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PubMed1981

Studies of esterase 6 in Drosophila melanogaster. VI. ejaculate competitive abilities of males having null or active alleles.

Recent studies of the function of the polymorphic seminal fluid enzyme, esterase 6, of Drosophila melanogaster suggested that it may act in the process of sperm displacement (Gilbert, Richmond and Sheehan, 1981a). This report examines the competitive ability of ejaculates from males homozygous for null or active alleles of esterase 6 under three experimental conditions that model aspects of sexual selection affecting males. The results demonstrate no significant difference in ejaculate competition between esterase 6 null or active male types, but marker males used for paternity identification had poorly competitive ejaculates. The proportion of second-male progeny, P2, used as an index of competition is primarily influenced by second-male genotype and uninfluenced by female genotype, P2 can change with time from remating and be unaffected by different intensities of competition, which suggests a complex ejaculate competition mechanism.

Animals↗
PubMed1993

Activity and electrophoretic characterization of esterases in insecticide-resistant and susceptible strains of German cockroach (Dictyoptera: Blattellidae).

Strains of German cockroach, Blattella germanica (L.) were tested for resistance to three insecticides using the time-mortality response technique in comparison with known susceptible strains. Dursban-R and Macy strains indicated high levels of resistance to chlorpyrifos and moderate resistance to propoxur and cypermethrin. The hydrolytic activity of esterase enzymes was determined with a model substrate, p-nitrophenyl acetate. The specific activity of the enzymes increased with a corresponding increase in substrate concentration. Maximum activity was observed at 80 microM. The resistant strains had significantly higher activity than the susceptible strains. The enzyme activity also increased with an increase in pH. Highest esterase activity was observed at pH 8.0 for all the strains. The calculated Michaelis Menten constant (Km) values for the resistant strains were nearly two-fold higher than for the susceptible strains. Nondenaturing gel electrophoresis revealed differences in isozyme composition. In total, 10 esterase bands were detected, and these bands were characterized using different inhibitors and substrates.

Animals↗
PubMed1994

Subcellular distribution and characterization of esterase isozymes from insecticide-resistant and -susceptible strains of German cockroach (Dictyoptera: Blattellidae).

Esterases from insecticide-resistant and -susceptible strains of German cockroach, Blattella germanica (L.), were isolated and analyzed for differences in activity. The isozymes E5, E6, E7, and E8 of resistant strains indicated about two- to fivefold increases in activity compared with those of the susceptible strain. These isozymes constituted approximately 60% of the total activity in the resistant strains, whereas they contributed only about 40% activity in the susceptible strain. Subcellular distribution studies showed that most esterase activity is present in the 100,000 x g fraction of the homogenate (cytosolic). Only a small portion of activity was membrane bound. Molecular weights of the esterase isozymes calculated based on their retardation coefficients ranged between 48 and 81 kd.

Animals↗
PubMedDate not supplied

Recombination between two amplified esterase alleles in Culex pipiens.

Esterase gene amplification at the Ester superlocus provides organophosphate resistance in the mosquito Culex pipiens (L.). In this study we explored the possibility of recombination between two amplified esterase alleles, thus generating a composite amplified allele. To do that, females heterozygous for two distinct amplified alleles (Ester(2) and Ester(4)) were crossed with males homozygous for a third resistance allele (Ester(8)). Among analyzed offspring, one recombinant composite allele (Ester(2-4)) was detected, providing a rate of recombination of approximately 0.2%. This is the first report of a recombination between two distinct amplified esterase alleles. This phenomenon renders the predictability of allele evolution considerably more complex than was previously thought.

Animals↗
PubMed1976

Relationship between the structures of S-acyl thiol compounds and their rates of hydrolysis by pancreatic lipase and hepatic carboxylic esterase.

About 100 S-fatty acyl thiol compounds designed as substrates for pancreatic lipase [EC 3.1.1.3] were synthesized and tested for susceptibility to hydrolysis by hog pancreatic lipase and hog hepatic carboxylic esterase [EC 3.1.1.1] using 5,5'-dithiobis(2-nitrobenzoic acid) as a chromogenic reagent to determine the hydrolytic rates of their S-acyl bonds. In general, the hydrolytic rates of S-acyl bonds by the lipase were fast with thioglycerol type thiol moieties, slow with dithioethyleneglycol type or monothiol type, and negligible with thiopolyol type. As for the acyl moieties, the hydrolysis of the S-acyl bonds was fast with C3-5 acyl groups, followed by C6-8 acyl groups, and the rate decreased as the acyl chain length deviated from these values or branched. On the other hand, the hydrolysis of S-acyl bonds by the esterase occurred with all types of S-acyl esters except for esters of long S-acyl chains. Of all the compounds tested with the lipase, the rate of hydrolysis of S-acyl bond was maximum with 2,3-dimercaptopropan-1-ol tributyroate [I], high with 3-mercaptopropane-1,2-diol tributyroate [II], but negligible with the analogous compound, 1,3-dimercaptopropan-2-ol tributyroate. Compounds [I] and [II] may be practically useful as substrates for lipase assay in human serum samples pretreated with phenylmethylsulfonyl fluoride, a potent inhibitor against both serum arylesterase [EC 3.1.1.2] and hepatic esterase, which attack [I] and [II].

Alcohols↗
PubMedDate not supplied

A trimeric esterase in the common shrew.

A variable kidney esterase found in the common shrew has a trimeric structure as indicated by the phenotypes of heterozygotes. From substrate specificity and tissue distribution this enzyme appears to be homologous with esterase-6 of the mouse, also a trimeric enzyme. It is suggested that a trimeric esterase may have been a feature of early eutherian mammals.

Animals↗
PubMed1996

Molecular evolution of the Sex-Ratio inversion complex in Drosophila pseudoobscura: analysis of the Esterase-5 gene region.

The Sex-Ratio chromosome in Drosophila pseudoobscura is subject to meiotic drive. It is associated with a series of three nonoverlapping paracentric inversions on the right arm of the X chromosome. The esterase-5 gene region has been localized to section 23 within the subbasal inversion of the Sex-Ratio inversion complex, making esterase-5 a convenient locus for molecular evolutionary analyses of the Sex-Ratio inversion complex and the associated drive system. A 504-bp fragment of noncoding, intergenic DNA from the esterase-5 gene region was amplified and sequenced from 14 Sex-Ratio and 14 Standard X chromosomes of D. pseudoobscura, and from 9 X chromosomes of its two sibling species, Drosophila persimilis and Drosophila miranda. There is extensive sequence differentiation between the Sex-Ratio and Standard chromosomal types. The common Standard chromosome is highly polymorphic, while, as expected from either the neutral mutation theory or the selective sweep hypothesis, the rarer Sex-Ratio chromosome has much less within-chromosome nucleotide polymorphism. We estimate that the Standard and Sex-Ratio chromosomes in D. pseudoobscura diverged between 700,000 and 1.3 Mya, or at least 2 million generations ago. The clustering of D. pseudoobscura Sex-Ratio chromosomes in a neighbor-joining phylogeny indicates a fairly old, monophyletic origin in this species. It appears from these data that Sex-Ratio genes were present prior to the divergence of D. pseudoobscura and D. persimilis and that both the Standard and Sex-Ratio chromosomes of D. persimilis were derived from the Standard chromosome of D. pseudoobscura after the inversion events that isolated the D. pseudoobscura Sex-Ratio chromosome.

Animals↗
PubMed2000

The evolution of an alpha-esterase pseudogene inactivated in the Drosophila melanogaster lineage.

Previous analyses of the alpha-esterase cluster of Drosophila melanogaster revealed 10 active genes and the DmalphaE4a-Psi pseudogene. Here, we reconstruct the evolution of the pseudogene from the sequences of 12 alleles from widely scattered D. melanogaster populations and single alleles from Drosophila simulans and Drosophila yakuba. All of the DmalphaE4a-Psi alleles contain numerous inactivating mutations, suggesting that pseudogene alleles are fixed in natural populations. Several lines of evidence also suggest that DmalphaE4a is now evolving without selective constraint in the D. melanogaster lineage. There are three polymorphic indels which result in frameshifts; a key nucleotide of the intron splice acceptor is polymorphic; the neutral mutation parameter is the same for replacement and silent sites; one of the nonsilent polymorphisms results in a stop codon; only 1 of the 13 replacement polymorphisms is biochemically conservative; residues that are conserved among active esterases have different states in DmalphaE4a-Psi; and there are about half as many transitional polymorphisms as transversional ones. In contrast, the D. simulans and D. yakuba orthologs DsalphaE4a and DyalphaE4a do not have the inactivating mutations of DmalphaE4a-Psi and appear to be evolving under the purifying selection typical of protein- encoding genes. For instance, there have been more substitutions in the introns than in the exons, and more in silent sites than in replacement sites. Furthermore, most of the amino acid substitutions that have occurred between DyalphaE4a and DsalphaE4a are located in sites that typically vary among active alpha-esterases rather than those that are usually conserved. We argue that the original alphaE4a gene had a function which it has lost since the divergence of the D. melanogaster and D. simulans lineages.

Amino Acid Sequence↗
PubMed1998

Converting trypsin to elastase: substitution of the S1 site and adjacent loops reconstitutes esterase specificity but not amidase activity.

The conversion of trypsin into a protease with chymotrypsin-like activity and specificity required substitution of fifteen residues in the S1 site and two surface loops with their chymotrypsin counterparts [Hedstrom,L., Szilagyi,L. and Rutter,W.J. (1992) Science, 255, 1249-1253]. These residues may define a set of general structural determinants of specificity in the trypsin family. In order to test this hypothesis, we have attempted to convert trypsin into a protease with specificity for substrates containing small aliphatic residues by replacing the S1 site and these surface loops with the analogous residues of elastase. Five elastase-like mutant enzymes were constructed with various combinations of these substitutions. Four mutant enzymes catalyze the hydrolysis of MeOSuc-Ala-Ala-Pro-Ala-SBzl more efficiently than the hydrolysis of Suc-Ala-Ala-Pro-Phe-SBzl. This observation indicates that the mutant enzymes have elastase-like esterase specificity. The best mutant, Tr-->E1-2, is a more specific esterase than elastase: the ratio of the values of kcat/Km for MeOSuc-Ala-Ala-Pro-Ala-SBzl and Suc-Ala-Ala-Pro-Phe-SBzl is greater than 160 for Tr-->E1-2 and 50 for elastase. However, the esterase activity of Tr-->E1-2 is 300-fold less than elastase; in addition, Tr-->E1-2 has no measurable amidase activity. Thus these substitutions do not construct a protease with elastase-like activity. These experiments indicate that a unique structural solution is required for each different specificity. Previous work suggested that instability of the S1 site is a major barrier to redesigning the specificity of trypsin. This view is corroborated by preliminary structural studies of Tr-->E1-2. One dimensional 1H NMR spectrum of Tr-->E1-2 suggests that the S1 site and the two surface loops of this mutant trypsin may be disordered.

Amidohydrolases↗
PubMed2000

Carboxylesterase and A-esterase activities during maturation and aging: relationship to the toxicity of chlorpyrifos and parathion in rats.

Chlorpyrifos (CPF) and parathion (PS), two common organophosphorus (OP) pesticides, exhibit higher acute toxicity in younger animals compared to adults. Maturational differences in detoxification via carboxylesterases (CEs) and A-esterases (AEs) have been suggested as contributors to the higher sensitivity of younger animals to OP toxicants. AEs (e.g., chlorpyrifos oxonase and paraoxonase) catalytically inactivate while CEs stoichiometrically eliminate OP anticholinesterases. While earlier studies have reported a relationship between the toxicity of some OP pesticides and the maturational profile of AEs and CEs, little information exists on the relative OP-toxicant sensitivity and detoxification capacities of aged animals. In the present study, we investigated the relationship between toxicity of CPF and PS and the activity of CEs and AEs in liver, plasma, and lung of neonatal (7 day), juvenile (21-day), adult (3-month), and aged (24-month) Sprague Dawley rats. CE sensitivity in vitro to chlopyrifos oxon and paraoxon was also evaluated across age groups. Neonatal and juvenile rats were more sensitive than adults to the acute lethality of both CPF and PS. Aged rats exhibited similar sensitivity to CPF but were markedly more sensitive than adults to PS. Levels of CEs and AEs in neonatal and juvenile rats were significantly lower than in adult tissues. Aged rats showed similar levels of AEs in all tissues and CEs in liver and lung, but plasma CE levels were significantly lower (50%) when compared to the adult rats. There were no significant age-related differences in in vitro sensitivity of CEs to either chlorpyrifos oxon or paraoxon in any tissues. In general, acute sensitivity (MTD) was highly correlated with age-related differences in both esterase activities across all 3 tissues with CPF, but only plasma carboxylesterase activity was highly correlated with sensitivity to parathion. The results suggest that both carboxylesterase and A-esterase activities can be correlated with acute sensitivity to CPF and PS, but that age-related differences in CE activity are probably more important in differential toxicity. Furthermore, plasma carboxylesterase activity may play a more pivotal role in the differential sensitivity to PS.

Age Factors↗
PubMed2001

Inhibition of fungal appressorium formation by pepper (Capsicum annuum) esterase.

A pepper esterase gene (PepEST) that is highly expressed during an incompatible interaction between pepper (Capsicum annuum) and the anthracnose fungus Colletotrichum gloeosporioides has been previously cloned. Glutathione-S-transferase-tagged recombinant PepEST protein expressed in Escherichia coli showed substrate specificity for p-nitrophenyl esters. Inoculation of compatible unripe pepper fruits with C. gloeosporioides spores amended with the recombinant protein did not cause anthracnose symptoms on the fruit. The recombinant protein has no fungicidal activity, but it significantly inhibits appressorium formation of the anthracnose fungus in a dose-dependent manner. An esterase from porcine liver also inhibited appressorium formation, and the recombinant protein inhibited appressorium formation in the rice blast fungus, Magnaporthe grisea. Inhibition of appressorium formation in M. grisea by the recombinant protein was reversible by treatment with cyclic AMP (cAMP) or 1,16-hexadecanediol. The results suggest that the recombinant protein regulates appressorium formation by modulating the cAMP-dependent signaling pathway in this fungus. Taken together, the PepEST esterase activity can inhibit appressorium formation of C. gloeosporioides, which may result in protection of the unripe fruit against the fungus.

Capsicum↗
PubMed1995

Esterase activity in the olfactory sensilla of the silkmoth Antheraea polyphemus.

We studied in individual males of Antheraea polyphemus the activity of the sensillar esterase, a pheromone-degrading enzyme present in the sensillum lymph surrounding the olfactory receptor cells. In parallel, receptor potentials from single pheromone-sensitive sensilla trichodea were recorded. Our screening revealed a large variability of the enzyme activity in individuals with similar electrophysiological responses. In some moths the sensillar esterase was not detectable, i.e. present with 100-fold less activity. However, such variable esterase activity showed no correlation to the time course of the receptor potential. Thus, enzymatic pheromone degradation does not seem to be involved in the rapid pheromone inactivation at the end of the stimulus, but rather serves as the final pheromone sequestration step.

Animals↗
PubMed1978

The null allele in the horse esterase (Es) system detected by enzyme assay and rocket immunoelectrophoresis in heterozygous animals.

The detection of the recessive null allele of horse serum esterase (Es) is possible in heterozygotes Es+/EsO which by starch gel electrophoresis appear like homozygotes Es+/Es+. Two methods are proposed, the titration of enzymatic activity of esterase and the immunochemical titration of esterase as antigen. These methods can be applied to solve the cases of suspect parentage or in population studies.

Alleles↗
PubMed1984

Polymorphism and inheritance of serum esterases and beta-globulins in the paradise fish (Macropodus opercularis; Anabantidae).

Electrophoretic variants of serum esterases and beta-globulins in two subspecies of paradise fish (Macropodus opercularis) were studied. Four esterase loci (Est-1, Est-2, Est-3 and Est-4), a single transferrin (Tf) and another major beta-globulin locus (Bg) were identified by segregational analysis. Est-3 seems to be a monomorphic locus. Three alleles of Est-1, two of Est-2, two of Est-4, four of Tf and two alleles of Bg were found in the laboratory population. None of these loci were closely linked. Electrophoretic patterns of F1 hybrids confirmed the monomeric structures of each of the studied proteins. Allelic segregation at the Tf and Bg loci was normal in F2 and backcross populations. In crosses of the two Macropodus subspecies there were deviations from Mendelian ratios because of missing recombinant esterase phenotypes. Each of these would have been homozygous Est-2f/f. We suppose that Est-2f/f causes lethality in the early phase of development, except in the Est-1c/c, Est-2f/f combination characteristic of the parental subspecies M.o. concolor.

Alleles↗
PubMed1992

Substrate specificity of purified rabbit liver esterase ES-1.

1. Substrate hydrolysis by two purified rabbit liver esterase-1 allozymes (ES-1A and ES-1B) was compared under conditions differing in substrate, pH and temperature. ES-1A and ES-1B activities had a similar pH and temperature dependency and similar thermal stability profile. 2. There were marked differences in specific activity of ES-1A and ES-1B. ES-1A hydrolysed procaine more rapidly than ES-1B, but was less active towards aspirin. The acetate and propionate esters of p-nitrophenyl were hydrolysed slower by ES-1A than by ES-1B. 3. The effect of substrate concentration on ES-1A activity did not comply with the Michaelis-Menten kinetics, which may be due to so-called substrate activation. 4. At identical substrate concentration, pH and temperature, selected artificial esters were better substrates for ES-1A than selected physiological substrates. Beta-Naphthyloctanoate was found to be a suitable substrate for ES-1A. 1,3-Dioctanoylglycerol was hydrolysed at a rate of only 2% of that of beta-naphthyloctanoate. 5. With methyl, p-nitrophenyl, beta-naphthyl and 4-methylumbelliferyl esters as substrates, ES-1A activity is influenced by length and structure of the acyl moiety. Likewise, ES-1A activity is influenced by the nature of the alkyl moiety of acetate esters. With acetate and methyl esters, branched chains when compared with unbranched chains reduced the esterase activity of ES-1A. Elongation of the acyl moiety up to four or five C atoms gradually raised the velocity of methyl, p-nitrophenyl, and 4-methylumbelliferyl ester hydrolysis by ES-1A. A similar pattern was found for the length of the alkyl moiety of acetate esters. 6. The high degree of similarity between the observed substrate specificity of rabbit ES-1A and that reported earlier for rat ES-10, suggests that these two esterases have a common evolutionary origin.

Animals↗
PubMed1976

Two esterases common to seminal plasma, other external secretions and leucocytes in man.

Two esterases previously identified in seminal plasma, on the basis of their electrophoretic mobility, immunogenicity and sensitivity to organophosphorus esters were detected in various human external secretions and leucocyte extracts. alpha-Esterase was found to be abundant in urine and milk whereas this enzyme occurred in a low concentration in seminal plasma, leucocyte extract, cervical mucus and sweat. The concentration of betagamma-esterase was high in seminal plasma and leucocyte extract. The enzyme was present in small amounts in urine, milk, gastric juice, saliva, sputum, tears, cervical mucus and sweat.

Bronchitis↗
PubMed1997

Membrane phenotype and expression of perforin and serine esterases by CD3- peripheral blood and decidual granular lymphocyte-derived clones.

PROBLEM: Human first-trimester pregnancy decidua were found to contain large numbers of perforin (P)-containing cells, which varied in their membrane antigen phenotype. In this study results obtained by analyzing CD3- clones derived from human early pregnancy decidua and peripheral blood are reported. METHOD OF STUDY: Decidual tissue was obtained from vaginal termination of first trimester normal human pregnancies. CD3- clones were generated by limiting dilution cloning after the depletion of CD3+ lymphocytes. The cell membrane phenotype was determine by flow cytometry. Perforin was detected by fluorescence-activated cell sorter (FACS) analysis of permeabilised cells. Serine esterases (SE) were identified by histochemical staining for BLT-esterase. RESULTS: Cloned decidual cell populations retained the overall antigenic phenotype of freshly isolated decidual natural killer (NK)-like cells. All CD3- clones, either derived from decidua or from peripheral blood contained perforin. Serine esterases were present in every decidual clone analyzed. CONCLUSIONS: Limiting dilution cloning allows the clear-cut analysis of homogenous subsets of decidua-derived NK-like clones. The presence of large amounts of perforin in all of the CD3- clones underlines the extensive transcription of the perforin gene by NK-like lymphocytes.

Antigens, Surface↗
PubMed2005

Changes in translucency of resin composites after storage in salivary esterase.

BACKGROUND: Dental resin composites are degraded by salivary enzymes, but the enzymatic influence on the translucency of resin composites has not been determined. PURPOSE: The purpose of this study was to evaluate the changes in translucency of resin composites after storage in the salivary enzyme esterase (ETE, porcine liver esterase, 400 mU/mL) compared with those in phosphate-buffered saline (PBS). MATERIALS AND METHODS: The colors of specimens of three brands of resin composites of various shades were measured after polymerization and polishing (baseline), and after immersion in PBS or ETE for 9 weeks; measurements were determined over white and black backgrounds according to the CIELAB color scale (established by Commission Internationale de l'Eclairage). The final specimen thickness was 1.75 mm. Translucency parameter (TP) was obtained by calculating the color difference between the specimen over a white background and that over a black background. Two-factor, repeated-measures analysis of variance was used to compare differences. RESULTS: TP values varied among and within different shade designations and also among different brands of resin composites. TP values were significantly changed after immersion in PBS and ETE and were influenced by the brand of resin composites, but they were not influenced differently by the immersion solutions of PBS and ETE (p = .05). CLINICAL SIGNIFICANCE: Translucency of dental resin composites is an important esthetic consideration. Based on the results of this study, the influence of salivary esterase on the changes in translucency of dental resin composites is not significantly different from that of phosphate-buffered saline. Therefore, it can be concluded that the enzymatic effects of saliva do not adversely alter the translucency of dental resin composites.

Analysis of Variance↗