Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have identified a carboxylesterase in A. suum that appears to be the homolog of the gut-specific C. elegans ges-1 enzyme. The A. suum esterase was purified and its N-terminal sequence found to be 50% identical to the C. elegans ges-1 protein. We have used isoelectric focusing analysis to demonstrate that, unlike the C. elegans ges-1 esterase, the A. suum enzyme is not restricted to the gut but is expressed in a wide range of tissues.
Comp Biochem Physiol B Biochem Mol Biol
PMID:A carboxylesterase from the parasitic nematode Ascaris suum homologous to the intestinal-specific ges-1 esterase of Caenorhabditis elegans. 755 43

Flestolol, N(1,1-dimethyl-2-ureidocthyl)-2-hydroxy-3-(o-fluorobenzoyloxy++ +) propylamine, (F), is an ester containing an ultra short-acting beta blocker intended for the treatment of myocardial dysfunctions. In vitro incubation of F, procaine, chloroprocaine, and atropine with blood from different New Zealand White (NZW) rabbits resulted in a bimodal distribution (70% fast, 30% slow) of ester hydrolysis rates. Using F as a model substrate, bimodal hydrolysis rates were also observed in NZW rabbit cornea but not aqueous humor, iris-ciliary body complex and ocular tissues of pigmented rabbits. In addition, the bimodal distribution of esterase activity was not observed in blood from rats, dogs, and humans. Incubation of esters at various positions of the phenoxypropanolamine nucleus of beta blockers with NZW rabbit blood indicated structural specificity of the carboxylesterase in terms of unimodal or biomodal distribution of activity. These results strongly suggest that the carboxylesterase in NZW rabbit blood that hydrolyzes F and similar compounds is atropine esterase as described in the literature.
Res Commun Mol Pathol Pharmacol 1995 Apr
PMID:Polymorphic metabolism of flestolol and other ester containing compounds by a carboxylesterase in New Zealand white rabbit blood and cornea. 762 Aug 41

No significant differences were found between C57BL/6 and BALB/c mice in the levels of Thy 1.2 antigen (a T-cell marker) or the activities of the T-cell maturation-related enzymes adenosine deaminase (ADA, EC 3.5.4.4), serine-esterase (SE, EC 3.4.21), N-acetyl-beta-D-glucosaminidase (NABG, EC 3.2.1.30) and beta-glucuronidase (BG, EC 3.1.1.1), in either unfractionated lymphoid cells or T-lymphocyte-enriched fractions. ADA, SE, NABG and BG activities were much higher (P < 0.01) in the calf than in the corresponding populations in mice. However, the distributions of these activities among thymocyte subpopulations were very similar in mice and the calf. These results provide indirect evidence to suggest that the course of T-cell maturation is similar in mice and the calf.
Comp Biochem Physiol B Biochem Mol Biol 1995 Feb
PMID:Markers of T-cell differentiation and maturation in C57BL/6 and BALB/c mice and in the calf: a comparative study. 771 43

Malathion resistance in a strain of Culex tarsalis mosquitoes is due primarily to the activity of a malathion carboxylesterase (MCE). The resistant strain was 150 times more resistant to malathion than the susceptible strain and was weakly resistant to malaoxon and carbaryl, but not to any other insecticide tested. The phenotype could be reversed with the carboxylesterase inhibitor triphenylphosphate, but no synergism was observed with either the phosphatase or polysubstrate monooxygenase inhibitors, NaF and piperonyl butoxide. MCE is expressed throughout development and is most concentrated in the gut tissues of the larvae. Subcellular fractionation indicated that MCE was localized primarily in the mitochondria of resistant insects and the cytoplasm of susceptible insects. The enzyme was purified to homogeneity from both strains, and has a molecular weight of 59,000. However, chromatofocusing indicated that resistant insects have two MCEs with pIs of 6.8 and 6.2, while susceptible insects possessed only one MCE with a pI of 6.8. The MCE unique to the resistant strain hydrolysed malathion 18 times faster than the MCE common to both strains, suggesting that malathion resistance in C. tarsalis is due to the presence of a qualitatively different esterase in the resistant strain.
Insect Biochem Mol Biol 1994 Sep
PMID:Isolation of an esterase conferring insecticide resistance in the mosquito Culex tarsalis. 798 29

Antibodies recognizing horse radish peroxidase (HRP) stain neurons in Drosophila and other insects. We have used Western blots to analyze and characterize some of the anti-HRP reactive components from Drosophila melanogaster. Anti-HRP reactive components can be reproducibly detected during all developmental stages, although the pattern changes at different developmental times. In adults, there are at least 10 reproducibly stained components. Two of the bands, with molecular sizes of 42 and 80 kDa are likely to be the major contributors to neuronal anti-HRP staining in Drosophila. These components are enriched in adult fly heads. In contrast, many of the other anti-HRP reactive components in adults are enriched in abdomen and are present exclusively or at much higher levels in male flies. We have purified and characterized two of the male specific components with molecular sizes of 62 and 48 kDa. Partial N-terminal amino acid sequencing revealed that the 62 kDa protein is identical to a part of D. melanogaster carboxylesterase to EC 3.1.1.1) while he 48 kDa protein does not match any known sequences. Esterase-6 has previously been shown to be enriched in male accessory gland and consistent with this we show staining of this structure with anti-HRP antibodies.
Insect Biochem Mol Biol 1994 Mar
PMID:Biochemical analysis of proteins recognized by anti-HRP antibodies in Drosophila melanogaster: identification and characterization of neuron specific and male specific glycoproteins. 801 74

Exposure of rabbit pulmonary arterial smooth muscle cells to 10 microM of the calcium ionophore A23187 dramatically stimulates cell membrane-associated phospholipase A2 activity and arachidonic acid release. In addition, A23187 also enhances cell membrane-associated serine esterase activity. Serine esterase inhibitors phenylmethylsulfonylfluoride and diisopropyl fluorophosphate prevent the increase in serine esterase and phospholipase A2 activities and arachidonic acid release caused by A23187. A23187 still stimulated serine esterase and phospholipase A2 activities and arachidonic acid release in cells pretreated with nominal Ca2+ free buffer. Treatment of the cell membrane with A23187 does not cause any appreciable change in serine esterase and phospholipase A2 activities. Pretreatment of the cells with actinomycin D or cycloheximide did not prevent the increase in the cell membrane associated serine esterase and phospholipase A2 activities, and arachidonic acid release caused by A23187. These results suggest that (i) a membrane-associated A2 activity (ii) in addition to the presence of extracellular Ca2+, release of Ca2+ from intracellular storage site(s) by A23187 also appears to play a role in stimulating the cell membrane-associated serine esterase and phospholipase A2 activities does not appear to require new RNA or protein synthesis.
Mol Cell Biochem 1994 Jan 26
PMID:Role of membrane associated serine esterase in the activation of phospholipase A2 by calcium ionophore (A23187) in pulmonary arterial smooth muscle cells. 802 91

We have previously shown that CTL and NK cells rapidly down regulate perforin mRNA and become functionally inactive within 4-6 hr after exposure to sensitive target cells (TC). We report here for the first time that CTL also down regulate perforin mRNA upon exposure to resistant, but binding, TC. When three separate human MHC-restricted CTL lines were exposed to resistant TC, perforin mRNA was rapidly degraded. Removal of both extracellular Ca++ and Mg++ prevented perforin message down regulation, whereas removal of Ca++ alone did not, indicating that CTL:TC binding was required. Unlike the response of CTL exposed to sensitive TC, resistant TC did not trigger serine esterase (SE) release, suggesting distinct signalling pathways for perforin mRNA down regulation and granule exocytosis. Moreover, using western analysis, we showed that there was limited (< 10%) perforin protein release after CTL:TC interaction, suggesting that CTL loss of lytic activity after exposure to sensitive TC is not due to massive depletion of perforin. Treatment of CTL with mAb to CD2, CD3, CD2 + CD3, CD8, Class I and LFA-1 did not induce perforin mRNA down regulation. Furthermore, mAb to CD2, CD3, CD8, Class I, Class II, CD54 and LFA-1 did not block TC-mediated perforin mRNA down regulation although lysis of TC was inhibited.
Mol Immunol 1994 Apr
PMID:Target cell-directed degradation of perforin mRNA in CTL: lack of correlation with loss of protein and lytic ability. 815 43

The gene encoding a 23 kDA serine esterase from the cyanobacterium Spirulina platensis has been identified, cloned, characterized and expressed in Escherichia coli. The primary structure of the esterase deduced from the DNA sequence displayed 32% sequence identity with the carboxylesterase (esterase II) encoded by estB of Pseudomonas fluorescens; the highest degree of homology is found in a stretch of 11 identical or highly conserved amino acid residues corresponding to the GXSXG consensus motif found in the catalytic site of many serine proteases, lipases and esterases.
Mol Gen Genet 1994 Apr
PMID:Cloning and characterization of the gene encoding an esterase from Spirulina platensis. 819 66

The ges-1 gene codes for a non-specific carboxylesterase that is normally expressed only in the intestine of the nematode Caenorhabditis elegans. In the current paper, we describe the cloning and characterization of the ges-1 gene from C. elegans, as well as the homologous gene from the nematode Caenorhabditis briggsae. The ges-1 esterases from the two nematodes are 83% identical at the amino acid level and contain regions of significant similarity to insect and mammalian esterases; these conserved regions can be identified with residues believed to be necessary for esterase function. The ges-1 mRNAs from both C. elegans and C. briggsae are trans-spliced. The coding regions, the codon bias and the splicing signals of the two ges-1 genes are quite similar and most (6/7) of the intron positions are retained precisely. Yet, the flanking sequences of the two ges-1 genes appear to have diverged almost completely. For example, the C. elegans ges-1 5'-flanking region (as well as several introns) contains copies of three different SINE-like sequences, previously identified near the hsp-16 genes, near the unc-22 gene and in a repetitive element CeRep-3; none of these elements are found in the C. briggsae ges-1 gene. We show that: (1) the C. elegans ges-1 gene can be used to transform C. briggsae, whereupon expression of the exogenous ges-1 gene is confined to the C. briggsae intestine; (2) the ges-1 homologue cloned from C. briggsae can be transformed into C. elegans, whereupon it is expressed largely in the C. elegans intestine; and (3) a 5'-deletion of the C. elegans ges-1 gene that we have previously shown to be expressed in the C. elegans pharynx is also expressed in the pharynx of C. briggsae (either in the presence or absence of vector sequences). These results suggest that the ges-1 gene control circuits have been maintained between the two nematode species, despite the divergent 5'-flanking sequences of the gene. This raises the question of the evolutionary distance between C. elegans and C. briggsae and we attempt to estimate the C. elegans-C. briggsae divergence time by analysing the rate of synonymous substitutions in coding regions of ges-1 and six other C. elegans-C. briggsae gene pairs. We propose a new method of analysis, which attempts to remove rate differences found between different genes by extrapolating to zero codon bias.(ABSTRACT TRUNCATED AT 400 WORDS)
J Mol Biol 1993 Feb 20
PMID:The gut esterase gene (ges-1) from the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. 844 54

Carboxylesterase ESB3 was extracted from ovine liver and purified to homogeneity by ammonium sulphate fractionation, hydrophobic interaction chromatography on Phenyl Sepharose, ion exchange chromatography on Mono-Q Sepharose and size exclusion chromatography on Superose 6. The enzyme is free of carboxylesterase ESB2 activity. The molecular mass of the enzyme is estimated 182 kDa as judged by size exclusion chromatography. Isoelectric focusing indicates the presence of six isoforms of pI 5.50-5.77 with three main isoforms of pI 5.55-5.65. The enzyme is active towards the substrates p-nitrophenyl acetate and the aliphatic substrates ethyl acetate, ethyl propionate, ethyl butyrate, and ethyl valerate. Of the ethyl esters the affinity is lowest towards acetate and highest towards ethyl butyrate. The enzyme is totally inhibited by phenylmethylsulphonyl fluoride (PMSF) and mercuric chloride but not affected by eserine or cupric chloride. The pH optimum of the enzyme is 7.5 and it is stable at 55 degrees C for 20 min.
Comp Biochem Physiol B Biochem Mol Biol 1996 May
PMID:Purification and some properties of a carboxylesterase from ovine liver. 875 99


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