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PubMedDate not supplied

Development of esterase activities in the chicken before and after hatching.

The embryonic chick has long been a model for developmental biology and has often been recommended as a model system in developmental toxicology. More recently, several investigators have shown that the chick embryo also provides a good model for identifying the neurotoxic effects of environmental pollutants, especially cholinesterase-inhibiting pesticides. Although numerous studies detail the structural development of chick embryos, few describe embryonic levels of enzyme synthesis and their changes during development. In this study, the development of esterase activity in chick embryos was measured from day 9 of incubation until 46 days after hatching. Brain acetylcholinesterase (AChE) activity was detected on day 9 of incubation at a concentration of 0.364 mumoles/min/g tissue. An increase between AChE activity and age of the embryos was observed. In the liver, the nonspecific cholinesterases (ChE) and carboxylesterase activities during incubation were not different from activities after the chicks had hatched. Plasma ChE and carboxylesterase activities did not change with age after hatching. Brain neuropathy target esterase (NTE) activity was not detected on day 9 of incubation and was extremely low (6.12 nmoles/15 min/mg protein) the next day, but increased rapidly with increasing age. This study demonstrates that chick embryos have developed esterase activities in the brain and liver by day 10 of incubation and again confirms that the insensitivity of chick embryos and young chicks to organophosphorus ester-induced delayed neurotoxicity is not due to absence of NTE. In addition, the results provide baseline data for evaluating the response of embryonic and immature chicks to neurotoxicants and teratogens.

Acetylcholinesterase↗
PubMedDate not supplied

Distinctive electrophoretic pattern of esterases produced by Alcaligenes species.

The esterases produced by 34 strains of Alcaligenes faecalis, 16 strains of A. denitrificans subsp. xylosoxydans, 5 strains of A. piechaudii and 10 strains of A. denitrificans subsp. denitrificans were analysed by horizontal polyacrylamide-agarose gel electrophoresis. These enzymes were distinguished by their spectra of hydrolytic activity towards 5 synthetic substrates (hydrolytic type) and their electrophoretic mobilities (electrophoretic type). Four hydrolytic types of esterases were produced by A. faecalis, three hydrolytic types by A. denitrificans subsp. xylosoxydans, three hydrolytic types by A. piechaudii and 14 hydrolytic types by A. denitrificans subsp. denitrificans. Both (hydrolytic and electrophoretic) properties and the pattern of esterases produced by each strain were used to define 8 zymotypes in A. faecalis, 6 zymotypes in A. denitrificans subsp. xylosoxydans, 3 zymotypes in Alcaligenes piechaudii and 10 zymotypes in Alcaligenes denitrificans subsp. denitrificans. These results permit precise identification of strains within the four species of Alcaligenes and provide useful epidemiological markers.

Alcaligenes↗
PubMed1994

Biotyping, ribotyping and esterase electrophoresis as epidemiological tools for Acinetobacter baumannii.

An epidemiological survey was carried out over a one-week period to assess the spread of Acinetobacter baumannii in a medical intensive care unit. Fifty strains were isolated from patients colonized or infected by the organism and from a hospital environment. These strains belonged to biotypes 9 or 18. The rRNA gene restriction patterns (using EcoRI and PvuII as restriction endonucleases) and the esterase electrophoretic profiles were determined on 31 strains, using as comparison strain isolates from another intensive care unit of our hospital and from two other French hospitals. Four EcoRI ribotypes, four PvuII ribotypes and six esterase profiles were identified. All biotype 9 strains isolated in our hospital presented the same ribotype after EcoRI digestion, the same ribotype after PvuII digestion and the same zymotype. The same observation was made on most of the biotype 18 strains. Biotyping is an appropriate method for screening of strains, and ribotyping and esterase electrophoresis could be used as additional methods to delineate outbreaks of nosocomial infections caused by A. baumannii.

Acinetobacter↗
PubMed1995

Combination of biotyping and electrophoretic patterns of esterases for differentiation of nosocomial Serratia marcescens strains.

A total of 292 Serratia marcescens strains isolated in seven Belgian hospitals between 1986 and 1992 were submitted to both biotyping by carbon source utilization and esterase electrophoresis typing. The strains were assigned to 11 biotypes (290 isolates) or were auxotrophic (2 isolates), whereas the various electrophoretic patterns of their esterases produced 54 zymotypes. The two typing methods correlate well, since biotypes embraced more than one zymotype, while each zymotype was restricted to a single biotype. Esterase electrophoretic patterns represent a potent marker for delineating outbreaks of nosocomial infections, whereas biotyping appears to be an appropriate method for screening of strains.

Bacterial Typing Techniques↗
PubMed1990

Purification of a membrane-associated serine esterase from murine cytotoxic T lymphocytes by a single reverse-phase column.

The plasma and organelle membranes of a cytotoxic T lymphocyte line, CTLL-R8, were isolated by subcellular fractionation. After dissolving in detergent-containing buffer, the membrane proteins were isolated by high-performance liquid chromatography on a single reverse-phase column. The serine esterase activity in the fractions was detected by measuring hydrolysis of the ester compound N alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester. A major band was revealed in the fraction with highest serine esterase activity. Under sodium dodecyl sulfate-polyacrylamide gel electrophoresis, this band assumes a molecular weight of about 30 kDa. The amino-terminal sequence of the protein was analyzed and shows 100% identity with that of MCSP-3/granzyme F, a soluble serine esterase previously identified in the cytoplasmic granules of cytotoxic T lymphocytes. Modifications of this reverse-phase column method would thus represent a simple, convenient strategy for obtaining high yields of all the lymphocyte surface proteases, which could then be further characterized for function.

Amino Acid Sequence↗
PubMed2005

Characterization of a thermoalkalophilic esterase from a novel thermophilic bacterium, Anoxybacillus gonensis G2.

Poly-3-hydroxybutyrate (P3HB) degradation capabilities of a novel bacterium, Anoxybacillus gonensis G2, were investigated. Both changes on film surfaces of the solution-cast films monitored by scanning electron microscopy (SEM) and weight loss up to 24% after 72 h exposure to A. gonensis G2 cultures indicated secretion of an active esterase responsible for the degradation of P3HB films. Kinetic parameters, Vmax and Km for the esterase activity of crude enzyme from A. gonensis G2 in the presence of p-nitrophenylbutyrate as substrate were observed as 50 U/L and 0.125 mM, respectively, in 50 mM phosphate buffer, pH 7.5 at 60 degrees C. The stimulation of the activity by Ca2+ is an evidence for the requirement of Ca2+ as a cofactor for the enzyme activity which is a characteristic for lipases/esterases. Inhibition of the esterase activity by metal chelating agents such as ethylenediamine tetraacetate, azide and cyanide has also supported the requirement of a metal ion for the activity. The thermal and pH stability profiles for the enzyme showed that the thermophilic bacterium A. gonensis G2 secretes an extracellular thermoalkalophilic PHB depolymerase active at 60 degrees C, and stable at this temperature for 120 min at pH 7.5 and for 24 h at pH 7.5-9.5 range at 4 degrees C by retaining over 75% of its initial activities.

Analysis of Variance↗
PubMed2005

Optimization of recombinant hyperthermophilic esterase production from agricultural waste using response surface methodology.

The aim of this work was to evaluate the capability of corn steep liquor being a low cost substrate on the recombinant protein production by cultivating recombinant Escherichia coli and increasing the production of hyperthermophilic esterase (HE). The effect of corn steep liquor, mineral salt and trace metals on hyperthermophilic esterase production was investigated by means of a five-level three-factor central composite rotatable design. Optimized values of the factors were determined and a maximum hyperthermophilic esterase production of 251.39 U/ml was obtained. This value equaled the yield by yeast extract and peptone medium on the whole.

Aeropyrum↗
PubMed2005

Role of the N terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family.

A superposition between the structures of Alicyclobacillus acidocaldarius esterase 2 (EST2) and Burkholderia cepacia lipase, the latter complexed with a phosphonate inhibitor, allowed us to hypothesize for the EST2 N terminus a role in restricting the access to the active site and therefore in modulating substrate specificity. In order to test this hypothesis we generated by site-directed mutagenesis some truncated versions of EST2 and its double mutant M211S/R215L (S/L) at the N terminus. In parallel, an analysis of the Sulfolobus solfataricus P2 genome allowed us to identify a gene coding for a putative esterase of the HSL family having a natural deletion of the corresponding region. The product of this gene and the above-mentioned EST2 mutants were expressed in Escherichia coli, purified and characterised. These studies support the notion that the N terminus affects substrate specificity other than several other enzyme parameters. Although the deletions afforded a tenfold and 550-fold decrease in catalytic efficiency towards the best substrate pNP-hexanoate at 50 degrees C for EST2 and S/L, respectively, the analysis of the specific activities with different triacylglycerols with respect to pNP-hexanoate showed that their ratios were higher for deleted versus non-deleted enzymes, on all tested substrates. In particular, the above ratios for glyceryl tridecanoate were 30-fold and 14-fold higher in S/L and EST2 deleted forms, respectively, compared with their full-length versions. This behaviour was confirmed by the analysis of the S.solfataricus esterase, which showed similar specific activities on pNP-hexanoate and triacylglycerols; in addition, higher activities on the latter substrates were observed in comparison with EST2, S/L and their deleted forms. Finally, a dramatic effect on thermophilicity and thermostability in the EST2 deleted forms was observed. This is the first report highlighting the importance of the "cap" domain in the HSL family, since the N terminus partly contributes to the building up of this structure.

Amino Acid Sequence↗
PubMed2006

Esterase activities and lipid peroxidation levels in offshore commercial species of the NW Mediterranean Sea.

There is a lack of information on monitoring neurotoxicity in offshore commercial species. To help fill this gap, we sampled hake (Merluccius merluccius) and Norway lobster (Nephrops norvegicus) in fishing grounds off the coast of l'Ametlla de Mar (NW Mediterranean) in June 2005 at a depth of 100 m and 400 m. Additionally, at 400 m depth, two other fish species, Micromesistius poutassou and Phycis blennoides were included. Neurotoxicity markers such as Colinesterases (ChEs), namely acethyl- (AChE), butyryl- (BChE), propionyl- (PrChE) and carboxilesterase (CbE) were measured in muscle. Lipid peroxidation (LP), a marker of oxidative damage, was also included. The results are discussed in relation to the animal's sex, size and fishing depth. A comparison of esterases and LP levels between muscle and liver of hake and between muscle and hepatopancreas of Norway Lobster was made. AChE was dominant in muscle and CbE in hepatopancreas. No differences between fish species were seen for AChE. However, N. norvegicus, presented lower levels of ChEs and LP. A size-dependence in ChEs was seen for M. merluccius, with larger animals showing significantly lower activities (p<0.05). Sex-dependence was seen in N. norvegicus for most esterases, except AChE, with males displaying higher activities (p<0.05). A sampling-depth effect was also seen in the crustacea, with animals from 100 m generally presenting lower esterase activities and higher LP levels.

Animals↗
PubMed2001

Concentration-dependent effects of the esterase inhibitor BNPP on macrophage migration and myelin phagocytosis.

Wallerian degeneration of a peripheral nerve is mainly characterized by axon and myelin degradation and is paralleled by a massive invasion of peripheral macrophages into the nerve. These cells enter the nerve attracted by a cascade of chemokines and cytokines but require proteolytic and enzymatic factors which enables them to cross the blood-nerve barrier. Here we investigated whether alpha-naphthyl (alpha-NA) esterases -- which have been shown to be exclusively expressed in human monocytes -- play a role during Wallerian degeneration. These enzymes were blocked by the specific inhibitor bis(4-nitrophenyl)-phosphate (BNPP) in an established in vitro model of Wallerian degeneration. Sciatic nerve segments of mice were co-cultured with peritoneal macrophages and BNPP was added to the cultures in various concentrations and at different timepoints. The macrophage numbers and myelin density in the nerve segments and the myelin load of macrophages were evaluated. After BNPP treatment the macrophage number within the nerve was significantly diminished and the myelin load within the macrophages was decreased, resulting in elevated levels of preserved myelin within the nerves. These experiments clearly showed a double effect of the alphaNA esterase inhibitor BNPP on macrophages. First, it suggests a role for alphaNA esterases on the migratory potential of macrophages since their invasion into the nerves was diminished. Second, the reduced myelin uptake is due to the inhibition of phagocytic capacity of these cells by BNPP. The therapeutical use of this inhibitor for treatment of autoimmune diseases such as multiple sclerosis or Guillain-Barré syndrome remains to be investigated.

Animals↗
PubMed1976

Lactate and malate dehydrogenase and alpha-esterases in oligospermia.

Lactate dehydrogenase (LDH), malate dehydrogenase, and alpha-esterase were studied electrophoretically in a total of 99 semen samples obtained from normal, vasectomized, oligospermic, and infertile males. The enzymatic patterns were compared with total sperm count and percentage sperm motility. Lactate dehydrogenase X was absent in semen samples from oligospermic as well as vasectomized males. An extra LDH band (between the second and third LDH bands) was detectable in samples which had a low sperm count but higher motility (80 to 90%). This extra band was absent in samples with higher sperm count regardless of the level of percentage motility, suggesting that the extra band possibly may be related to motility factors of low sperm count but not normal sperm count. The fastest moving alpha-esterase bands were absent in samples from oligospermic or vasectomized males. These bands were also absent in samples from infertile patients having a very low sperm count. It is not clear whether the fast-moving esterase bands are related to sperm count or possible differences in hormonal levels of individuals with low or zero sperm count samples. The patterns of malate dehydrogenase did not differ in individuals with zero, low, or normal sperm count.

Electrophoresis, Starch Gel↗
PubMed2002

Purification and partial amino acid sequences of an esterase from tomato.

Screening of 18 suspension plant cell cultures of taxonomically distant species revealed that a methyl jasmonate hydrolysing enzyme activity (0.21-5.67 pkat/mg) occurs in all species so far analysed. The methyl jasmonate hydrolysing esterase was purified from cell cultures of Lycopersicon esculentum using a five-step procedure including anion-exchange chromatography, gel-filtration and chromatography on hydroxylapatite. The esterase was purified 767-fold to give an almost homogenous protein in a yield of 2.2%. The native enzyme exhibited a M(r) of 26 kDa (gel-filtration chromatography), which was similar to the M(r) determined by SDS-PAGE and MALDI-TOF analysis (M(r) of 28547 kDa). Enzyme kinetics revealed a K(m) value of 15 microM and a V(max) value of 7.97 nkat/mg, an pH optimum of 9.0 and a temperature optimum of 40 degrees C. The enzyme also efficiently hydrolyzed methyl esters of abscisic acid, indole-3-acetic acid, and fatty acids. In contrast, methyl esters of salicylic acid, benzoic acid and cinnamic acid were only poor substrates for the enzyme. N-Methylmaleimide, iodacetamide, bestatin and pepstatin (inhibitors of thiol-, metal- and carboxyproteases, respectively) did not inactivate the enzyme while a serine protease inhibitor, phenylmethylsulfonyl fluoride, at a concentration of 5 mM led to irreversible and complete inhibition of enzyme activity. Proteolysis of the pure enzyme with endoproteinase LysC revealed three peptide fragments with 11-14 amino acids. N-Terminal sequencing yielded an additional peptide fragment with 10 amino acids. Sequence alignment of these fragments showed high homologies to certain plant esterases and hydroxynitrile lyases that belong to the alpha/beta hydrolase fold protein superfamily.

Acetates↗
PubMedDate not supplied

Esterases as biomarkers in Nereis (Hediste) diversicolor exposed to temephos and Bacillus thuringiensis var. israelensis used for mosquito control in coastal wetlands of Morbihan (Brittany, France).

Since 1998, a biomonitoring programme has been implemented to assess the potential impact of chemical mosquito control on macroinvertebrates of the coastal wetlands of Morbihan (Brittany, France). Acetylcholinesterase and carboxylesterases were used as biomarkers to assess the effects of Abate 500e (a.i. temephos) and Vectobac 12 AS (a.i. endotoxins of Bacillus thuringiensis var. israelensis, Bti) in Nereis (Hediste) diversicolor. Esterase inhibition revealed a marked impact of temephos, suggesting preferential contamination of the worms through the food. In Bti-exposed N. diversicolor, random variations of esterase activities were observed, that could not be attributed to the larvicide. However, esterases only reflected indirect physiological effects of Bti, and further investigations are needed to identify biomarkers more specific of Bti endotoxins.

Animals↗
PubMed1999

Structure-reactivity probes for active site shapes of cholesterol esterase by carbamate inhibitors.

4,4'-Biphenyl-di-N-butylcarbamate (1), (S)-1,1'-bi-2-naphthyl-2, 2'-di-N-butylcarbamate (S-2), (S)-1, 1'-bi-2-naphthyl-2-N-butylcarbamate-2'-butyrate (S-3), 2, 2'-biphenyl-di-N-butylcarbamate (4), 2, 2'-biphenyl-2-N-octadecylcarbamate-2'-N-octylcarbamate (5), 2, 2'-biphenyl-2-N-octadecylcarbamate-2'-N-phenylcarbamate (6), 2, 2'-biphenyl-2-N-butylcarbamate-2'-butyrate (7), 2, 2'-biphenyl-2-N-butylcarbamate-2'-ol (8), 2, 2'-biphenyl-2-N-octylcarbamate-2'-ol (9), (R)-1, 1'-bi-2-N-naphthyl-2-butylcarbamate-2'-ol (R-10), and glyceryl-1,2, 3-tri-N-butylcarbamate (11) are prepared and evaluated for their inhibition effects on porcine pancreatic cholesterol esterase. All inhibitors are irreversible inhibitors of the enzyme. Carbamates 1-3 and 7-10 are the first alkyl chain and esteratic binding site-directed irreversible inhibitors due to the fact that the reactivity of the enzyme is protected by the irreversible inhibitor, trifluoroacetophenone in the presence of these carbamates. Carbamate 1 is the least potent inhibitor for the enzyme probably due to the fact that the inhibitor molecule adopts a linear conformation and one of the carbamyl groups of the inhibitor molecule covalently interacts with the first alkyl chain binding site of the enzyme while the other carbamyl group of the inhibitor molecule exposes outside the active site. With near orthogonal conformations at the pivot bond of biaryl groups, one carbamyl group of carbamates S-2, S-3, and R-10 covalently binds to the first alkyl chain binding site of the enzyme while the other carbamyl, butyryl, or hydroxy group can not bind covalently to the second alkyl chain binding site probably due to the orthogonal conformations. Carbamates 4-9 and 11 are very potent inhibitors for the enzyme probably due to the fact that all these molecules freely rotate at the pivot bond of the biphenyl or glyceryl group and therefore can fit well into the bent-shaped first and second alkyl chains binding sites of the enzyme. Although, carbamates 4-6 and 11 are irreversible inhibitors of cholesterol esterase, the enzyme is not protected but further inhibited by trifluoroacetophenone in the presence of these carbamates. Therefore, carbamates 4-6 and 11 covalently bind to the first alkyl chain binding site of the enzyme by one of the carbamyl groups and may also bind to the second alkyl chain binding site of the enzyme by the second carbamyl group. Besides the bent-shaped conformation, the inhibition by carbamate 6 is probably assisted by a favorable pi-pi interaction between Phe 324 at the second alkyl chain binding site of the enzyme and the phenyl group of the inhibitor molecule. For cholesterol esterase, carbamates 8-10 are more potent than carbamates S-2, 4, and 5 probably due to the fact that the inhibitor molecules interact with the second alkyl chain binding site of the enzyme through a hydrogen bond between the phenol hydroxy group of the inhibitor molecules and the His 435 residue in that site.

Binding Sites↗
PubMed1999

Arecoline cytotoxicity on human oral mucosal fibroblasts related to cellular thiol and esterase activities.

Betel quid (BQ) chewing is associated with an increased risk of oral submucous fibrosis (OSF) and oral cancer in India and many south-east Asian countries. Recently, we have shown that arecoline is cytotoxic to cultured human oral mucosal fibroblasts. This study investigated protective effects of various agents against the cytotoxicity of arecoline and its mechanisms. Arecoline, at concentrations of 0.2 and 0.4 mM, decreased the cell numbers by 38% and 63%, respectively. At a concentration of 2 mM, N-acetyl-L-cysteine [a glutathione (GSH) synthesis precursor] could prevent arecoline-induced cytotoxicity. The decrease in cell numbers was reduced to 17% relative to control. Extracellular addition of esterase at a concentration of 0.1 U/ml could almost completely protect the oral mucosal fibroblast (OMF) from arecoline-induced cytotoxicity. Arecoline is a muscarinic receptor agonist. However, atropine, a muscarinic receptor antagonist was unable to protect the cells from arecoline cytotoxicity at a concentration of 10 microM. Pretreatment of OMF with 50 microM buthionine sulfoximine (a cellular GSH synthesis inhibitor) or 0.5 mM diethylmaleate (a cellular GSH depleting agent) potentiated the cytotoxic effects of arecoline. These results indicate that cytotoxicity of arecoline on OMF is associated with cellular GSH levels and esterase activities. Factors that induce the GSH synthesis or esterase activity of oral mucosal cells can be used for future chemoprevention of BQ chewing-related lesions.

Acetylcysteine↗
PubMed2000

What distinguishes an esterase from a lipase: a novel structural approach.

Esterases and lipases both hydrolyse ester bonds. Whereas the lipases display high activity towards the aggregated state of its substrate, the esterases typically show highest activity towards the soluble state of its substrate. We have compared the amino acid sequence, the 3D-structure as well as the pH-dependent electrostatic signature of selected members of the two families, for which 3D-structural information is publicly available. Lipases display a statistically significant enhanced occurrence of non-polar residues close to the surface, clustering around the active-site. Lid opening appears to strengthen this pattern further. As we have proposed earlier the active site of lipases displays negative potential in the pH-range associated with their maximum activity, typically at pH values above 8. The esterases show a very similar pattern, however, at pH values around 6 correlated with their usually lower pH-activity optimum.

Amino Acid Sequence↗
PubMed2001

High-performance liquid chromatographic-fluorimetric assay of chymotrypsin-like esterase activity.

A sensitive and reproducible assay for the determination of chymotrypsin-like esterase activity is reported. This method is based on fluorimetric detection of a dansylated amino acid, 5-dimethylaminonaphthalene-1-sulfonyl-L-phenylalanine, enzymatically formed from the substrate 5-dimethylaminonaphthalene-1-sulfonyl-L-phenylalanine ethyl ester, after separation by high-performance liquid chromatography using a C18 reversed-phase column and isocratic elution. This method is sensitive enough to measure 5-dimethylaminonaphthalene-1-sulfonyl-L-phenylalanine at concentrations as low as 40 pmol/ml, yields highly reproducible results and requires less than 9.5 min per sample for quantitation. The optimum pH for chymotrypsin-like esterase activity was 7.7-8.3. The Km and Vmax values were, respectively 25 microM and 0.241 pmol/microg protein/h with the use of enzyme extract obtained from mouse kidney. The approximate molecular mass of this enzyme was estimated to be 67000 by gel filtration. Chymotrypsin-like esterase activity was strongly inhibited by N-tosyl-L-phenylalaline chloromethyl ketone. Among the mouse organs examined, the highest specific activity of the enzyme was found in lung. This new method would be useful for clarification of the physiological role of this enzyme.

Chromatography, Gel↗
PubMedDate not supplied

[Electrophoretic polymorphism of lactate, malate and glutamate dehydrogenases, acid phosphatase and esterases of Providencia alcalifaciens, P. stuartii and P. rustigianii].

The polymorphism of glutamate, lactate and malate dehydrogenases, of acid phosphatase and of esterases of 27 strains of Providencia alcalifaciens, 35 strains of P. stuartii and 17 strains of P. rustigianii was investigated by conventional electrophoresis in polyacrylamide agarose gel and by isoelectric focusing in thin-layer polyacrylamide gel. For each enzyme analysed, the three species were characterized by a distinct electrophoretic pattern. The number of allozymes detected by conventional electrophoresis was greater than that detected by isoelectric focusing. The use of these two techniques in parallel led to improved detection of polymorphism of esterase alpha beta from P. alcalifaciens. A two-dimensional profile obtained by plotting isoelectric points against electrophoretic mobilities for malate dehydrogenase, acid phosphatase and beta-A esterase showed a molecular relationship between the diverse allozymes and demonstrated their taxonomic values. Polymorphism varied considerably according to the enzyme and species analysed and was correlated with DNA heterogeneity. The strains of P. alcalifaciens exhibited the greatest enzyme polymorphism and were classified into two main zymotypes reflecting genetic divergence within this species, whereas the strains of P. stuartii were electrophoretically less variable.

Acid Phosphatase↗