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 metabolism of fungicide benzoic acid, 1,3-dithiolan-2-ylidenehydrazied (Yekuling) was studied quantitatively in rat liver microsomes and liver soluble fractions pretreated with phenobarbital (PB) and 3-methylcholanthrene (3-MC) by high pressure liquid chromatography. The experimental results indicated that the major metabolic pathway of Yekuling in vitro was hydrolysis. PB can enhance amidase activity to increase formation of benzoic acid and 1,3-dithiolan-2-ylidenehydrazine. 3-MC treatment elevated rat liver microsomal cytochrome P-448, enhancing S-oxidation of Yekuling. On the other hand, S-oxidation of Yekuling by rat liver microsomal MFO was NADPH-dependent.
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PMID:[Studies on metabolism of fungicide benzoic acid, 1,3-dithiolan-2-ylidenehydrazide in vitro]. 130 96

The effects of various commercial and model surfactants of different structure and hydrophilicity were studied on water-in-oil (w/o) emulsion stability, potassium cation leakage and permeation of 6-nitro-3-phenylacetamide benzoic acid in a model system using Penicillin acylase (EC 3.5.1.11) immobilized in a liquid membrane. Both emulsion stability, potassium leakage and permeation of organic substances depend upon hydrophilicity of surfactants. Hydrophilic surfactants may be used to stabilize emulsions only in mixtures with hydrophobic emulsifiers. Additions of small quantities of hydrophilic surfactants to the system in which permeation occurs together within an enzymatic process may be advantageous. Both the rate of permeation and potassium transfer significantly increase when hydrophilic surfactants are present. There was no relationship observed between potassium cation transfer from the internal phase and emulsion stability in the storage test.
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PMID:Permeation of 6-nitro-3-phenylacetamide benzoic acid (NIPAB) and hydrolysis by penicillin acylase immobilized in emulsion liquid membranes. 136 99

The metabolism of a fungicide Yekuling was studied in rat after oral administration. Four metabolites were isolated and purified by means of reverse-phase HPLC and TLC. They were identified to be acetic acid, 1,3-dithiolan-2-ylidenehydrazide; pyruvic acid, 1,3-dithiolan-2-ylidenehydrazide; benzoic acid and hippuric acid with UV and MS. The latter was further confirmed by chemical synthesis. The experimental results showed that Yekuling was metabolized extensively in rat. Yekuling was hydrolyzed by amidase to produce benzoic acid and 1,3-dithiolan-2-ylidenehydrazide. The latter was further acetylated by N-acetyltransferase to form acetic acid, 1,3-dithiolan-2-ylidenehydrazide, or condensed spontaneously to form pyruvic acid, 1,3-dithiolan-2-ylidenehydrazide. Benzoic acid was further conjugated with glycine to produce hippuric acid.
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PMID:[Studies on metabolism of a fungicide yekuling in rat]. 145 79

A strain of Klebsiella pneumoniae that used aliphatic nitriles as the sole source of nitrogen was adapted to benzonitrile as the sole source of carbon and nitrogen. Gas chromatographic and mass spectral analyses of culture filtrates indicated that K. pneumoniae metabolized 8.4 mM benzonitrile to 4.0 mM benzoic acid and 2.7 mM ammonia. In addition, butyronitrile was metabolized to butyramide and ammonia. The isolate also degraded mixtures of benzonitrile and aliphatic nitriles. Cell extracts contained nitrile hydratase and amidase activities. The enzyme activities were higher with butyronitrile and butyramide than with benzonitrile and benzamide, and amidase activities were twofold higher than nitrile hydratase activities. K. pneumoniae appears promising for the bioremediation of sites contaminated with aliphatic and aromatic nitriles.
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PMID:Metabolism of benzonitrile and butyronitrile by Klebsiella pneumoniae. 153 79

A novel method for detecting microorganisms capable of producing cephalosporin C (CPC) acylase and/or 7-(4-carboxybutanamido)cephalosporanic acid (GL-7-ACA) acylase has been developed. The method is based on the degradation of 2-nitro-5-(6-bromohexanoylamino)benzoic acid (NBHAB), a chromogenic substrate, into yellow 2-nitro-5-aminobenzoic acid by the action of the CPC acylase or the GL-7-ACA acylase. This method is very sensitive and quite specific, and has been successfully applied to screen the acylases from a variety of bacteria. A large number of colonies isolated on a plate surface from more than 67 samples and several known bacteria were tested by the NBHAB paper. Five NBHAB-positive strains and isolates were obtained. They were further examined by the reaction of their bacterial cells upon CPC and GL-7-ACA, respectively, and by thin-layer chromatography in order to distinguish the CPC acylase from the GL-7-ACA acylase.
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PMID:2-Nitro-5-(6-bromohexanoylamino)benzoic acid test paper method for detecting microorganisms capable of producing cephalosporin acylases. 177 68

A bacterium capable of utilizing either acetonitrile as the sole source of carbon and nitrogen or biphenyl as the sole source of carbon was isolated from soil and identified as Pseudomonas aeruginosa. The bacterium also utilized other nitriles, amides, and polychlorinated biphenyls (PCBs) as growth substrates. Acetonitrile- or biphenyl-grown cells oxidized these substrates without a lag. In studies with [14C]acetonitrile, nearly 74% of the carbon was recovered as 14CO2 and 8% was associated with the biomass. In studies with [14C]biphenyl, nearly 68% of the carbon was recovered as 14CO2 and nearly 6% was associated with the biomass. Although higher concentrations of acetonitrile as the sole sources of nitrogen inhibited the rates of [14C]biphenyl mineralization, lower concentrations (0.05%, w/v) gave a 77% stimulation in 14CO2 recovery. Pseudomonas aeruginosa metabolized acetonitrile to ammonia and acetic acid and biphenyl to benzoic acid. The bacterium also simultaneously utilized biphenyl as the sole carbon source and acetonitrile as the sole nitrogen source. However, biphenyl utilization increased only after the depletion of acetonitrile. Metabolites of the mixed substrate were ammonia and benzoic acid, which completely disappeared in the later stages of incubation. Nitrile hydratase and amidase were responsible for the transformation of acetonitrile to acetic acid and ammonia.
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PMID:Simultaneous degradation of acetonitrile and biphenyl by Pseudomonas aeruginosa. 191 44

The basis for the difference between Campylobacter jejuni and Campylobacter coli is the presence and expression of the N-benzoylglycine amidohydrolase (hippuricase) gene only in C. jejuni. A pBR322 recombinant clone (pHIP-O) of C. jejuni TGH9011 capable of converting hippuric acid into benzoic acid and glycine, the hallmark of hippuricase activity, was characterized and sequenced. The hippuricase gene (hipO) was identified by use of deletion subclones and insertional inactivation. The transcription start point of the hippuricase gene was determined by primer extension analysis. A hippuricase-specific gene fragment was used to determine the presence of the gene in Campylobacter species. Maxicell analysis of recombinant plasmid pHIP-O by sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated the production of a 42-kDa protein corresponding to the HipO gene product, in excellent agreement with the predicted molecular mass of the protein.
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PMID:Expression and characterization of Campylobacter jejuni benzoylglycine amidohydrolase (Hippuricase) gene in Escherichia coli. 773 Feb 70

The hydrolysis of penicillin-V to phenoxyacetic acid and 6-aminopenicillanic acid by the fungal enzyme penicillin-V amidase is of industrial importance since the 6-aminopenicillanic acid produced is an intermediate for semisynthetic penicillins. A rapid colorimetric assay of penicillin-V amidase was developed which uses 2-nitro-5-(phenoxyacetamido)-benzoic acid as a substrate. The released chromophore, 2-amino-5-nitrobenzoic acid, was detected at 405 nm. Using penicillin-V amidase from the fungus Fusarium oxysporum, the KM and Vmax for this substrate were 0.89 mM and 2.6 mumol/min/mg enzyme, respectively. Hydrolysis could be competitively inhibited by penicillin-V with a Ki of 4 mM. The change in the initial velocity of hydrolysis of 2-nitro-5-(phenoxyacetamido)-benzoic acid at 500 microM was linear over the range of 0.5 to 10 micrograms/ml enzyme. These results show that this new compound is useful in determining the presence and levels of penicillin-V amidase.
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PMID:A colorimetric assay for penicillin-V amidase. 847 Aug 5

The amidase from Rhodococcus rhodochrous J1, which hydrolyses amide to acid and ammonia, was found to catalyze the synthesis of hydrazide using hydrazine as a substrate. This is the first report on the hydrazide synthesis through enzymatic reactions. The enzyme also acted on benzoic acid in the presence of hydrazine, yielding benzoic hydrazide. Together with the finding that benzoic hydrazide was converted into benzoic acid (when it was used as a substrate in the absence of hydrazine), these unique characteristics suggest that the reaction route for the formation of the acid from the hydrazide and that of the hydrazide from the acid are reversible to each other via the acyl-enzyme. Not only aromatic hydrazides but also aliphatic hydrazides were synthesized from the corresponding amides and hydrazine.
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PMID:Hydrazide synthesis: novel substrate specificity of amidase. 1007 99

In this study mid-infrared spectroscopy was used to follow the enzyme kinetics involved in nitrile biocatalysis using whole cell suspensions of the bacterium Rhodococcus rhodochrous LL100-21. The bacteria were grown on acetonitrile to induce a two-step enzymatic pathway. Acetonitrile was biotransformed to acetamide by a nitrile hydratase enzyme and subsequently to acetic acid (carboxylate ion) by an amidase enzyme. The bacteria were also grown on benzonitrile to induce a one-step enzymatic pathway. Benzonitrile was biotransformed directly to benzoic acid (carboxylate ion) by a nitrilase enzyme. These reactions were followed by React IR using a silicon probe and gave excellent quantitative and qualitative real-time data of both nitrile biocatalytic reactions. This study has shown that this novel technique has potentially useful applications in biocatalysis.
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PMID:Real-time monitoring of nitrile biotransformations by mid-infrared spectroscopy. 1085 79


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