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)

A Rhodococcus erythropolis strain was isolated from soil on the basis of its ability to use acetaminophen as the sole source of both carbon and energy for growth. When grown in a complex medium containing an anilide inducer compound, the bacterium exhibited aryl acylamidase (EC 3.5.1.13) activity. This activity was not subject to carbon or nitrogen repression by the growth medium constituents as the enzyme was present throughout the exponential growth phase. The anilide was converted to the corresponding aniline, which was not further degraded. The enzyme was partially purified by a variety of methods including a batch ion exchange procedure, column ion exchange chromatography and hydrophobic interaction chromatography. The enzyme had a maximum activity at around pH 8.0 and had a Km for acetaminophen of 0.11 mM. Electrochemical assays of aryl acylamidase activity are described. The enzyme is suitable for use as a reagent in the clinical diagnostic measurement of acetaminophen.
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PMID:Aryl acylamidase from Rhodococcus erythropolis NCIB 12273. 136 73

Retinal synthesis of melatonin, a potent modulator of rhythmic retinal processes, is elevated at night as a result of regulation by a circadian clock. Despite high nocturnal synthetic capacity, both melatonin content and release are low in the retina of the frog Xenopus laevis. We report here that cultured eyecups from Xenopus have the capacity for rapid metabolic breakdown of melatonin. Pharmacological analysis indicates that the initial step in this degradation pathway is deacetylation of melatonin by the enzyme aryl acylamidase (aryl-acylamide amidohydrolase, EC 3.5.1.13). This produces 5-methoxytryptamine, which is then deaminated by monoamine oxidase [amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4], producing 5-methoxyindoleacetic acid and 5-methoxytryptophol. Inhibition of aryl acylamidase with eserine dramatically increases the release of endogenous melatonin by eyecups cultured at night, indicating that this pathway is the normal fate of retinal melatonin. Metabolism within the eye suggests a local neuromodulatory role for retinal melatonin, in contrast to the hormonal role of pineal melatonin.
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PMID:Retinal melatonin is metabolized within the eye of xenopus laevis. 249 61

Human cerebrospinal fluid contained both acetylcholinesterase (EC 3.1.1.7) and butyrylcholinesterase (EC 3.1.1.8) and they were estimated in the presence of selective inhibitors. Butyrylcholinesterase of human cerebrospinal fluid was similar to human serum butyrylcholinesterase in its electrophoretic mobility, glycoprotein nature and tyramine activation of the aryl acylamidase (EC 3.5.1.13) activity exhibited by butyrylcholinesterase. Moreover antibody raised against human serum purified butyrylcholinesterase could completely immunoprecipitate butyrylcholinesterase from human cerebrospinal fluid without affecting acetylcholinesterase. It is suggested that a useful method for the precise determination of acetylcholinesterase in human cerebrospinal fluid would be removal of butyrylcholinesterase by immunoprecipitation using antibody raised against human serum butyrylcholinesterase.
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PMID:Human cerebrospinal fluid acetylcholinesterase and butyrylcholinesterase. Evidence for identity between the serum and cerebrospinal fluid butyrylcholinesterase. 279 3

The specific activities of two forms of aryl acylamidase (AAA) were examined in 7 regions of the developing rat brain, plus the remainder of the brain and the whole brain. AAA-1 activity peaked at 15 days old in all brain regions studied except the whole brain where it peaked at 22 days of age. AAA-2 activity peaked between 15 and 29 days old in most brain regions studied except corpus striatum and hippocampus where the AAA-2 activity peaked before 15 days old. In all areas and at all time periods, with the exception of CS after 15 days of age, AAA-2 activity was much higher than that of AAA-1. The developmental pattern of AAA-1 is generally the same in the different brain regions while that of AAA-2 shows more regional specificity. These results indicate that neither AAA-1 nor AAA-2 may be associated with amine N-acetyltransferase in the brain which has an entirely different developmental pattern.
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PMID:Multiple forms of aryl acylamidase in regional tissues of developing rat brain. 345 84

Erythrocyte acetylcholinesterase (EC 3.1.1.7) and plasma pseudocholinesterase (EC 3.1.1.8) were determined from the day of admission up to 10 days in patients who have consumed organophosphate or carbamate poisons. In a number of patients, plasma pseudocholinesterase was completely inhibited on the day of admission but increased with the passage of days. Erythrocyte acetylcholinesterase was not completely inhibited and it also tended to increase with time in most cases. Patients in whom the erythrocyte acetylcholinesterase was very low and did not show an increase within the first few days expired indicating the prognostic importance of erythrocyte acetylcholinesterase. The profile of aryl acylamidase (EC 3.5.1.13) activity in plasma or erythrocytes showed a pattern similar to the respective cholinesterases. Moreover, whole blood aryl acylamidase activity was found to be a good index of erythrocyte acetylcholinesterase suggesting the prognostic usefulness of blood aryl acylamidase in the poisoned patients.
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PMID:Aryl acylamidase activity in human erythrocyte, plasma and blood in pesticide (organophosphates and carbamates) poisoning. 397 15

From Bacillus sphaericus ATCC 12123 an aryl acylamidase (EC 3.5.1.13) was purified to homogeneity by ion exchange chromatography, gel filtration, and polyacrylamide gel electrophoresis. The enzyme is inducible by various phenylamides of the acylanilide, phenylcarbamate, and methoxysubstituted phenylurea type. It has a molecular weight of 75,000. Enzyme activity was inhibited by sulfhydryl reagents, several metal ions, and 3,4-dichloroaniline (a product of linuron degradation). A requirement for divalent metal ions in enzyme activity could not be demonstrated. In the presence of 6 M urea an irreversible inactivation of the enzyme occurred. The hydrolysis of L-alanine-4-nitroanilide was competitively inhibited by puromycin.
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PMID:Purification and properties of an aryl acylamidase of Bacillus sphaericus, catalyzing the hydrolysis of various phenylamide herbicides and fungicides. 476 92

The intracellular localization of aryl acylamidase (aryl-acylamide amidohydrolase, EC 3.5.1.13) in chicken kidney was investigated. By separation on density gradients of the silica sol Ludox AM, the enzyme was localized in the mitochondrial fraction. This mitochondrial fraction was shown to be substantially free of lysosomal contamination. Subfractionation of the purified mitochondria indicates that the enzyme is located on the outer membrane, can be solubilized, and may be a suitable marker enzyme for kidney mitochondria.
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PMID:Subcellular localization of chicken kidney aryl acylamidase activity. 624 88

1. The serotonin (5-HT) sensitive brain aryl acylamidase (AAA) has received considerable attention due to its potential involvement in 5-HT action mechanism in CNS. 2. Multiple forms, AAA-1 and 2, have been separated by ammonium sulfate precipitation of brain extract and subsequent gel filtration. 3. Their chemical properties have been characterized and differentiated by effects of several classes of drugs including d-LSD, 5-HT, 5-HT related compounds and tetrahydro-beta-carbolines on their enzyme activities. 4. In the rat brain, AAA-1 shows highest specific activity in corpus striatum and lowest activity in cerebellum whereas AAA-2 shows highest specific activity in cerebellum and lowest activity in corpus striatum. 5. Subcellularly, AAA-1 exhibits highest specific activity in synaptosomal fraction of rat corpus striatum, lowest activity in mitochondrial fraction and no activity in nuclear fraction while AAA-2 exhibits highest specific activity in microsomal fraction and lowest activity in nuclear fraction. 6. Triton X-100 treatment altered the subcellular distribution pattern of both AAA-1 and AAA-2. 7. AAA-2 is possibly associated with true acetylcholinesterase (AChE) in brain based on its inhibition by neostigmine but its identity with AChE needs further elucidation. 8. To determine the physiological role(s) for brain AAA, naturally occurring aromatic alkylamines other than melatonin need to be tested as possible substrate(s) for the enzyme activity.
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PMID:Brain aryl acylamidase. 675 8

1. Two fractions of aryl acylamidase (EC 3.5.1.13) were further separated from rat brain extracts at pH 7.5 by ammonium sulfate precipitation and Bio-Gel chromatography. 2. 1,2,3,4-Tetrahydro-beta-carboline competitively inhibited (67%) fraction-1 but slightly inhibited (13%) fraction-2. Tetrahydroharman, 6-hydroxy-tetrahydroharman and harminic acid slightly inhibited both fractions. Harmalol inhibited fraction-1 but enhanced fraction-2. 6-Methoxy-harman, 6-methoxy-harmalan and harmaline enhanced both fractions. 3. Pargyline did not affect either fraction. Methiothepin, cyproheptadine and chlorimipramine inhibited fraction-1 but stimulated fraction-2. 4. Neostigmine moderately (30%) inhibited AAA-2 but did not have any significant effect on AAA-1. 5. These results indicate that the beta-carboline compounds might play a role in regulating activity of AAA-1 and 2 in brain. 6. Both fractions might be related to serotonergic neurons but only AAA-2 might be associated with acetylcholinesterase.
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PMID:Rat brain aryl acylamidase: further characterization of multiple forms. 710 57

Serotonin-sensitive aryl acylamidase (AAA, EC 3.5.1.13) was purified to apparent homogeneity from sheep platelets by affinity chromatography and it was shown to be associated with the platelet acetylcholinesterase (AChE, EC 3.1.1.7). The basis for the association of the two enzymes was the following. Both enzyme activities co-eluted from the affinity columns with constant ratios of specific activities and percentage recoveries. Both enzymes co-migrated on gel electrophoresis. Both enzymes co-eluted during sepharose 6B gel filtration. Potent inhibitors of AChE such as bis(4-allyldimethyl ammoniumphenyl) pentan-3-one dibromide (BW 284C51), neostigmine and eserine also inhibited AAA potently. Both enzymes lost significant activity on treatment with deoxycholate or taurodeoxycholate and the loss could be partly restored by a mixture of phospholipids. The platelet AAA was specifically inhibited by serotonin and to a lesser extent by tryptamine but not by several other amines. It was also inhibited by acetylcholine and several of its analogues and homologues. It is suggested that in the platelets the two enzymes (AAA and AChE) are probably identical.
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PMID:Serotonin-sensitive aryl acylamidase activity of platelet acetylcholinesterase. 712 46


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