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PubMed2003

Identification and characterization of a GDSL esterase gene located proximal to the swr quorum-sensing system of Serratia liquefaciens MG1.

Serratia liquefaciens MG1 employs the swr quorum-sensing system to control various functions, including production of extracellular enzymes and swarming motility. Here we report the sequencing of the swr flanking DNA regions. We identified a gene upstream of swrR and transcribed in the same direction, designated estA, which encodes an esterase that belongs to family II of lipolytic enzymes. EstA was heterologously expressed in Escherichia coli, and the substrate specificity of the enzyme was determined in crude extracts. With the aid of zymograms visualizing EstA on polyacrylamide gels and by the analysis of a transcriptional fusion of the estA promoter to the promoterless luxAB genes, we showed that expression of the esterase is not regulated by the swr quorum-sensing system. An estA mutant was generated and was found to exhibit growth defects on minimal medium containing Tween 20 or Tween 80 as the sole carbon source. Moreover, we show that the mutant produces greatly reduced amounts of N-acyl-homoserine lactone (AHL) signal molecules on Tween-containing medium compared with the wild type, suggesting that under certain growth conditions EstA may be important for providing the cell with precursors required for AHL biosynthesis.

Amino Acid Sequence↗
PubMed2004

Characterization and heterologous gene expression of a novel esterase from Lactobacillus casei CL96.

A novel esterase gene (estI) of Lactobacillus casei CL96 was localized on a 3.3-kb BamHI DNA fragment containing an open reading frame (ORF) of 1,800 bp. The ORF of estI was isolated by PCR and expressed in Escherichia coli, the methylotrophic bacterium Methylobacterium extorquens, and the methylotrophic yeast Pichia pastoris under the control of T7, methanol dehydrogenase (P(mxaF)), and alcohol oxidase (AOX1) promoters, respectively. The amino acid sequence of EstI indicated that the esterase is a novel member of the GHSMG family of lipolytic enzymes and that the enzyme contains a lipase-like catalytic triad, consisting of Ser325, Asp516, and His558. E. coli BL21(DE3)/pLysS containing estI expressed a novel 67.5-kDa protein corresponding to EstI in an N-terminal fusion with the S. tag peptide. The recombinant L. casei CL96 EstI protein was purified to electrophoretic homogeneity in a one-step affinity chromatography procedure on S-protein agarose. The optimum pH and temperature of the purified enzyme were 7.0 and 37 degrees C, respectively. Among the pNP (p-nitrophenyl) esters tested, the most selective substrate was pNP-caprylate (C(8)), with K(m) and k(cat) values of 14 +/- 1.08 microM and 1,245 +/- 42.3 S(-1), respectively.

Amino Acid Sequence↗
PubMed2006

Analysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure.

The three-dimensional (3D) structure of the hyperthermophilic esterase EstE1 was constructed by homology modeling using Archaeoglobus fulgidus esterase as a reference, and the thermostability-structure relationship was analyzed. Our results verified the predicted 3D structure of EstE1 and identified the ion pair networks and hydrophobic interactions that are critical determinants for the thermostability of EstE1.

Archaeoglobus fulgidus↗
PubMed1973

Extracellular esterases of group A streptococci.

Methods were devised to prepare and estimate quantitatively the extracellular esterases of group A streptococci (STE). Two types of esterase preparations were prepared, corresponding to Stock and Lynn's serotype I (STE I) and II (STE II). The former was prepared from Streptococcus pyogenes strain SS379 (group A, type 40), and the latter from S. pyogenes strain 69882 (group A, type 49). Effects of cupric acetate, sera of various animals, and rabbit antisera to STE I and II on the activities of STE were tested. Cupric acetate added in substrate solution inhibited the activities of STE according to the concentration of cupric acetate. Sera of various animals (calf, guinea pig, horse, sheep, and pig) stimulated the activities of STE and protected them from the inhibitory effect of cupric acetate. Among the sera of various animals, horse serum gave the most potent activating and protecting effect, and was the serum from which the effective factor (horse serum-activating factor, HAF) was extracted by precipitation with ammonium sulfate. STE I was not stimulated by serum or HAF as markedly as STE II, but both enzymes were protected likewise by serum or HAF from the inhibition of cupric acetate. Antibodies to STE I and II were prepared in rabbits. Their effects on STE resembled that of HAF, but differed from the latter in immunological specificity. Activities of STE were stimulated and protected more markedly by homologous antiserum than by heterologous antiserum or normal rabbit serum. Applying suitable conditions, we defined the potency of STE and differentiated antibodies to STE I and II and normal serum quantitatively.

Acetates↗
PubMed1973

Characterization of esterases produced by a ruminal bacterium identified as Butyrivibrio fibrisolvens.

An obligately anaerobic ruminal bacterial isolate was selected from 18 tributyrin-degrading isolates and identified as Butyrivibrio fibrisolvens strain 53. The culture in late exponential phase contained enzymes which could be released by sonic disruption. These enzymes degraded substrates at a rate in the order 1-naphthyl acetate (NA) > 1-naphthyl butyrate > 1-naphthyl propionate but did not degrade 1-naphthyl palmitate or 1-naphthyl phosphate. The enzymes on NA were neither stimulated nor inhibited by CoCl(2), MgCl(2), and MnCl (each varied from 10(-6) to 10(-4) M). CaCl at 10(-3) M stimulated esterase activity by 16%. Aliphatic substrates were hydrolyzed at a rate in the order triacetin > tributyrin > tripropionin, and ethyl acetate > ethyl formate. Similarly, aromatic fluorescein diesters were degraded at a rate in the order acetyl > propionyl > caproyl > butyryl > capryl > lauryl. Polyacrylamide gel electrophoretic zymograms indicated that the enzyme composite contained cathodally migrating bands. By column chromatography, these enzymes were separated into six NA-degrading fractions. Fraction V contained an esterase which had an optimal temperature of 39 C, a K(m) of 7.6 x 10(-4) on NA, and a molecular weight of about 66,000. This enzyme was inhibited by paraoxon (41%, 10(-4) M), eserine (17%, 10(-2) M), NaF (17%, 10(-2) M), and diisopropyl fluorophosphate (62%, 10(-4) M) but not by 1-naphthyl N-methyl carbamate at 8.4 x 10(-4) M.

Anaerobiosis↗
PubMed1982

Identification and localization of two membrane-bound esterases from Escherichia coli.

Hydrolytic activities of isolated membrane fractions of Escherichia coli against chromogenic substrates, p-nitrophenyl ester and beta-naphthyl ester derivatives of N-substituted amino acids, were investigated by spectrophotometric and electrophoretic methods. Although detergents were absolutely necessary for the solubilization of enzymes, the amount of solubilized activities was increased by adding salt, such as NaCl or KCl. Two esterases were identified and separated by PAGE and by chromatography of the solubilized proteins in the presence of detergent. One hydrolyzed the alanine derivatives preferentially, whereas the other was mainly active on phenylalanine derivatives. Only the first was inactivated by diisopropyl fluorophosphate, a serine hydrolase inhibitor. Whereas the chymotrypsin-like enzyme was equally distributed between the inner and the outer membrane, the alanine activity was only detected in the inner membrane. They were both resistant to extraction with high salt concentrations, indicating their integral association with membranes. A study of the accessibility of these enzymes to their substrate in membrane vesicles with known polarity suggests that both alanine and phenylalanine activities are localized near the external surface of the cytoplasmic (inner) membrane. However, the phenylalanine activity (chymotrypsin-like enzyme) appears to be deeply buried inside the outer membrane. Because of its insensitivity to diisopropyl fluorophosphate, this last esterase seems to be distinct from the previously isolated periplasmic endopeptidase, protease I, which is also a chymotrypsin-like enzyme.

Alanine↗
PubMed1985

Exocellular esterase and emulsan release from the cell surface of Acinetobacter calcoaceticus.

An esterase activity has been found, both in the cell-free growth medium and on the cell surface of the hydrocarbon-degrading Acinetobacter calcoaceticus RAG-1. The enzyme catalyzed the hydrolysis of acetyl and other acyl groups from triglycerides and aryl and alkyl esters. Emulsan, the extracellular heteropolysaccharide bioemulsifier produced by strain RAG-1, was also a substrate for the enzyme. Gel filtration showed that the cell-free enzyme was released from the cell surface either emulsan free or associated with the bioemulsifier. The partially purified enzyme was found to interact specifically with the esterified fully active emulsan, but not with the deesterified polymer. A role for esterase in emulsan release from the cell surface was indicated when the enzyme was preferentially depleted from the cell surface under conditions in which emulsan was not released. Such cells lost the capacity to release the biopolymer.

Acinetobacter↗
PubMed2002

prbA, a gene coding for an esterase hydrolyzing parabens in enterobacter cloacae and Enterobacter gergoviae strains.

The new gene prbA encodes an esterase responsible for the hydrolysis of the ester bond of parabens in Enterobacter cloacae strain EM. This gene is located on the chromosome of strain EM and was cloned by several PCR approaches. The prbA gene codes for an immature protein of 533 amino acids, the first 31 of which represent a proposed signal peptide yielding a mature protein of a putative molecular mass of 54.6 kDa. This enzyme presents analogies with other type B carboxylesterases, mainly of eukaryotic origin. The cloning and expression of the prbA gene in a strain of Escherichia coli previously unable to hydrolyze parabens resulted in the acquisition of a hydrolytic capacity comparable to the original activity of strain EM, along with an increased resistance of the transformed strain to methyl paraben. The presence of homologues of prbA was tested in additional ubiquitous bacteria, which may be causative factors in opportunistic infections, including Enterobacter gergoviae, Enterobacter aerogenes, Pseudomonas agglomerans, E. coli, Pseudomonas aeruginosa, and Burkholderia cepacia. Among the 41 total strains tested, 2 strains of E. gergoviae and 1 strain of Burkholderia cepacia were able to degrade almost completely 800 mg of methyl paraben liter(-1). Two strains of E. gergoviae, named G1 and G12, contained a gene that showed high homology to the prbA gene of E. cloacae and demonstrated comparable paraben esterase activities. The significant geographical distance between the locations of the isolated E. cloacae and E. gergoviae strains suggests the possibility of an efficient transfer mechanism of the prbA gene, conferring additional resistance to parabens in ubiquitous bacteria that represent a common source of opportunistic infections.

Amino Acid Sequence↗
PubMed1985

Laboratory evaluation of leukocyte esterase and nitrite tests for the detection of bacteriuria.

We compared the sensitivity, specificity, and predictive values of the 1-min leukocyte esterase test and the test for urinary nitrite alone and in combination as screening tests for bacteriuria in over 5,000 clinical urine specimens. The leukocyte esterase-nitrite combination had a sensitivity of 79.2%, a specificity of 81%, and a negative predictive value of a negative test of 94.5% for specimens with greater than or equal to 10(5) CFU/ml. Although the sensitivity of this test was too low to allow its use as the only screening test for bacteriuria, it may serve as a useful adjunct to culturing and other urine-processing systems in the microbiology laboratory.

Bacteriuria↗
PubMed1989

Detection of influenza C virus by using an in situ esterase assay.

A variety of chemically defined compounds were tested to characterize the substrate specificity of the influenza C virus esterase and to determine whether a substrate could be found that would be useful in an assay to detect the virus. Two new substrates, alpha-naphthyl acetate and alpha-naphthyl propionate, were identified; alpha-naphthyl acetate was employed to develop an assay specific for influenza type C virus in MDCK cells. The assay was sufficiently sensitive to detect esterase activity in a single cell and distinguished influenza C virus infections from those of types A and B viruses. Infected cells could be detected as early as 8 h postinfection, with maximal enzyme detection occurring at 24 h. Assay of influenza C virus in the chorioallantoic or amniotic fluid of infected eggs was performed by applying fluids directly onto nitrocellulose strips and then incubating with alpha-naphthyl acetate. Both the cellular and nitrocellulose-bound assays are rapid, inexpensive, and easy to perform, offering advantages for use in clinical laboratories.

Animals↗
PubMed1978

Esterase activity in Candida species.

The purpose of this investigation was to ascertain the lipolytic activities (specifically, esterase) of those species of Candida that are most commonly isolated from human infections. Eight species of Candida were surveyed for their ability to hydrolyze various polyoxyethylene sorbitan compounds (Tweens). Of the 64 isolates tested, each had activity for at least one of the substrates. Most of the isolates hydrolyzed Tweens 40, 60, and 85. In contrast, none hydrolyzed Tween 80. Only one species hydrolyzed Tween 20. The patterns of precipitation resulting from reactions of fatty acids hydrolyzed from Tweens 40, 60, and 85 with calcium ions in the media were also useful in distinguishing some of the species. In the past, such reactions have been reported as being dependent on esterase activity.

Candida↗
PubMed1982

A quantitative study of alpha-naphthyl acetate esterase-positive cells in non-Hodgkin's lymphomas and reactive lymph nodes.

The numbers of alpha-naphthyl acetate esterase (ANAE)-containing cells (other than T lymphocytes) in non-Hodgkin's lymphomas (NHL) and reactive lymph nodes have been counted, using the Reichert-Jung (Kontron) MOP-AMO3 user-controlled image analyzer. Twenty specimens of NHL and ten reactive nodes were examined. Cells were demonstrated by their content of acid alpha-naphthyl acetate esterase (ANAE) in fixed frozen sections. It was found that lymphomas of high-grade malignancy contained much larger numbers of ANAE-positive cells (10.8-20.5%) than those of low-grade malignancy (1.4-4.1%). The number of ANAE-positive cells (1.4-3.2%) in reactive lymph nodes was similar to that in low-grade NHL nodes.

Carboxylic Ester Hydrolases↗
PubMed1983

The possible role of juvenile hormone esterase in the regulation of juvenile hormone titre in the female cockroach Diploptera punctata.

Juvenile hormone (JH) degradation in vitro and in vivo was studied in the viviparous cockroach Diploptera punctata. In vitro studies with juvenile hormone esterase (JHE) and "general" or l-naphthyl acetate esterase (NAcE) revealed that diethyl-p-nitrophenylphosphate (paraoxon) inhibited both JHE and NAcE activity, but the latter was more sensitive and was completely inhibited at 0.1 mM. NAcE activity was resistant to inhibition with Triton X-100, whereas JHE activity in haemolymph of adult females was inhibited 100% at Triton X-100 concentration of 0.25%. Eighty percent inhibition of JHE activity in vivo was observed following injection of 0.2 microL Triton X-100. In contrast to the previously observed dose-dependant increase in JHE activity. NAcE activity did not increase following treatment of allatectomized females with the JH analogue ethyl-2E,4E-3,7,11-trimethyl-2,4-dodecadienoate (hydroprene). Hydroprene was not catabolized in haemolymph of D. punctata in vitro. The half-life of C16 JH (JH III) in the haemolymph, in vivo, was 1.65 h for day 5 females and 2 h for day 6 females.

Animals↗
PubMed2001

RAPD analysis, serotyping, and esterase typing indicate that the population of Listeria monocytogenes strains recovered from cheese and from patients with listeriosis in Belgium are different.

Populations of Listeria monocytogenes strains isolated in Belgium from cheese and from patients with listeriosis were characterised by randomly amplified polymorphic DNA (RAPD) analysis using two 10-mers primers (OPA-04 and OPA-13). High discrimination levels were obtained with each of these primers alone (discrimination indices (DI) of 0.899 and 0.935 for OPA13 and OPA04, respectively) or in combination (DI of 0.960). The clustering of strains obtained by RAPD was compared with a clustering previously made using serotyping and esterase typing. RAPD allowed the subdivision of each serovar cluster and of most of the clusters determined by the polymorphism of the bacterial esterases. Our analysis indicates that the population of strains of L. monocytogenes found in cheese differs from the one isolated from patients with listeriosis during the same period.

Belgium↗
PubMedDate not supplied

In situ detection of human monocyte/macrophage serine esterase-1 mRNA expression in human tissues.

Human monocyte/macrophage serine esterase (HMSE) can be distinguished from esterases of other blood cells by a specific isoelectric focusing pattern of five enzyme variants. Using a HMSE-1 cDNA, expression of mRNA was investigated by nonradioactive in situ hybridization of human biopsy specimens and cytospin preparations. HMSE-1 transcripts could be detected in the myelomonocytic cell line U-937, blood monocytes and in tissue macrophages. Immune accessory cells of the monocyte/macrophage lineage did not express detectable amounts of HMSE-1 mRNA. These results indicate that HMSE-1 represents a cell-lineage-specific enzyme which can be used to characterize physiological and neoplastic variants of the human monocyte/macrophage cell system. The method described will enable further insight into the physiological function of HMSE-1.

Blotting, Western↗
PubMed1986

Naphthol-AS-D-chloroacetate esterase activity in globule leucocytes in the tracheal epithelium of rats.

The enzyme naphthol-AS-D-chloroacetate esterase is histochemically demonstrated in the granules of globule leucocytes in the tracheal epithelium of rats. The enzyme reactivity may be used as a cytochemical marker of these cells. The previously postulated mast cell origin of globule leucocytes is doubted, and the possibility that globule leucocytes belong to the group of natural killer cells is discussed. The biological role of the located esterase and the function of the globule leucocytes are also briefly discussed.

Animals↗
PubMed1976

Human saliva esterases: genetic studies.

Esterases from human saliva have been demonstrated by the zymogram technique. Three phenotypes were found in region 1. Family and population studies suggested that these phenotypes are the products of an autosomal locus with two alleles, Set-1F and Set-1S. Region 1 esterases are carboxylesterases.

Alleles↗