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PubMed1980

I-Naphthyl acetate esterase isoenzymes in synovial fluids and radiography of temporomandibular and knee joints.

Esterase isoenzymes of synovial fluids were presented in cases of pain-dysfunction syndrome, osteoarthrosis, osteochondroma, malignant fibrous histiocytoma of temporomandibular joint, and hemarthrosis, rheumatoid arthritis of the knee joint. Radiographic features of them were also comparatively presented in several cases. The electrophoretogram of I-Naphthyl acetate esterase of pain-dysfunction syndrome showed the esterase-I, while when inflammatory process developed at joints, electrophoretic pattern of synovial fluids revealed a rather similar feature of sera with variable stainabilities of esterase-I, and -III, irrespective of any inflammation. Osteochondroma showed two components of esterase-I and -III, on the other hand malignant fibrous histiocytoma presented esterase-I and -III in the early stage but a more complicated pattern in recurrence. Among these conditions, the most similarity between synovial fluid and serum was demonstrated in the case of hemarthrosis on the electrophoretogram of I-Naphthyl acetate esterases.

Adult↗
PubMed2001

Purification and characterization of trans-permethrin metabolizing microsomal esterases from workers of the eastern subterranean termite, Reticulitermes flavipes (Kollar).

Three alpha-naphthyl acetate hydrolyzing esterase isozymes were purified from microsomes prepared from Reticulitermes flavipes workers. The two step process involved sequential preparative IEF followed by continuous elution preparative electrophoresis on a 5% non-denaturing polyacrylamide gel. The first IEF run resulted in 5.4-fold purification with a yield of 46.1%. Subsequent IEF further purified the esterases 14.3-fold and 12% yield. Preparative electrophoresis of the pooled IEF fractions produced three major peaks of alpha-naphthyl acetate hydrolyzing activity. The esterases were correspondingly designated microsomal esterase (ME) 1, ME 2, and ME 3 based on increasing molecular retention on a native PAGE gel. ME 1, ME 2, and ME 3 were acidic proteins with pI values of 4.61, 4.70, and 4.77, respectively. Molecular mass as determined by gel filtration chromatography of ME 1, ME 2, and ME 3 was 69, 64, and 62 kDa, respectively. SDS-PAGE gels produced a single band for each of the isozymes with a molecular mass of 63 kDa indicating that the esterases were monomers. Specific activities of ME 1, ME 2, and ME 3 increased with increasing pH and the enzymes were active over a broad temperature range (25-55 degrees C). The three purified isozymes were inhibited at low concentration by paraoxon (10(-10) M), chlorpyrifos (10(-6) M), DEF (10(-6) M), and PMSF (10(-6) M) indicating that they were "B" type serine esterases. Conversely, inhibition was not observed at 10(-4) M eserine, PHMB, or CaCl(2), further supporting the conclusion that the microsomal esterases were of the "B" type. None of the isozymes was inhibited by 10(-4) M imidacloprid, fipronil, or PBO. Quantitatively, ME 1, ME 2 and ME 3 metabolized t-permethrin at 21.8, 21.0, and 38.8 nmol/h/mg protein, representing a purification factor of 333-, 318-, and 591-fold over microsomes, respectively. The three isozymes produced the same type and number of t-permethrin metabolites.

Animals↗
PubMed2000

The atomic-resolution structure of a novel bacterial esterase.

BACKGROUND: A novel bacterial esterase that cleaves esters on halogenated cyclic compounds has been isolated from an Alcaligenes species. This esterase 713 is encoded by a 1062 base pair gene. The presence of a leader sequence of 27 amino acids suggests that this enzyme is exported from the cytosol. Esterase 713 has been over-expressed in Agrobacterium without this leader sequence. Its amino acid sequence shows no significant homology to any known protein sequence. RESULTS: The crystal structure of esterase 713 has been determined by multiple isomorphous replacement and refined to 1. 1 A resolution. The subunits of this dimeric enzyme comprise a single domain with an alpha/beta hydrolase fold. The catalytic triad has been identified as Ser206-His298-Glu230. The acidic residue of the catalytic triad (Glu230) is located on the beta6 strand of the alpha/beta hydrolase fold, whereas most other alpha/beta hydrolase enzymes have the acidic residue located on the beta7 strand. The oxyanion hole is formed by the mainchain nitrogens of Cys71 and Gln207 as identified by the binding of a substrate analogue, (S)-7-iodo-2,3,4,5-tetrahydro-4-methyl-3-oxo-1H-1, 4-benzodiazepine-2-acetic acid. Cys71 forms a disulphide bond with the neighbouring Cys72. CONCLUSIONS: Despite negligible sequence homology, esterase 713 has structural similarities to a number of other esterases and lipases. Residues of the oxyanion hole were confirmed by structural comparison with Rhizomucor miehei lipase. It is proposed that completion of a functional active site requires the formation of the disulphide bond between adjacent residues Cys71 and Cys72 on export of the esterase into the oxidising environment of the periplasmic space.

Alcaligenes↗
PubMed1986

Effects of diethylstilbestrol, 2,2'-dithiodipyridine, and chloral hydrate on the esterase activity of sheep liver cytoplasmic aldehyde dehydrogenase.

The binding of diethylstilbestrol (DES) to aldehyde dehydrogenase (ALDH) has a very similar effect on the dehydrogenase activity of the enzyme as has modification of the enzyme by 2,2'-dithiodipyridine [Kitson, T.M. (1982) Biochem. J. 207, 81-89]. The latter modification may occur at the site of the esterase activity of the enzyme [Kitson, T.M. (1985) Biochem. J. 228, 765-767]. This suggests that DES might be a competitive inhibitor of the esterase reaction. However, in the absence of oxidized nicotinamide adenine dinucleotide (NAD+) or reduced nicotinamide adenine dinucleotide (NADH), and at low concentrations of substrate (4-nitrophenyl acetate, PNPA), DES is a potent partial noncompetitive inhibitor. It is concluded therefore that DES binds at a site different from the esterase active site and that the enzyme-DES complex retains some ability to act as an esterase. High concentrations of PNPA appear to displace DES from its binding site. In the presence of NAD+, DES is a weaker inhibitor, and in the presence of NADH, DES has very little effect. Esterase activity is enhanced by NADH when PNPA concentrations are high but is inhibited when they are low. The rate of reaction of ALDH with 2,2'-dithiodipyridine is only slightly reduced by DES, suggesting that the site at which thiol modifiers react and the DES binding site are different. When ALDH is modified by 2,2'-dithiodipyridine, it has reduced esterase activity, which declines further as the modified enzyme loses its 2-thiopyridyl label. In the presence of NAD+, chloral hydrate is a simple competitive inhibitor of the esterase reaction.(ABSTRACT TRUNCATED AT 250 WORDS)

2,2'-Dipyridyl↗
PubMed2001

Differential esterase expression in leaves of Manihot esculenta Crantz infected with Xanthomonas axonopodis pv. manihotis.

The polyacrylamide gel electrophoresis system (PAGE) and inhibition tests for biochemical characterization of alpha- and beta-esterases were used to obtain a functional classification of esterases in plants and to show a differential expression of esterases as markers of pathogenesis in cassava plants (Manihot esculenta Crantz). The characterization of alpha- and beta-esterases from leaves of M. esculenta by the PAGE system was possible using an extraction solution containing two phenol-complexing agents (PVP-40 and sodium metabisulfite), three antioxidant agents (EDTA, beta-mercaptoethanol, and DTT), and one quinone reducer (ascorbic acid). Fourteen esterase isozymes were detected in young unexpanded leaves of M. esculenta cultivars. The inhibition pattern of alpha- and beta-esterases of M. esculenta showed that Est-9 is an arylesterase, and in the unexpanded leaves of the M. esculenta plants infected with Xanthomonas axonopodis pv. manihotis, the Est-7 beta-esterase showed the characteristic staining of an alpha/beta-esterase. This diffrential expression of Est-7 isozyme in young unexpanded leaves of cassava plants can be used as a marker of pathogenesis after infection with X. axonopodis pv. manihotis.

Electrophoresis, Polyacrylamide Gel↗
PubMed2002

Esterase patterns and phylogenetic relationships of Drosophila species in the saltans subgroup (saltans group).

The esterase patterns of sixteen strains from four species in the saltans subgroup were analyzed using polyacrylamide gel electrophoresis. Thirty-four esterase bands were detected. By using alpha and beta naphthyl acetates as substrates, they were classified in 18 alpha-esterases (they hydrolyse the alpha-naphtyl substrate), 15 beta-esterases (they hydrolyse the beta-naphtyl substrate) and 1 alpha/beta-esterase (it hydrolyses the alpha and beta-naphtyl substrates). Among the alpha-esterases, three were detected exclusively in males. Malathion, Eserine and pCMB were used as inhibitors in order to characterize biochemically the esterases. The results indicated the presence of cholinesterases, carboxylesterases and acetylesterases. The degree of mobility of the bands in the gels, their specificity to alpha and beta naphthyl acetates and the results of the inhibition tests allowed us to recognize tentatively nine genetic loci. Phylogenetic relationships among species inferred on the basis of the esterase patterns by PAUP 4.0b8, with neighbor-joining search and a bootstrap analysis showed that, although the four species are closely related, D. septentriosaltans, D. saltans and D. austrosaltans are closer to each other than to D. prosaltans. These results showed to be consistent with phylogenetic relationships previously inferred from inversion polymorphism.

Animals↗
PubMed1997

Isozyme polymorphism of esterases in the genus Lanistes (Mollusca:Prosobranchiata) and genetic analysis of populations.

Esterases from the digestive gland of the snails Lanistes carinatus and Lanistes bolteni collected from Egyptian governorates were extracted and analyzed using starch gel electrophoresis and five substrates. Twelve esterase bands were detected in both Lanistes species. The esterase bands were distributed in three main zones, which could be classified as acetylesterases, carboxylesterases, and cholinesterases. Depending on the substrates specificity, inhibition properties, and relative mobility of esterase bands, the three zones of esterase activity could be traced to eight genetic loci. Locality-specific loci were found. Inter- and intrapopulation variations are discussed. There is an absence of equilibria at all esterase loci in all populations studied, and a high proportion of genetic diversity in different esterase loci. The absence of interspecific variations proves that Lanistes snails in Egypt belong to one species.

Animals↗
PubMed1968

Purification and properties of esterases characteristic of adult rat brain.

1. A method for the partial purification of an esterase fraction, present in the brain of the adult but not the newborn rat, is described. A 54-fold purification was achieved in three steps. 2. When subjected to starch-gel electrophoresis, the purified fraction resolved into three bands of esterase activity. Two of these bands migrate close together and faster than other esterases in the brain. These two esterases are inhibited by p-hydroxymercuribenzoate but not by di-isopropyl phosphorofluoridate. The third band is di-isopropyl phosphorofluoridate-sensitive and migrates just behind the two leading esterases. 3. After treatment with di-isopropyl phosphorofluoridate, to obviate the effects of the di-isopropyl phosphorofluoridate-sensitive esterase, the enzyme preparation hydrolyses alpha-naphthyl acetate, alpha-naphthyl propionate and alpha-naphthyl butyrate, but not cholesteryl acetate. The V(max.) for the naphthyl esters decreased with increase in chain length of the acyl group. The acetate ester is hydrolysed 34 times as fast as the butyrate and about seven times as fast as the propionate derivative. The K(m) values for these three esters, measured at pH7.2 and 37 degrees , are 2.8x10(-4)m, 3.1x10(-4)m and 7.3x10(-5)m for the acetate, propionate and butyrate derivatives respectively. 4. The Hofstee (1952) plots for the kinetic data show a single line, indicating that the two most-rapidly migrating esterases, although electrophoretically separable, are not kinetically distinguishable in the substrate ranges examined.

Acetates↗
PubMed1971

Differences in distribution of esterase between cell fractions of rat liver homogenates prepared in various media. Relevance to the lysosomal location of the enzyme in the intact cell.

The distribution of esterase in subcellular fractions of rat liver homogenates was compared with that of the lysosomal enzyme acid phosphatase and the microsomal enzyme glucose 6-phosphatase. Most of the esterase from sucrose homogenate sediments with glucose 6-phosphatase and about 8% is recovered in the supernatant. However, up to 53% of the esterase can be washed from microtome sections of unfixed liver, in which less cellular damage would be expected than that caused by homogenization. About 40% of both esterase and acid phosphatase are recovered in the soluble fraction after homogenization in aqueous glycerol or in a two-phase system (Arcton 113-0.25m-sucrose), although glucose 6-phosphatase is still recovered in the microsomal fraction of such homogenates. The esterase of the microsomal fraction prepared from a sucrose homogenate is much more readily released by treatment with 0.26% deoxycholate than are other constituents of this fraction. The release of esterase from the microsomal fraction by the detergent and its concomitant release with acid phosphatase after homogenization in glycerol or the two-phase system suggests that a greater proportion of esterase may be present in lysosomes of the intact cell than is indicated by the results of standard fractionation procedures.

Acid Phosphatase↗
PubMed2007

An active site tyrosine residue is essential for amidohydrolase but not for esterase activity of a class 2 histone deacetylase-like bacterial enzyme.

HDACs (histone deacetylases) are considered to be among the most important enzymes that regulate gene expression in eukaryotic cells acting through deacetylation of epsilon-acetyl-lysine residues within the N-terminal tail of core histones. In addition, both eukaryotic HDACs as well as their bacterial counterparts were reported to also act on non-histone targets. However, we are still far from a comprehensive understanding of the biological activities of this ancient class of enzymes. In the present paper, we studied in more detail the esterase activity of HDACs, focussing on the HDAH (histone deacetylase-like amidohydrolase) from Bordetella/Alcaligenes strain FB188. This enzyme was classified as a class 2 HDAC based on sequence comparison as well as functional data. Using chromogenic and fluorogenic ester substrates we show that HDACs such as FB188 HDAH indeed have esterase activity that is comparable with those of known esterases. Similar results were obtained for human HDAC1, 3 and 8. Standard HDAC inhibitors were able to block both activities with similar IC(50) values. Interestingly, HDAC inhibitors such as suberoylanilide hydroxamic acid (SAHA) also showed inhibitory activity against porcine liver esterase and Pseudomonas fluorescens lipase. The esterase and the amidohydrolase activity of FB188 HDAH both appear to have the same substrate specificity concerning the acyl moiety. Interestingly, a Y312F mutation in the active site of HDAH obstructed amidohydrolase activity but significantly improved esterase activity, indicating subtle differences in the mechanism of both catalytic activities. Our results suggest that, in principle, HDACs may have other biological roles besides acting as protein deacetylases. Furthermore, data on HDAC inhibitors affecting known esterases indicate that these molecules, which are currently among the most promising drug candidates in cancer therapy, may have a broader target profile requiring further exploration.

Alcaligenes↗
PubMed1990

Purification and properties of an esterase from organophosphate-resistant strain of the mosquito Culex quinquefasciatus.

Organophosphate-resistant and -susceptible strains of Culex quinquefasciatus (mosquito) have been compared on the basis of their esterase activities. The homozygous resistant strain (Dar) shows two highly active esterases after starch-gel electrophoresis, of Rm 0.2 and 0.4, which are absent from susceptible strains (Apo, Mon), and which previous selection studies have shown to be inseparable from organophosphate resistance. After SDS/polyacrylamide-gel electrophoresis and silver staining of total C. quinquefasciatus proteins, a 62 kDa band is observed in strain Dar at high concentrations, and in susceptible strains in trace amounts. After Western blotting, this 62 kDa protein is recognized by antisera raised against the two esterases eluted from starch gels. After chromatofocusing of Dar proteins, the 62 kDa protein is seen to be associated with esterase activity, and of a similar pI to that observed for esterases after isoelectric focusing. Post-translational modification is not required for recognition of the 62 kDa putative esterase, since the protein is immunoprecipitated by the anti-esterase serum from products of translation of Dar mRNA in vitro.

Animals↗
PubMed1995

Calcium mobilization and protein kinase C activation are required for cholecystokinin stimulation of pancreatic cholesterol esterase secretion.

The bile salt-stimulated cholesterol esterase is a digestive enzyme synthesized by the acinar cells of the pancreas. Previous results have shown that cholesterol esterase biosynthesis and secretion in the AR42J pancreatoma cells could be increased 3-5-fold by intestinal hormones such as cholecystokinin (CCK). The purpose of the current study is to explore the signalling mechanism by which CCK stimulation of AR42J cells results in increased biosynthesis and secretion of the cholesterol esterase. The results showed that the CCK-induced cholesterol esterase secretion could be mimicked by addition of the Ca2+ ionophore A23187 or by transient incubation of AR42J cells with the protein kinase C activator phorbol 12-myristate 13-acetate (PMA). Cholesterol esterase stimulation by CCK, A23187 and PMA could be abolished by the calcium chelator BAPTA or by specific protein kinase C inhibitors such as chelerythrine. Additionally, prolonged incubation of AR42J cells with PMA to reduce the protein kinase C level, also reduced CCK-stimulated cholesterol esterase secretion to a level similar to that observed in control cells. Taken together, these data suggested that CCK activation of cholesterol esterase secretion may be mediated by a Ca(2+)-dependent protein kinase C pathway, requiring increases in calcium mobilization and activation of protein kinase C.

Animals↗
PubMed1985

Leukocyte esterase activity in the rapid detection of urinary tract and lower genital tract infections in obstetric patients.

Infections of the vagina and urinary tract are important problems for the obstetrician. Examination of the vaginal discharge and urine for the presence of leukocytes is an important part of the evaluation for vaginitis and urinary tract infections. Neutrophils contain several esterases that are not present in serum, urine, or vaginal secretions. These esterases are not influenced by bacteria, commonly used drugs, or variable compositions of urine or vaginal secretions. A prospective study was performed to assess the sensitivity and specificity of leukocyte esterase activity as measured by dipstick (Chemstrip 9, Biodynamics) for the prediction of vaginitis and urinary tract infections during pregnancy. Results were compared with those obtained from potassium hydroxide smears, wet preps, and urine cultures. The vaginal discharge and urine of 65 patients was tested for leukocyte esterase activity on their initial OB visit. Leukocyte esterase was 100% sensitive and 100% specific for detecting urinary tract infections. It was 100% sensitive and 90% specific for predicting vaginal infections. Trichomonas infections accounted for the positive leukocyte esterase results when the urine culture was negative. On the basis of this study we believe that leukocyte esterase activity is sufficiently sensitive and specific to permit use of this test as a rapid and inexpensive screening procedure for vaginitis and urinary tract infections.

Chlamydia Infections↗
PubMed1990

Characterization of amplification core and esterase B1 gene responsible for insecticide resistance in Culex.

Organophosphorus insecticide (OP) resistance in several Culex species is associated with increased esterase activity resulting from amplification of the corresponding structural gene. In Culex pipiens quinquefasciatus, high levels of OP resistance (approximately 800 times) are due to the esterase B1 gene, which is amplified at least 250-fold. This gene has now been sequenced, and the structure of the amplification unit (amplicon) encompassing the structural gene has been partially characterized. The inferred amino acid sequence of the enzyme revealed regions of strong homology with other eukaryotic serine-esterases, such as cholinesterases, which are the target of OPs. The amplicon covers at least 30 kilobases and contains a constant and highly conserved "core" of 25 kilobases. This core carries a single copy of the esterase gene (2.8 kilobases) as well as other sequences that are present as single or low number copies in the genomes of mosquitoes lacking overproduction of the esterase B1 protein. In the amplicon, the esterase gene is framed by two DNA sequences that are repeated in other parts of the genome of resistant mosquitoes and found in the genome of susceptible mosquitoes but not near the esterase B1 gene. It is suggested that these repetitive sequences may have a role in the amplification process.

Amino Acid Sequence↗
PubMed2004

Mode of inheritance of the polymorphic esterases in Myzus persicae (Hemiptera: Aphididae) in Japan.

Crossing experiments were conducted with 43 different parental clones of Myzus persicae (Sulzer) to clarify the genetic bases of esterase variations detected by electrophoresis. A total of 468 F1 clones obtained were analysed for variants at six polymorphic esterase loci, including one associated with resistance to organophosphorus insecticides (RAE). In addition, the effect of six different host plants on the activity of esterases was examined. The inheritance of variants at two loci could be explained by two-allele models, and that at three other loci by three-allele models, while segregation ratios at the RAE locus suggested a cumulative effect of the multiple genes. An interdependent assortment was found between two loci. The activity of the esterases detected in the alimentary canal was affected by the host plant. By combining the variants at the six polymorphic esterase loci with those in body colour, a total of 2592 colour-esterase forms were distinguishable. Thus esterases could be useful as genetic markers to study the genotypic composition and its dynamics of M. persicae populations.

Animals↗
PubMed1978

Electrophoretic properties of esterases in chronic granulocytic leukemia.

Granulocytes were obtained from samples of peripheral blood of five patients who had untreated chronic granulocytic leukemia, and polymorphonuclear leukocytes were isolated from peripheral blood of three normal persons. Specific and nonspecific esterases were extracted from leukocyte preparations with cetyltrimethylammonium bromide and with lysolecithin, and subjected to polyacrylamide disk electrophoresis. In samples from both patients and normal persons, electrophoretic patterns of nonspecific esterase activity using alpha-naphthyl acetate and alpha-naphthyl butyrate were similar, and the esterase bands were weakly inhibited by fluoride. Lysolecithin extracts of specific esterase showed similar electrophoretic patterns for patients and normal subjects. However in cetyltrimethylammonium bromide extracts of specific esterase, 11 bands were seen in preparations from all of the patients with chronic granulocytic leukemia. In preparations of normal polymorphonuclear leukocytes, only eight bands were visualized. The results are consistent with an interpretation that these fast-moving components of specific esterase in chronic granulocytic leukemia granulocytes are present in normal polymorphonuclear leukocytes, but in quantities too small to be visualized with the technics used. Alternatively, the apparent "additional" bands of specific esterase may reflect abnormal metabolism of malignant granulocytes in chronic granulocytic leukemia.

Chronic Disease↗
PubMed1990

Production of null mutants in the major intestinal esterase gene (ges-1) of the nematode Caenorhabditis elegans.

The ges-1 gene of the nematode Caenorhabditis elegans codes for a nonspecific carboxylesterase that is expressed only in the intestinal lineage. This esterase has turned out to be a convenient biochemical marker for lineage-specific differentiation. In the present paper, we describe the production of several C. elegans strains that lack detectable activity of the ges-1 esterase. To isolate these ges-1 null strains, we first produced a strain of hermaphrodites in which the wild-type copy of the ges-1 gene was stably balanced over a previously isolated isoelectric focusing allele, ges-1(ca6); this parental strain was then mutagenized with EMS and isoelectric focusing gels were used to identify progeny populations that lacked either ges-1(+) or ges-1(ca6) esterase activity. This method is a straightforward and general approach to obtaining null mutations in any gene that has a biochemical or immunological assay. The ges-1 gene is not essential to worm survival, development or reproduction. Furthermore, lack of the ges-1 product has no obvious effect on the ability of worms (containing either normal or greatly reduced levels of acetylcholinesterases) to survive exposure to esterase inhibitors. The ges-1 gene product provides roughly half of the total esterase activity measured in crude extracts of L1 larvae or mixed worm populations. However, histochemical staining of individual ges-1(0) embryos shows that the ges-1 esterase is the first and essentially the only esterase to be produced during embryonic development, from the midproliferation phase up to at least the twofold stage of morphogenesis. These ges-1(0) strains now allow us to investigate the developmental control of the ges-1 gene by DNA-mediated transformation, in which the ges-1 gene acts as its own reporter.

Animals↗
PubMed1976

Comparative autosomal linkage in mammals: genetics of esterases in Mus musculus and Rattus norvegicus.

Recombination between Esterase-4 and Esterase-2 in the rat was not observed in 278 backcross offspring. Es-4 is thus included within the "esterase cluster" in Linkage group V. A new map of this region was constructed and the relationship of the four esterase loci was found to be: Es-4-(9.6+/-1.6 cM)-Es-2, Es-4-(1.5+/-0.7cM)-Es-3. Homology of this region with a region of Linkage Group XVIII (Chromosome 8) of the mouse was proposed on the basis of tissue distribution, subcellular localization and response of enzymes to inhibiotrs. Specifically, rat Es-1 was suggested as the homolog of mouse Es-6. An autosomal segment comprising at least 15cM of the rat and mouse genomes appears to have remained relatively intact with respect to genetic content during rodent speciation. In addition, a new polymorphism for mouse esterase was described. The locus was designated Esterase-10 (Es-10) and proposed as the mouse homolog of human Esterase D. Linkage of Es-10 with nucleoside phosphorylase-1-(Np-1) on Chromosome 14 was established.

Alleles↗