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)

Construction of a malE-ampD gene fusion allowed purification of biologically active fusion protein by affinity chromatography. The cloned malE-ampD gene fusion complemented a chromosomal ampD mutation. Purified MalE-AmpD fusion protein was found to have murein amidase activity with a pronounced specificity for 1,6-anhydromuropeptides, the characteristic murein turnover products in Escherichia coli. Being a N-acetyl-anhydromuranmyl-L-alanine amidase AmpD is likely to be involved in recycling of the turnover products. It is suggested that the negative regulatory effect of AmpD is due to the hydrolysis of anhydro-muropeptides which may function as signals for beta-lactamase induction.
FEMS Microbiol Lett 1994 Sep 15
PMID:The negative regulator of beta-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase. 795 68

Endo beta-N-acetylglucosaminidase activities were determined based on conversion of oligosaccharides containing two N-acetylglucosamines to the oligosaccharides with a single N-acetylglucosamine at the reducing terminal and following their separation on a carbohydrate analyzer. The oligosaccharides eluted from the high performance anion exchange column in the order of fucosyl-N,N'-diacetylchitobiose, N,N'-diacetylchitobiose and N-acetylglucosamine containing reducing terminals. Using this assay, differences in cleavage specificity of the endo beta-N-acetylglucosaminidase F (Endo F) activity on various free oligosaccharides obtained from the standard glycoproteins was determined. The commercial Endo F-peptide N-glycosidase/glycanyl amidase (PNGase) mixture readily cleaved high mannose and complex oligosaccharides (neutral and sialyated) with common core alpha 1-6 linked fucose found in porcine thyroglobulin including the trimannosyl-chitobiose core structure. However, the same Endo F mixture did not cleave the non-fucosylated complex oligosaccharides found in human transferrin and also the common core structure. Glycopeptide counterparts with and without fucose were good substrates for the endoglycosidases. These results show that the specificity of these enzymes is such that they can recognize the conformational differences between free oligosaccharides and glycopeptides with and without the common core alpha 1-6 linked fucose. In contrast, highly purified Endo F cleaved only the high mannose type oligosaccharides and was unable to cleave ovalbumin hybrid type oligosaccharides.(ABSTRACT TRUNCATED AT 250 WORDS)
J Mol Recognit 1993 Sep
PMID:Endo beta-N-acetylglucosaminidase F cleavage specificity with peptide free oligosaccharides. 806 Jun 71

Arachidonoyl ethanolamide (anandamide) is a naturally occurring brain constituent that binds to a specific brain cannabinoid receptor (CBR1). An amidase activity (anandamide amidase) in membrane fractions of brain and in cultured neuroblastoma cells rapidly degrades anandamide to arachidonic acid (Deutsch, D. G., and Chin, S. (1993) Biochem. Pharmacol. 46, 791-796). In the current study, analogs of anandamide representing three classes of putative transition-state inhibitor (trifluoromethyl ketones, alpha-keto esters, and alpha-keto amides) were synthesized and tested as inhibitors of anandamide hydrolysis in vitro and as ligands for CBR1. The trifluoromethyl ketones and alpha-keto esters showed nearly 100% inhibition of anandamide hydrolysis in vitro at 7.5 microM inhibitor and 27.7 microM anandamide. Arachidonyl trifluoromethyl ketone was the only synthetic compound in the series of fatty acid derivatives able to displace [3H]CP-55940 binding to CBR1 with a Ki of 0.65 microM. It was also the most effective inhibitor in intact neuroblastoma cells, leading to a 12-fold increase of cellular anandamide levels at 12 microM. From the action of these inhibitors on this hydrolytic enzyme, it seems likely that anandamide is cleaved by a mechanism that involves an active-site serine hydroxyl group. These inhibitors may serve as useful tools to elucidate the role anandamide plays in vivo.
J Biol Chem 1994 Sep 16
PMID:Inhibitors of arachidonoyl ethanolamide hydrolysis. 808 91

Malignant pleural mesothelioma is a tumor very difficult to diagnose and with a very controversial therapy. We describe an illustrative case with development of pleural overflow and detection of high adenosine-deaminase levels. Surgical resection combined with radiotherapy and/or chemotherapy is the current therapeutics. We describe the state-of-the-art advances in the immunohistochemical diagnosis and therapeutics and we stress the need to conduct cooperative studies in order to achieve a better knowledge of the prognosis factors, an effective step-by-step approach and innovative therapy strategies.
An Med Interna 1993 Sep
PMID:[Malignant pleural mesothelioma. A diagnostic and therapeutic challenge]. 821 2

Amide-inducible expression of the aliphatic amidase system of Pseudomonas aeruginosa can be reconstituted in Escherichia coli with only the amidase structural gene amiE, the negative regulator amiC and the positive regulator amiR, a transcription antitermination factor. Complementation experiments in E. coli suggest that negative control of amidase expression by AmiC is mediated by a protein-protein interaction with AmiR. Purified AmiC binds acetamide with a KD of 3.7 microM in equilibrium dialysis studies, and therefore AmiC appears to be the sensory partner of the AmiC/AmiR pair of regulatory proteins, responding to the presence of amides. Sequence analysis techniques suggest that AmiC is a member of the structural family of periplasmic binding proteins, but has a distinct and novel cytoplasmic role.
EMBO J 1993 Sep
PMID:Antitermination of amidase expression in Pseudomonas aeruginosa is controlled by a novel cytoplasmic amide-binding protein. 825 87

A new method of assaying deaminase activity was established in which methylamine and/or dimethylamine formed from drugs containing N,N-dimethyl or N-methyl group were derivatized with phenylisothiocyanate to phenylthiourea derivatives. After purification with Sep-PAK C18 cartridge, the derivatives were separated by a reversed phase high-performance liquid chromatography monitored by ultraviolet absorption. The recoveries and determination limits of methylamine and dimethylamine were over 55% and about 0.4 nmol/ml of incubation mixture, respectively. The method was used to measure the deaminase activities of liver microsomes of rats, rabbits and guinea pigs for 11 drugs. Of the compounds tested, diphenhydramine and diltiazem are deaminated with microsomes from all the above animal species; rat and rabbit liver microsomes also well deaminated promethazine. Most other drugs such as chlorpromazine, promazine, imipramine, amitriptyline and tetracaine were found to be poor substrates. In general, dimethylamine but not methylamine was the predominant metabolite formed from drugs containing N,N-dimethylamino group. The results also suggested that the deamination of these compounds takes place mainly via a one step mechanism, thus implying that the sequential reaction consisting of N-demethylation and elimination of ammonia is of minor importance. The relation between in vitro deaminase activity and the extent of the in vivo deamination for drugs is discussed.
Biol Pharm Bull 1993 Sep
PMID:Metabolic formation of dimethylamine and methylamine from basic drugs containing N-methyl group: a newly established chromatographic assay and its application to the determination of deaminase activity. 826 49

Enzymatic activities have been identified which catalyze both the hydrolysis and synthesis of arachidonylethanolamide (anandamide). Anandamide was taken up by neuroblastoma and glioma cells in culture, but it did not accumulate since it was rapidly degraded by an amidase activity that resided mainly in the membrane fractions. This amidase activity was expressed in brain and the majority of cells and tissues tested. Phenylmethylsulfonyl fluoride (PMSF) was found to be a potent inhibitor of this amidase. A catalytic activity for the biosynthesis of anandamide from ethanolamine and arachidonic acid was readily apparent in incubations of rat brain homogenates. The stability of anandamide in serum and its rapid breakdown in cells and tissues are consistent with the observation that it is active when administered systemically, and its duration of action will be regulated by its rate of degradation in cells.
Biochem Pharmacol 1993 Sep 01
PMID:Enzymatic synthesis and degradation of anandamide, a cannabinoid receptor agonist. 837 32

The purified autolytic endo-beta-N-acetylglucosaminidase of Bacillus subtilis AC327 was cleaved with cyanogen bromide, and the N-terminal amino acid sequence of one of the peptide fragments was determined. Then, a DNA fragment containing a part of the glucosaminidase gene was cloned into Escherichia coli JM109 using synthetic oligonucleotides as probes whose sequences had been deduced from the N-terminal amino acid sequence. Zymographic analysis showed that the resultant glucosaminidase-deficient strain lacked a 35-kDa lytic band in addition to a 90-kDa lytic one corresponding to the glucosaminidase. A double mutant strain deficient in the major two autolysins (amidase and glucosaminidase) exhibited greatly impaired motility on a swarm plate whereas the single mutant strains were motile.
FEMS Microbiol Lett 1993 Sep 01
PMID:Bacillus subtilis mutant deficient in the major autolytic amidase and glucosaminidase is impaired in motility. 840 54

The asparagine-linked oligosaccharides from an adult female mouse submandibular gland mucin were released by treatment with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F or endo-beta-N-acetylglucosaminidase H. Endo-beta-N-acetylglucosaminidase H appeared to be more effective at releasing the asparagine-linked oligosaccharides from this mucin than was peptide-N4-(N-acetyl-beta-glucosaminyl)-asparagine amidase F. After quantitative reductive labelling with the fluorophore, 8-aminonaphthalene-1,3,6-sulphonic acid, the oligosaccharides were separated by polyacrylamide gel electrophoresis and isolated. The individual oligosaccharides were sequenced by a battery of recombinant exoglycosidases. Approximately 50% of the oligosaccharides were of the high-mannose type. The five-mannose member of this family was the most prevalent. The second group of oligosaccharides were of the non-bisected hybrid type. No complex asparagine-linked oligosaccharides were detected. The hybrids exhibited both biantennary and triantennary branching patterns. The triantennary hybrid was the most common hybrid at > 30% of all oligosaccharides. With approximately 98% of the hybrid oligosaccharides sialylated and all lacking a bisecting N-acetylglucosamine, these oligosaccharides as a group have been only rarely observed in other glycoproteins. The fully sialylated triantennary hybrid may be unique.
Glycobiology 1995 Sep
PMID:Characterization of asparagine-linked oligosaccharides on a mouse submandibular mucin. 856 46

A 3.2-kbp PstI fragment of DNA encoding formamidase from the methylotrophic bacterium Methylophilus methylotrophus which had previously been cloned (pNW3) [Wyborn, N.R., Scherr, D.J. & Jones, C.W. (1994) Microbiology 140, 191-195], was subcloned as a 2.3 kbp HindIII fragment (pNW323). Nucleotide sequencing showed that the subclone contained two genes which encoded formamidase (fmdA) and a possible regulatory protein (fmdB). Predicted molecular masses for FmdA and FmdB were 44438 Da (compared with approximately 44500 Da by electrospray mass spectrometry and 51000 Da by SDS/PAGE of the purified enzyme) and 12306 Da, respectively. The derived amino acid sequence of formamidase was supported by N-terminal amino acid sequencing of the enzyme and of proteolytic fragments prepared from it using V8 endoproteinase and was 57% similar to that of the acetamidase from Mycobacterium smegmatis. The structural similarities between these two enzymes, and their existence as a separate class of bacterial amidase, were confirmed by immunological investigations.
Eur J Biochem 1996 Sep 01
PMID:Molecular characterisation of formamidase from Methylophilus methylotrophus. 884 93


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