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PubMed2000

Specificity of papaya lipase in esterification with respect to the chemical structure of substrates.

Esterification, catalyzed by papaya (Carica papaya) lipase (CPL), was studied with various alcohols and carboxylic acids under competitive conditions. Acids studied were straight-chain saturates of different chain lengths, with octanoic acid as the reference. Alcohols chosen were aliphatic straight-chain, branched, secondary, tertiary, terpene, and aromatic alcohols of different chain lengths, using 1-hexanol as the reference. The initial reaction rate increased with increasing chain length of the acid from C4:0 to C18:0, followed by a slight decrease with C20:0. In the case of alcohols, an optimum chain length of 8 carbon atoms was obtained for the straight-chain aliphatic group (C2 to C16). Ethanol, 1-propanol, and secondary and tertiary alcohols showed rather low reactivity. Branching of the alcohols was found not to affect the reactivity in esterification; among the terpenes, beta-citronellol [(2E)-3, 7-dimethyl-6-octenol] and geraniol [(2E)-3,7-dimethylocta-2, 6-dien-1-ol] were found to be more reactive than nerol [(2Z)-3, 7-dimethylocta-2,6-dien-1-ol]. The highest reaction rate was found for the aromatic benzyl alcohol (phenylmethanol).

Fruit↗
PubMed2006

Highly chemoselective methylation and esterification reactions with dimethyl carbonate in the presence of NaY faujasite. The case of mercaptophenols, mercaptobenzoic acids, and carboxylic acids bearing OH substituents.

In the presence of NaY faujasite, the reactions of dimethyl carbonate (DMC) with several ambident nucleophiles such as o- and p-mercaptophenols (1a,b), o- and p-mercaptobenzoic acids (2a,b), o- and p-hydroxybenzoic acids (3a,b), mandelic and phenyllactic acids (4, 5), have been explored under batch conditions. Highly chemoselective reactions can be performed: at 150 degrees C, compounds 1 and 2 undergo only a S-methylation reaction, without affecting OH and CO2H groups; at 165 degrees C, acids 3-5 form the corresponding methyl esters, while both their aromatic and aliphatic OH substituents are fully preserved from methylation and/or transesterification processes. Typical selectivities are of 90-98% and isolated yields of products (S-methyl derivatives and methyl esters, respectively) are in the range of 85-96%. A comparative study with K2CO3 as a catalyst is also reported. Although the base (K2CO3) turns out to be more active than the zeolite, the chemoselectivity is elusive: compounds 2a,b undergo simultaneous S-methylation and esterification reactions, and acids 3-5 yield complex mixtures of products of O-methylation, O-methoxycarbonylation, and esterification of their OH and CO2H groups, respectively. Overall, the combined use of a nontoxic reagent/solvent (DMC) and a safe promoter (NaY) imparts a genuine ecofriendly nature to the investigated synthesis.

Journal Article↗
PubMed2005

N-alkyl-4-boronopyridinium halides versus boric acid as catalysts for the esterification of alpha-hydroxycarboxylic acids.

[reaction: see text] Boric acid is a highly effective catalyst for the dehydrative esterification reaction between equimolar mixtures of alpha-hydroxycarboxylic acids and alcohols. In contrast, N-methyl-4-boronopyridinium iodide (2a) is a more effective catalyst than boric acid for the similar esterification in excess alcohol. A heterogeneous catalyst, such as N-polystyrene-bound 4-boronopyridinium chloride, is also an effective catalyst and can be recovered by filtration.

Journal Article↗
PubMed2003

Amino acid ester prodrugs of floxuridine: synthesis and effects of structure, stereochemistry, and site of esterification on the rate of hydrolysis.

PURPOSE: To synthesize amino acid ester prodrugs of floxuridine (FUdR) and to investigate the effects of structure, stereochemistry, and site of esterification of promoiety on the rates of hydrolysis of these prodrugs in Caco-2 cell homogenates. METHODS: Amino acid ester prodrugs of FUdR were synthesized using established procedures. The kinetics of hydrolysis of prodrugs was evaluated in human adenocarcinoma cell line (Caco-2) homogenates and pH 7.4 phosphate buffer. RESULTS: 3'-Monoester, 5'-monoester, and 3',5'-diester prodrugs of FUdR utilizing proline, L-valine, D-valine, L-phenylalanine, and D-phenylalanine as promoieties were synthesized and characterized. In Caco-2 cell homogenates, the L-amino acid ester prodrugs hydrolyzed 10 to 75 times faster than the corresponding D-amino acid ester prodrugs. Pro and Phe ester prodrugs hydrolyzed much faster (3- to 30-fold) than the corresponding Val ester prodrugs. Further, the 5'-monoester prodrugs hydrolyzed significantly faster (3-fold) than the 3',5'-diester prodrugs. CONCLUSIONS: Novel amino acid ester prodrugs of FUdR were successfully synthesized. The results presented here clearly demonstrate that the rate of FUdR prodrug activation in Caco-2 cell homogenates is affected by the structure, stereochemistry, and site of esterification of the promoiety. Finally, the 5'-Val and 5'-Phe monoesters exhibited desirable characteristics such as good solution stability and relatively fast enzymatic conversion rates.

Amino Acids↗
PubMed2004

Selective esterifications of alcohols and phenols through carbodiimide couplings.

Esterification of carboxylic acids capable of forming ketene intermediates upon treatment with carbodiimides permits the selective acylation of alcohols in the presence of phenols lacking strong electron-withdrawing groups. The selectivity of acylations involving highly acidic phenols could be reversed through the addition of catalytic amount of acid. Esterification of other carboxylic acids was found to proceed through the formation of symmetric anhydrides and provide the opposite chemoselectivity. In both cases the relative acylation rates of substituted phenols are consistent with a reaction mechanism involving an attack of phenolate anions on electrophilic intermediates such as ketenes and symmetric anhydrides, with the carbodiimides serving both as an activating reagent and as a basic catalyst.

Journal Article↗
PubMed1999

Insulin decreases plasma cholesteryl ester transfer but not cholesterol esterification in healthy subjects as well as in normotriglyceridaemic patients with type 2 diabetes.

BACKGROUND: Plasma cholesterol esterification (EST) and subsequent cholesteryl ester transfer (CET) from high-density lipoproteins (HDLs) towards apolipoprotein (apo) B-containing lipoproteins are key steps in HDL metabolism. MATERIALS AND METHODS: The effects of exogenous hyperinsulinaemia on plasma CET and EST, measured with isotope methods, were evaluated in 10 male normotriglyceridaemic (plasma triglycerides <2.0 mmol L-1) patients with type 2 diabetes and 10 individually matched healthy subjects during a two-step hyperinsulinaemic euglycaemic clamp over 6-7 h. RESULTS: No between-group differences in baseline plasma lipid parameters were observed, but the HDL cholesteryl ester content was lower (P < 0.02) and the HDL triglyceride content was higher (P < 0.05) in diabetic patients. Baseline CET and EST were similar in the groups. In both groups, hyperinsulinaemia decreased plasma triglycerides (P < 0.01) and the HDL triglyceride content (P < 0.01) compared with saline infusion in healthy subjects, whereas the HDL cholesteryl ester content increased (P < 0.05 vs. saline infusion) in diabetic patients. CET was similarly decreased by hyperinsulinaemia in both groups (P < 0.01 vs. saline infusion). In contrast, the change in EST in either group was not different from that during saline administration. In the combined group, baseline CET was positively correlated with plasma triglycerides (Rs = 0.68, P < 0.01). The HDL cholesteryl ester content was negatively (Rs = -0.48, P < 0.05) and the HDL triglyceride content was positively (Rs = 0.64, P < 0.01) correlated with CET. CONCLUSION: Insulin infusion decreases plasma CET in conjunction with a fall in triglycerides but does not decrease cholesterol esterification in healthy and type 2 diabetic subjects, indicating that acute hyperinsulinaemia has a different effect on these processes involved in HDL metabolism. Despite unaltered fasting plasma CET, HDL core lipid composition was abnormal in diabetic patients, suggesting that additional mechanisms may contribute to changes in HDL metabolism in diabetes mellitus.

Apolipoproteins B↗
PubMed1990

Acylation-stimulatory activity in hyperapobetalipoproteinemic fibroblasts: enhanced cholesterol esterification with another serum basic protein, BP II.

Cultured fibroblasts from patients with familial hyperapobetalipoproteinemia (hyperapoB) were used to determine if a defect in lipid metabolism was present. Three basic proteins (BP I, BP II, and BP III) were isolated from normal human serum by preparative isoelectric focusing, preparative SDS/PAGE, and reversed-phase HPLC. The Mr and pI values of these proteins were 14,000 and 9.10 for BP I, 27,500 and 8.48 for BP II, and 55,000 and 8.73 for BP III. These proteins differed significantly in their content of arginine, cysteine, proline, histidine, serine, and methionine. BP I appears to be the same protein as acylation-stimulating protein, but BP II and BP III appeared different from acylation-stimulating protein and other lipid carrier proteins. BP I, BP II, and BP III stimulated the incorporation of [14C]oleate into lipid esters in normal fibroblasts, an effect that was time and concentration dependent. In hyperapoB cells, BP II markedly increased (up to 9-fold) the incorporation of [14C]oleate into cholesteryl ester compared with that in normal cells; in addition, there was a 50% decrease in the stimulation of triglyceride acylation and cholesterol esterification with BP I. No difference between normal and hyperapoB cells was observed with BP III. In summary, the identification of another serum basic protein, BP II, led to the elucidation of another cellular defect in hyperapoB fibroblasts, enhanced cholesterol esterification, which may be related to the precocious atherosclerosis and abnormal lipoprotein metabolism seen in hyperapoB.

Amino Acids↗
PubMed1996

Auto-regulation of retinoic acid biosynthesis through regulation of retinol esterification in human keratinocytes.

In this report, we describe an auto-regulatory loop in human keratinocytes, whereby all-trans retinoic acid (retinoic acid) regulates its own biosynthesis from all-trans retinol (retinol) through regulation of retinol esterification. Retinol esterification activity was low in normal proliferating human keratinocytes, cultured in retinoid-free media. Treatment of keratinocytes with retinoic acid induced retinol esterifying activity (8-fold). Induction of retinol esterifying activity was blocked by either actinomycin D or cycloheximide. Based on substrate specificity and inhibitor sensitivity, lecithin:retinol acyltransferase (LRAT) was identified as the retinoic acid-inducible retinol esterifying enzyme. Induction of LRAT by retinoic acid reduced conversion of retinol to retinoic acid by 50%. This reduction in retinoic acid synthesis resulted from sequestration of retinol as retinyl esters, since inhibition of LRAT restored retinoic acid synthesis to control levels. In normal human skin, undifferentiated keratinocytes, in the lowest cell layer, esterified retinol 4 times greater, than differentiating keratinocytes, in upper cell layers, reflecting an induced state, under conditions of retinol sufficiency. Regulation of LRAT activity by retinoic acid provides a novel mechanism through which retinoic acid can regulate its own level by controlling availability of retinol for conversion to retinoic acid. In human skin in vivo, retinyl esters synthesized in basal keratinocytes could undergo hydrolysis during differentiation and thus serve as a source of retinol for keratinocytes in upper layers of skin.

Acyltransferases↗
PubMed1990

Non-esterified fatty acid and glycerol kinetics and fatty acid re-esterification in goats during early lactation.

Non-esterified fatty acid (NEFA) and glycerol kinetics were studied in lactating goats to gain insight into the mechanisms by which animals in early lactation can initially mobilize and later replenish body fat reserves. Kinetic measurements were made at days 10, 38 and 76 post-partum in ten multiparous lactating does. Plasma NEFA concentrations and NEFA entry rate decreased as lactation advanced, being significantly higher at day 10 than at either days 38 or 76 of lactation. Both plasma NEFA concentrations and NEFA entry rate were negatively correlated with calculated energy balance. In contrast, glycerol entry rate was significantly higher at day 76 than at day 10 of lactation and was positively related to both calculated energy intake and energy balance. Apparent intracellular fatty acid re-esterification was lower at day 10 than at later stages of lactation and was positively related to calculated energy balance. It is suggested that during early lactation, substantial shifts in adipose tissue fat reserves can occur via altering rates of fatty acid re-esterification and de novo lipogenesis, without major changes in the rate of lipolysis.

Animals↗
PubMed2004

Spectroscopic determination of the degree of esterification of pectic substances from kenaf.

Pectins were isolated from bark, wood and pith of four kenaf (Hibiscus cannabinus L.) varieties. The degree of esterification of isolated pectins was studied using Fourier transform infrared spectroscopy. It was determined as being between 57 and 90% and there were no notable differences between kenaf varieties. The higher value of the degree of esterification was presented in wood pectins (86-90%), the interim in pith (75-83%) and the lower in bark (57-64%).

Hibiscus↗
PubMed1975

Depression of lecithin-cholesterol acyltransferase esterification in vitamin E-deficient monkeys.

Vitamin E deficiency in two species of monkeys (capuchins and cynamolgus) reduced the in vitro cholesterol esterification by plasma lecithin-cholesterol acyltransferase. The reduction was greates in the most deficient species and in animals fed a diet rich in polyunsaturated fat (safflower oil) stripped of vitamin E. The best correlate of total esterification was the plasma concentration of free cholesterol which reflected the degree of hyperlipidemia, found to be greatest in capuchins fed coconut oil. A logical explanation for the decreased LCAT activity in vitamin E deficiency would be peroxidative damage of substrate (the PUFA of lecithin) or of sulfhydryl sited on lecithin-cholesterol acyltransferase itself. However, neither case was fully supported by the data suggesting that additional information concerning the nature of the reaction and the role of vitamin E is required.

Acyltransferases↗
PubMed1974

Enzymatic Esterification of Indole-3-acetic Acid to myo-Inositol and Glucose.

Incubation of mature sweet corn kernels of Zea mays in dilute solutions of (14)C-labeled indole-3-acetic acid leads to the formation of (14)C-labeled esters of myo-inositol, glucose, and glucans. Utilizing this knowledge it was found that an enzyme preparation from immature sweet corn kernels of Zea mays catalyzed the CoA- and ATP-dependent esterification of indole-3-acetic acid to myo-inositol and glucose. The esters formed were 2-O-(indole-3-acetyl)-myo-inositol, 1-dl-1-O-(indole-3-acetyl)-myo-inositol, di-O-(indole-3-acetyl)-myo-inositol, tri-O-(indole-3-acetyl)-myo-inositol, 2-O-(indole-3-acetyl)-d-glucopyranose, 4-O-(indole-3-acetyl)-d-glucopyranose and 6-O-(indole-3-acetyl)-d-glycopyranose. An assay system was developed for measuring esterification of (14)C-labeled indole-3-acetic acid by ammonolysis of the esters followed by isolation and counting the radioactive indole-3-acetamide.

Journal Article↗
PubMed1992

Changes in Esterification of the Uronic Acid Groups of Cell Wall Polysaccharides during Elongation of Maize Coleoptiles.

Cell walls of grasses have two major polysaccharides that contain uronic acids, the hemicellulosic glucuronoarabinoxylans and the galactosyluronic acid-rich pectins. A technique whereby esterified uronic acid carboxyl groups are reduced selectively to yield their respective 6,6-dideuterio neutral sugars was used to determine the extent of esterification and changes in esterification of these two uronic acids during elongation of maize (Zea mays L.) coleoptiles. The glucosyluronic acids of glucuronoarabinoxylans did not appear to be esterified at any time during coleoptile elongation. The galactosyluronic acids of embryonal coleoptiles were about 65% esterified, but this proportion increased to nearly 80% during the rapid elongation phase before returning to about 60% at the end of elongation. Methyl esters accounted for about two-thirds of the total esterified galacturonic acid in cell walls of unexpanded coleoptiles. The proportion of methyl esters decreased throughout elongation and did not account for the increase in the proportion of esterified galactosyluronic acid units during growth. The results indicate that the galactosyluronic acid units of grass pectic polysaccharides may be converted to other kinds of esters or form ester-like chemical interactions during expansion of the cell wall. Accumulation of novel esters or ester-like interactions is coincident with covalent attachment of polymers containing galactosyluronic acid units to the cell wall.

Journal Article↗
PubMed1987

Retinol esterification by mouse epidermal microsomes: evidence for acyl-CoA:retinol acyltransferase activity.

In an attempt to characterize the enzyme(s) responsible for retinol esterification in hairless mouse epidermis, various subcellular fractions were incubated with [3H]retinol and the reaction products (retinyl esters) isolated by high-performance liquid chromatography. The microsomal fraction exhibited the highest esterifying activity and was stimulated by the addition of palmitoyl-CoA and dithiothreitol, but not by palmitic acid. Saturation kinetics with an apparent Km of about 6 microM for retinol were noted. Experiments with competitive and noncompetitive inhibitors of [3H]retinol esterification established that the epidermal enzyme was an acyl-CoA:retinol acyltransferase (ARAT; EC 2.3.1.76). The specificity for retinol was not absolute; a few closely related vitamin A alcohols were equally good substrates. The ARAT activity was not significantly altered by physiologic variations in the epidermal vitamin A content. In conclusion, mouse epidermis expresses ARAT activity which may be of importance for the regulation of vitamin A metabolism at the cellular level.

Acyltransferases↗
PubMed1996

Coupling of Metabolism and Bioconversion: Microbial Esterification of Citronellol with Acetyl Coenzyme A Produced via Metabolism of Glucose in an Interface Bioreactor.

Microbial esterification of citronellol with acetyl coenzyme A (acetyl-CoA) produced via metabolism of glucose was performed with Hansenula saturnus IFO 0809 in an interface bioreactor by using a hydrophilic carrier (an agar plate or an agar-coated filter pad) and a hydrophobic organic solvent (decane). An increase in the glucose concentration on an agar plate led to a decrease in oxidation of citronellol and an increase in the amount of citronellyl acetate. Fed-batch addition of citronellol efficiently alleviated substrate toxicity and resulted in the accumulation of high levels of citronellyl acetate. Furthermore, triple coupling of acetyl-CoA formation, microbial reduction of citronellal to citronellol, and esterification of the resulting citronellol with acetyl-CoA was also an efficient way to prepare citronellyl acetate. By using coupling systems, citronellyl acetate could be efficiently produced without any acetyl donor.

Journal Article↗
PubMed2001

Transcriptional regulation of the two sterol esterification genes in the yeast Saccharomyces cerevisiae.

Saccharomyces cerevisiae transcribes two genes, ARE1 and ARE2, that contribute disproportionately to the esterification of sterols. Are2p is the major enzyme isoform in a wild-type cell growing aerobically. This likely results from a combination of differential transcription initiation and transcript stability. By using ARE1 and ARE2 promoter fusions to lacZ reporters, we demonstrated that transcriptional initiation from the ARE1 promoter is significantly reduced compared to that from the ARE2 promoter. Furthermore, the half-life of the ARE2 mRNA is approximately 12 times as long as that of the ARE1 transcript. We present evidence that the primary role of the minor sterol esterification isoform encoded by ARE1 is to esterify sterol intermediates, whereas the role of the ARE2 enzyme is to esterify ergosterol, the end product of the pathway. Accordingly, the ARE1 promoter is upregulated in strains that accumulate ergosterol precursors. Furthermore, ARE1 and ARE2 are oppositely regulated by heme. Under heme-deficient growth conditions, ARE1 was upregulated fivefold while ARE2 was down-regulated. ARE2 requires the HAP1 transcription factor for optimal expression, and both ARE genes are derepressed in a rox1 (repressor of oxygen) mutant genetic background. We further report that the ARE genes are not subject to end product inhibition; neither ARE1 nor ARE2 transcription is altered in an are mutant background, nor does overexpression of either ARE gene alter the response of the ARE-lacZ reporter constructs. Our observations are consistent with an important physiological role for Are1p during anaerobic growth when heme is limiting and sterol precursors may accumulate. Conversely, Are2p is optimally required during aerobiosis when ergosterol is plentiful.

Acyltransferases↗
PubMed1982

The effect of lidocaine on cholesterol influx, esterification, and accumulation in cultured cells.

Lidocaine, a local anesthetic, inhibited cholesterol esterification in various cultured cells derived from tissues of the mouse, rat, hamster, monkey, and man. Esterification of exogenous [1-14C]oleate, fatty acid synthesized in situ from [1-14C]acetate, and exogenous [7-3H]cholesterol was reduced 20-50% with 1.5 mM lidocaine in the culture medium. In Fu5AH rat hepatoma cells, incubated for 24 h with hyperlipemic serum lipoproteins and increasing levels of lidocaine up to 1.5 mM, unesterified (free) cholesterol mass of the cells increased about 25% whereas the cholesteryl ester mass fell about 40%. The net result was a reduction in total cellular sterol. When the cells were incubated with lidocaine and hyperlipemic serum lipoproteins labeled with [7-3H(N)]cholesterol of known specific activity, incorporation of exogenous free cholesterol into cellular free cholesterol was constant, whereas there was a dose-dependent reduction in the amount of exogenous cholesterol appearing in cholesteryl esters. Additionally, a comparison of specific activities of cellular free cholesterol and cholesteryl esters at intervals over a 24-h period suggests that lidocaine also inhibits lysosomal cholesterol ester hydrolase (EC 3.1.1.13) in the Fu5AH cell line.

Acetates↗