000 and RP-1 exert an action on submaxillary glands similar to that which has been previously reported for the enzyme pancreatin. Neither DN-50000 nor RP-1 were mutagenic in the Ames assay using Salmonella typhimurium strains TA100, TA1535, TA98, TA1537 or Escherichia coli strain WP2uvrA, in the presence or absence of S9 mix.
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PMID:Toxicity and mutagenicity studies of DN-50000((R)) and RP-1((R)) enzymes. 1076 29