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PubMed1998

Biochemical properties of staphylococcal (phospho)lipases.

Various staphylococci secrete lipases which require calcium ions for activity, and have profound preferences for substrates with different chain lengths. The lipase from Staphylococcus hyicus is exceptional since it has higher phospholipase than lipase activity. This paper gives an overview of the biochemical properties of these enzymes. It appears that chain length selectivity of these enzymes resides in the acylation step. Interfaces mainly influence the acylation step. Calcium ions do not influence the rate of acylation or deacylation although stabilise the enzyme against denaturation. Molecular modelling based on the X-ray structure of Pseudomonas glumae lipase was used to construct a model of the staphylococcal lipases. With this model the position of serveral residues involved in stubstrate selectivity was predicted. Moreover, a sequence element could be assigned that may function as the so-called lid domain in staphylococcal lipases. Sequence alignment of four staphylococcal lipases, and lipases from P. glumae and Bacillus thermocatenulatus identified several potential calcium ligands, one of which was verified by site directed mutagensesis. It is concluded that stabilisation of lipases by calcium ions might be a more general phenomenon than recognized so far.

Amino Acid Sequence↗
PubMed2000

Thermal stability of Rhizopus niveus lipase expressed in a kex2 mutant yeast.

Lipase from Rhizopus niveus (RNL) has a complex structure, and recombinant RNL, has even more complex structural properties in the yeast, Saccharomyces cerevisiae. These properties are due to the processing and to the size of the glycosylated sugar chain. The processing site was presumed to be that for the proteinase product of the KEX2 gene in yeast. We therefore, constructed an expression system in which the KEX2 gene was disrupted to produce a non-processed type of lipase with high thermal stability. This type of lipase was thermally stable to a temperature 15 degrees C higher than that of each processed type of lipase. This non-processed lipase had 50% residual activity after 2 h at 50 degrees C, while the residual activity of the processed lipases was only 10% after 30-45 min of incubation at 50 degrees C. The CD spectrum of the non-processed type of lipase at 222 nm was almost unchanged by heating, suggesting that this group of lipases had a very rigid structure and that the peptide bond between the A- and B-chain contributed to maintain this rigid structure. On the other hand, the length of the sugar chain bound to the lipase had no effect on the thermal stability.

Enzyme Stability↗
PubMed2003

Binding of phage displayed Bacillus subtilis lipase A to a phosphonate suicide inhibitor.

Phage display can be used as a protein engineering tool to select proteins with desirable binding properties from a library of randomly constructed mutants. Here, we describe the development of this method for the directed evolution of Bacillus subtilis lipase A, an enzyme that has marked properties for the preparation of pharmaceutically relevant chiral compounds. The lipase gene was cloned upstream of the phage g3p encoding sequence and downstream of a modified g3p signal sequence. Consequently, the enzyme was displayed at the surface of bacteriophage fd as a fusion to its minor coat protein g3p. The phage-bound lipase was correctly folded and fully enzymatically active as determined from the hydrolysis of p-nitrophenylcaprylate with K(m)-values of 0.38 and 0.33 mM for the phage displayed and soluble lipase, respectively. Both soluble lipase and lipase expressed on bacteriophages reacted covalently with a phosphonate suicide inhibitor. The phage does not hamper lipase binding, since both soluble and phage-bound lipase have a similar half-life of inactivation of approximately 5 min. Therefore, we conclude that the Bacillus lipase can be functionally expressed on bacteriophages as a fusion to the phage coat protein g3p. The specific interaction with the suicide inhibitor offers a fast and reproducible method for the future selection of mutant enzymes with an enantioselectivity towards new substrates.

Bacillus Phages↗
PubMed1997

In vivo and in vitro studies on the stereoselective hydrolysis of tri- and diglycerides by gastric and pancreatic lipases.

The stereoselectivity of dog gastric and dog pancreatic lipases was investigated both in vitro, under simulated physiological conditions, and in vivo, during the digestion of a liquid test meal. In vitro it was observed that although both lipases had a stereopreference for the sn-3 position in triglycerides, it was about three times higher in the case of the gastric lipase. On the other hand, both lipases clearly showed a comparable enantioselectivity for the sn-1 position when a racemic diolein was used as the substrate. In the case of pancreatic lipase, the enantiomeric excess of 1,2-sn-diolein generated in vitro by the hydrolysis of triolein was found to decrease significantly, and even to be slightly reversed, at high rates of hydrolysis (above 50%) due to the further stereoselective hydrolysis of diglycerides into monoglycerides. This finding may explain the low enantiomeric excess of the diglycerides observed in vivo during the early phase of intraduodenal digestion when pancreatic lipase plays a predominant role and the rate of triolein hydrolysis is already high. On the other hand, a large enantiomeric excess of 1,2-sn-diolein generated from triolein was always the fingerprint of the gastric lipase in vitro even at high hydrolysis rates. This fingerprinting of gastric lipase was observed during both the intragastric phase and the late intestinal phase of lipolysis. This feature was therefore taken as an index to determine the respective roles of gastric and pancreatic lipases during in vivo lipolysis. To the best of our knowledge, this is the first time that stereoselectivity has been used as a tool to discriminate between the activities of two enzymes hydrolyzing the same substrate in vivo.

Animals↗
PubMed2003

Highly sensitive active-site titration of lipase in microscale culture media using fluorescent organophosphorus ester.

The fluorescent organophosphorus esters, diethyl 4-methylumbelliferyl phosphate (1), ethyl hexyl 4-methylumbelliferyl phosphate (2) and ethyl 4-methylumbelliferyl heptylphosphonate (3) have been synthesized and evaluated as a sensitive active-site titrant of lipase. The phosphorus esters 1, 2 and 3 inactivated the lipase from Pseudomonas aeruginosa (LPL-312) with a second-order rate constant for enzyme inactivation (k(on)) of 1.8, 32 and 5600 s(-1) M(-1), respectively. The long-chain phosphonate 3 turned out to be the most potent inactivator of the lipase to release a stoichiometric amount of highly fluorescent 4-methylumbelliferone (4MU) as a leaving group. By using the phosphate 3 as an active-site titrant, the low concentration (4.5 nM) of the active lipase was titrated successfully. The highly sensitive active-site titration with 3 enabled the direct determination of the concentration of the active lipase expressed in a microscale culture medium. Although the expression level differed significantly from one culture to another, the titrated concentration of the active lipase was proportional to the apparent activity for all the independent cultures. The molecular activity calculated for the expressed lipase was found to be the same as that of the purified lipase. The present active-site titration method is widely applicable to the biocatalytic engineering of lipases such as directed evolution, site-directed mutagenesis, chemical modification and immobilization.

Binding Sites↗
PubMed1994

Diacylglycerol hydrolysis to arachidonic acid is necessary for insulin secretion from isolated pancreatic islets: sequential actions of diacylglycerol and monoacylglycerol lipases.

Arachidonic acid has been implicated as a second messenger in insulin secretion on the basis of (1) mobilization of intracellular Ca2+ from the endoplasmic reticulum of islets and (2) amplification of voltage-dependent Ca2+ entry. The insulin secretagogues D-glucose and the muscarinic agonist carbachol both increase unesterified arachidonic acid accumulation in isolated islets. We now show that diacylglycerol, a product of phospholipase C action, is a major source of free arachidonic acid in islets. Diacylglycerol hydrolysis in islets occurs through a two-step process. In the first step, the sn-1 bond of 1-stearoyl-2-arachidonyl-sn-glycerol is hydrolyzed by a diacylglycerol lipase, giving rise to 2-arachidonyl-sn-glycerol. Next, the sn-2 bond of 2-arachidonyl-sn-glycerol is hydrolyzed by a monoacylglycerol lipase, which is the rate-limiting step, releasing unesterified arachidonic acid. Both diacylglycerol lipase and monoacylglycerol lipase are highly enriched in the plasma membrane of beta-cells. Diacylglycerol lipase activity in islet homogenates is selectively inhibited in a dose-dependent manner by the compound RHC-80267, a specific diacylglycerol lipase inhibitor. RHC-80267 inhibits glucose- and carbachol-induced insulin release from intact islets in a dose-dependent manner that parallels its inhibition of diacylglycerol lipase activity. Importantly, RHC-80267, at concentrations that almost completely inhibit diacylglycerol lipase activity and glucose- and carbachol-induced insulin secretion by islets, markedly inhibits glucose- and carbachol-induced increases in islet arachidonic acid levels, as measured by gas chromatography with electron-capture detection of its pentafluorobenzyl esters. RHC-80267 did not significantly affect islet glucose oxidation, phospholipase C, monoacylglycerol lipase, or phospholipase A2. Since glucose and carbachol are known to stimulate phospholipase C, our observations indicate that diacylglycerol is an important source of arachidonic acid and other free fatty acids in islets. Furthermore, production of arachidonic acid from the hydrolysis of diacylglycerol is essential for glucose- and carbachol-induced insulin secretion.

Animals↗
PubMed1991

Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum.

The Ser-His-Asp triad is a well known structural feature of the serine proteases. It has also been directly observed in the catalytic sites of two lipases, whose high-resolution three-dimensional structures have been determined 1,2. Lipases show a wide variety of sizes, substrate and positional specificities, and catalytic rates 3. They achieve maximal catalytic rates at oil-water interfaces. The fungus Geotrichum candidum produces several different forms of lipases, two of which have been purified to homogeneity 4,5. Two lipase genes have been identified, cloned and sequenced 6,7. Both code for proteins of 544 amino acids with a total relative molecular mass of about 60,000 (Mr 60K). The two forms are 86% identical. Their isoelectric points differ slightly, being between 4.3 and 4.6. About 7% of the total Mr is carbohydrate. Until now, only a low resolution structure of GCL has been reported 8, but no high resolution structure has followed. We now report the three-dimensional structure of a lipase from G. candidum (GCL) at 2.2 A resolution. Unlike the other lipases and serine proteases, the catalytic triad of GCL is Ser-His-Glu, with glutamic acid replacing the usual aspartate. Although the sequence similarity with the other two lipases is limited to the region near the active-site serine, there is some similarity in their three-dimensional structures. The GCL is also an alpha/beta protein with a central mixed beta sheet whose topology is similar to that of the N-terminal domain of human pancreatic lipase. As in the other lipases 1,2, the catalytic site is buried under surface loops. Sequence comparisons with proteins from the cholinesterase family suggest that they also contain the Ser-His-Glu triad.

Amino Acid Sequence↗
PubMed2000

Stimulation of hormone-sensitive lipase activity by contractions in rat skeletal muscle.

Because the enzymic regulation of muscle triglyceride breakdown is poorly understood we studied whether neutral lipase in skeletal muscle is activated by contractions. Incubated soleus muscles from 70 g rats were electrically stimulated for 60 min. Neutral lipase activity against triacylglycerol increased after 1 and 5 min of contractions [0.36 +/- 0.02 (basal) versus 0.49 +/- 0.05 (1 min) and 0.54 +/- 0.05 (5 min) m-unit.mg of protein(-1), means +/- S.E.M., P < 0.05]. After 10 min the neutral lipase activity (0.40 +/- 0.05 m-unit.mg of protein(-1)) had decreased to basal values (P > 0.05). The contraction-mediated increase in lipase activity was increased by approximately 110% when muscle was stimulated in the presence of okadaic acid. Conversely, treatment of muscle homogenate with alkaline phosphatase completely reversed the contraction-mediated lipase activation. Lipase activity did not change during contractions when analysed in the presence of anti-hormone-sensitive-lipase (HSL) antibody [0.17 +/- 0.02 (basal) versus 0.21 +/- 0.02 (5 min) m-unit.mg of protein(-1), P > 0.05]. Furthermore, immunoprecipitation with affinity-purified anti-HSL antibody reduced muscle-HSL protein concentration by 81+/-4% and caused similar reductions in lipase activity against triacylglycerol and in the contraction-induced increase in this activity. Neither prior sympathectomy [0.33+/- 0.02 (basal) versus 0.53 +/- 0.06 (5 min) m-unit.mg of protein(-1), P < 0.05] nor propranolol impaired the lipase response to contractions. Glycogen phosphorylase activity in the absence of AMP increased after 1 min [27.3 +/- 3.1 versus 8.9 +/- 1.8% (activity without AMP/total activity with AMP), P < 0.05] and returned to basal levels after 5 min. In conclusion, skeletal-muscle-immunoreactive HSL is transiently stimulated by contractions and the mechanism probably involves phosphorylation. The time course of HSL activation is similar to that of glycogen phosphorylase. Apparently, the two enzymes are regulated in parallel by contraction-induced as well as hormonal mechanisms, allowing simultaneous recruitment of all major extra- and intra-muscular energy stores.

Adenosine Monophosphate↗
PubMed1975

[Serum lipase activity and endoscopic retrograde pancreatography in chronic pancreatitis and pancreatic neoplasm (author's transl)].

Serum lipase activity was measured in 360 patients with the clinical suspicion of chronic pancreatic disease, 60 of them also having the lipase evocation test (serum lipase activity before and after pancreatic stimulation with secretin and pancreozymin). Of 48 with chronic pancreatitis (40 confirmed at operation) the diagnosis was made by endoscopic retrograde pancretography in all but one. Serum lipase activity was abnormal in 38. Without those cases associated with pancreatic insufficency, serum lipase activity-spontaneously and after the evocation test-was abnormal in 46 patients. Nine of 10 patients with papillary stenosis had the diagnosis confirmed at surgery, the pancretographic findings co-inciding with the surgical ones in all instances. All the five patients with abnormally high serum lipase activity also had chronic pancreatitis on pancreatography. In all of the 18 patients with pancreatic neoplasm pancreatography gave the same results as operation or post-mortem findings. In eight of these serum lipase activity was spontaneously elevated. The lipase evocation test was shown to be most effective if 2 C.H.R.- U/KG-h each of pancreozymin and secretin were administered. Serum lipase results were falsely positive in 17 of 300 patients with clinical suspicion of pancreatic disease but normal pancreatographic findings.

Adult↗
PubMed1991

Lipoprotein lipase enhances the binding of chylomicrons to low density lipoprotein receptor-related protein.

Chylomicron catabolism is known to be initiated by the enzyme lipoprotein lipase (triacylglycero-protein acylhydrolase, EC 3.1.1.34). Chylomicron remnants, produced by lipolysis, are rapidly taken up by the liver via an apolipoprotein E (apoE)-mediated, receptor-dependent process. The low density lipoprotein (LDL) receptor-related protein (LRP) has been suggested as the potential apoE receptor. We have analyzed the binding of human chylomicrons to HepG2 cells in the absence and presence of lipoprotein lipase. Bovine and human lipoprotein lipases were able to increase the specific binding of the chylomicrons by up to 30-fold. This effect was not dependent on lipolysis but appeared to be due to the lipase protein itself. It was not found when a structurally unrelated, bacterial lipase was used. Using beta-migrating very low density lipoproteins (beta-VLDLs), known as a good ligand for LRP, binding studies were performed on LDL receptor-negative human fibroblasts. The binding was increased 40-fold by addition of lipoprotein lipase. Crosslinking experiments on cells with 125I-labeled apoE liposomes or lipoprotein lipase showed that both proteins were able to bind to LRP on the cell surface. The binding of apoE to LRP was highly increased by the addition of lipase. We conclude that lipoprotein lipase strongly enhances the binding of apoE-containing lipoproteins to LRP and therefore might play an important role in chylomicron catabolism not only because of its lipolytic activity but also because of its structural properties.

Apolipoproteins E↗
PubMed2000

Cephalic phase of lipolysis is impaired in pancreatic insufficiency: role of gastric lipase.

BACKGROUND: Gastric lipase contributes significantly to overall lipolysis and is regulated by interacting neuro-hormonal mechanisms. Patients with alcoholic chronic pancreatitis (ACP) have low, or even absent, activity of pancreatic lipases. In that state the secretion of gastric lipase could be essential and compensate for the pancreatic defect. However, conflicting studies have not resolved the order of magnitude of gastric lipase secretion in these patients. This could be explained by differences in regulatory mechanisms, gastric mucosal changes, and abdominal vagal tone. METHODS: Nasogastric intubation with modified sham feeding and upper endoscopy including biopsies for histologic classification and Helicobacter pylori infection status were performed in eight ACP patients, and eight healthy volunteers were studied on separate occasions. Vagal nerve function was assessed by calculation of heart rate variability in ACP patients. Gastric lipase was measured in aspirates by means of enzyme-linked immunosorbent assay and an enzyme kinetic assay. Plasma concentrations of gastrin, secretin, cholecystokinin, and pancreatic polypeptide were measured throughout the study. RESULTS: Sham feeding rapidly and significantly increased gastric lipase secretion in healthy volunteers, whereas ACP patients did not respond to sham feeding. Two of eight patients were infected with H. pylori and had mucosal changes accordingly. The lack of lipase response could not be ascribed to dysfunction of the abdominal vagus. CONCLUSIONS: The cephalic phase of gastric lipase secretion is impaired in ACP patients. Although their fundic cells continue to secrete gastric lipase, they are not subject to normal neuro-hormonal regulation.

Adult↗
PubMed2004

Preparation and properties of lipases immobilized on different supports.

Porcine pancreatic lipase and Candida cylindracea lipase were immobilized on Celite and Amberlite IRA-938. Activities and stabilities of immobilized lipases were investigated. The immobilized lipase derivatives on Celite exhibited grater residual activity and more resistance to thermal inactivation than their immobilized counterpart on Amberlite IRA-938. The apparent optimum temperatures of the immobilized lipases were 7-10 degrees C higher than that of the free enzymes. The native lipase and lipases immobilized on Celite showed same behaviors of pH dependence. But the pH optimum values for lipases immobilized on Amberlite IRA-938 were shifted to the acidic region relative to that of free enzymes. The stabilities of free and immobilized lipases were also investigated.

Animals↗
PubMed1995

Investigations into the actions of glucose-dependent insulinotropic polypeptide and glucagon-like peptide-1(7-36)amide on lipoprotein lipase activity in explants of rat adipose tissue.

The direct actions of glucose-dependent insulinotropic polypeptide, glucagon-like peptide-1(7-36)amide and insulin on lipoprotein lipase activity in explants of rat epididymal adipose tissues were investigated. Lipoprotein lipase was extracted into the incubation medium by heparin release of lipoprotein lipase and measured by fatty acid release from a glyceroltriolein emulsion. Insulin and glucose-dependent insulinotropic polypeptide caused a significant stimulation of lipoprotein lipase activity over a dose range of 0.25-4 nmol/L and 4-8 nmol/L, respectively. Explants incubated in the presence of both insulin and glucose-dependent insulinotropic polypeptide (at 0.5 and 4 nmol/L, respectively) showed levels of lipoprotein lipase activity significantly greater than that seen with either hormone alone. Neither insulin- nor glucose-dependent insulinotropic polypeptide-stimulated lipoprotein lipase was modified by the presence of the antibiotic actinomycin-D in the incubation medium, indicating that these two hormones exert their actions on the pre-existing cellular pool of lipoprotein lipase. Glucagon-like polypeptide-1(7-36)amide, over a dose range of 1-8 nmol/L, did not stimulate lipoprotein lipase activity. This study indicates that glucose-dependent insulinotropic polypeptide, in addition to stimulating insulin secretion, has a direct biological action on adipose tissue and in vivo, together with insulin, may promote lipoprotein lipase activity postprandially.

Adipose Tissue↗
PubMed1998

C-terminal peptide of fusarium heterosporum lipase is necessary for its increasing thermostability.

Saccharomyces cerevisiae bearing a lipase cDNA from Fusarium heterosporum produced two lipases, A and B. Lipase B was significantly more stable to temperature than lipase A, but their optimum temperatures were similar. Lipase B was composed of one polypeptide (301 amino acids), and lipase A was composed of two polypeptides (275 and 26 amino acids) generated by the cleavage between Arg275 and Asp276 with a trypsin-like protease. It was suggested that the C-terminal peptide (26 amino acids) tightened the lipase structure when bound to the catalytic domain (275 amino acids) through a peptide bond. The tight structure was loosened by cleavage of the C-terminal peptide, even though the peptide interacted noncovalently with the catalytic domain, possibly through charged amino acids, in which it is rich. Deletion of the C-terminal peptide greatly decreased the lipase production by the recombinant S. cerevisiae, although its transcriptional level was the same as that of cells carrying the wild-type gene. These facts suggested that the C-terminal peptide affected the lipase production in the post-transcriptional step.

Amino Acid Sequence↗
PubMed1990

cDNA cloning and characterization of Geotrichum candidum lipase II.

Geotrichum candidum produces two extracellular lipases, I and II. A lipase II cDNA clone was isolated from a cDNA library by colony hybridization using the 32P-labeled fragment of lipase I cDNA isolated previously. The nucleotide sequence of lipase II cDNA determined by the dideoxy chain terminating method includes the N- and C-terminal amino acid sequences of lipase II, and the overall amino acid composition deduced from the cDNA coincides with that deduced on amino acid analysis of this protein. The cloned lipase II cDNA codes a protein of 544 amino acids and a part of the signal sequence of 13 amino acids. The peptide chain lengths of lipases I and II are the same, their overall identity being 84%. Furthermore, four Cys residues are completely conserved, which may participate in the formation of disulfide bridges. A homology search indicated that the G. candidum lipases and Candida cyclindracea lipase are homologous enzymes and that they are members of the cholinesterase family.

Amino Acid Sequence↗
PubMed1981

Reversibility of the modification of Rhizopus delemar lipases by phosphatidylcholine.

Rhizopus (Rh.) delemar (ATCC 34612) lipase is modified by its binding with phosphatidylcholine (PC); such binding enhances the lipoprotein lipase (LPL) activity, shifts the isoelectric point (pI) to the acidic side and decreases its alpha-helical content ((1980) J. Biochem. 88, 533-538). The results of density gradient ultracentrifugation proved that PC binding to lipase molecule was depleted by the treatment of PC-bound lipase with 0.3% Triton X-100 and 0.1 M NaCl. By this treatment, LPL activity was decreased almost to the original activity. At the same time, alpha-helical content recovered to that of the original lipase and the isoelectric point recovered from pI 6.5 to nearly the pI of the original lipase. These data indicate that the modification of Rh. lipase by PC is reversible. Furthermore, the results of an experiment with 2-[1(-14) C]oleoyl PC showed that lipase having high LPL activity contained about 5 mol of PC per mol of lipase.

Isoelectric Point↗
PubMed1994

The structure-function relationship of the lipases from Pseudomonas aeruginosa and Bacillus subtilis.

Within the BRIDGE T-project on lipases we investigate the structure-function relationships of the lipases from Bacillus subtilis and Pseudomonas aeruginosa. Construction of an overproducing Bacillus strain allowed the purification of > 100 mg lipase from 30 l culture supernatant. After testing a large variety of crystallization conditions, the Bacillus lipase gave crystals of reasonable quality in PEG-4000 (38-45%), Na2SO4 and octyl-beta-glucoside at 22 degrees C, pH 9.0. A 2.5 A dataset has been obtained which is complete from 15 to 2.5 A resolution. P.aeruginosa wild-type strain PAC1R was fermented using conditions of maximum lipase production. More than 90% of the lipase was cell bound and could be solubilized by treatment of the cells with Triton X-100. This permitted the purification of approximately 50 mg lipase. So far, no crystals of sufficient quality were obtained. Comparison of the model we built for the Pseudomonas lipase, on the basis of sequences and structures of various hydrolases which were found to possess a common folding pattern (alpha/beta hydrolase fold), with the X-ray structure of the P.glumae lipase revealed that it is possible to correctly build the structure of the core of a protein even in the absence of obvious sequence homology with a protein of known 3-D structure.

Amino Acid Sequence↗
PubMed1993

Total serum amylase but not lipase correlates with measured glomerular filtration rate.

Elevated serum amylase and lipase levels have been reported in patients with renal failure. Because the diagnosis of pancreatitis is often based on elevations in serum amylase or lipase along with abdominal pain, we determined the relationship between total serum amylase, lipase, and glomerular filtration rate (GFR). Thirty-three subjects, 13 men and 20 women (age range, 21-79), were included in the study. There was a statistically significant correlation between serum amylase and the actual GFR (r = -0.43, p = 0.01). However, no such correlation was seen with lipase. No correlation between total serum amylase and lipase was observed. Three subjects had elevated amylase (240-433 U/L, normal 50-225). Three patients had slightly elevated lipase (29-31 U/dl, normal 8-28). All patients were asymptomatic. Of 11 subjects with GFR < 50 cc/min, only one had an elevated amylase and another an elevated lipase. Our data suggest that although the total serum amylase level is determined in part by the GFR, elevations in either amylase or lipase may not occur even in the presence of renal failure. Therefore, even small elevations in the total serum amylase or lipase in a patient with renal insufficiency may be clinically significant.

Adult↗