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PubMed1995

Kinetic analysis of cardiolipin synthase: a membrane enzyme with two glycerophospholipid substrates.

Mitochondrial cardiolipin synthase catalyzes the transfer of a phosphatidyl moiety from phosphatidyl-CMP (PtdCMP) to phosphatidylglycerol (PtdGro) in the presence of specific divalent cations. The synthase was solubilized from Saccharomyces cerevisiae mitochondria and purified about 300-fold. The partially enzyme was part of a medium-size, mixed micelle which had to bind to a foreign substrate/detergent micelle before catalysis could occur. The kinetics of cardiolipin synthase were studied by changing the molar fraction of substrate in the micelles. The enzyme obeyed Michaelis-Menten kinetics in relation to PtdCMP with a Km of 0.03 mol%. PtdGro caused sigmoidal kinetics with a low apparent affinity. It is speculated that it was involved in docking the enzyme to the substrate/detergent micelle. Cardiolipin synthase did not catalyze isotope exchange between [14C]CMP and PtdCMP, virtually excluding a ping-pong catalytic mechanism. Mg2+ stimulated the activity by increasing the turnover number rather than the substrate affinity, a mechanism which was also found for the Co(2+)-activation of rat liver cardiolipin synthase. It is concluded that a direct association of the metal ion and the enzyme forms the active cardiolipin synthase which has a very high affinity for PtdCMP and a lower affinity for PtdGro.

Animals↗
PubMed1995

Inhibition of cardiolipin biosynthesis in the hypoxic rat heart.

Cardiolipin is the principal polyglycerophospholipid in the heart. The effect of hypoxia on cardiolipin biosynthesis was investigated in isolated rat hearts perfused in the Langendorff mode. Hearts were pulsed-labeled for 60 min with 0.1 mM [1,(3)-3H]glycerol in Krebs Henseleit buffer saturated with either 95% O2/5% CO2 (control) or 95% N2/5% CO2 (hypoxic). Radioactivity incorporated into phosphatidylglycerol and cardiolipin were reduced 88% (P < .05) and 79% (P < .05), respectively, in hypoxic hearts compared to controls. In other experiments, hearts were pulse-labeled for 15 min with 1.4 mM [32P]Pi in Krebs Henseleit buffer saturated with 95% O2/5% CO2 and subsequently perfused for 60 min under control or hypoxic conditions. The radioactivity incorporated into CDP-1,2-diacyl-sn-glycerol, phosphatidylglycerol, and cardiolipin were reduced 61% (P < .05), 71% (P < .05), and 70% (P < .05), respectively, in the hypoxic hearts compared to controls, indicating a decreased formation of CDP-1,2-diacyl-sn-glycerol in the hypoxic heart. The activities of the enzymes involved in cardiolipin biosynthesis and the cardiac pool sizes of cardiolipin, phosphatidylglycerol, and CDP-1,2-diacyl-1,2-diacyl-sn-glycerol were unaltered between hypoxic and control hearts. In contrast, cardiac adenosine-5'-triphosphate and CPT levels were decreased 94% (P < .05) and 92% (P < .05), respectively, in hypoxic hearts compared to controls. We postulate that the biosynthesis of the cardiac polyglycerophospholipid cardiolipin may be inhibited by a decreased adenosine-5'-triphosphate and cytidine-5'-triphosphate level in the heart.

Adenosine Triphosphate↗
PubMed1980

Changes in CTP:phosphatidate cytidylyltransferase activity during rabbit lung development.

The specific activity of CTP:phosphatidate cytidylyltransferase in rabbit lung and liver microsomes during fetal and neonatal development has been measured. The enzyme in the microsomal fraction of lung tissue has a requirement for Mg2+. Optimal enzyme activity is achieved with phosphatidate (4 mM) and CTP (2 mM) in the presence of ATP (6 mM). Analysis of the reaction products demonstrates that the ATP serves to inhibit the hydrolysis of CTP by microsomal pyrophosphatases. The specific activity of the microsomal enzyme remains constant from day 23 through day 28 of gestation, then increases 2.4-fold between day 28 and day 1 post-partum. The specific activity of the enzyme in the microsomal fraction from rabbit liver tissue does not change significantly, and is less than in the lung tissue at all stages of development. The increase in the activity of microsomal CTP:phosphatidate cytidylyltransferase in lung tissue is concurrent with the appearance of pulmonary surfactant containing phosphatidylglycerol during the perinatal period of rabbit lung development.

Adenosine Triphosphate↗
PubMed1981

Phosphatidylinositol-inositol exchange in a rabbit lung.

A microsomal fraction prepared from rabbit lung tissue was found to catalyze CDPdiacylglycerol-independent incorporation of [3H]inositol into phosphatidylinositol. This incorporation resulted from CMP-dependent phosphatidylinositol-inositol exchange and did not constitute a net synthesis of phosphatidylinositol. The phosphatidylinositol-inositol exchange activity was distinct from the phospholipid-base exchange enzymes and was specific for inositol. Optimal in vitro phosphatidylinositol-inositol exchange activity was observed at pH 8.5--8.8 and either Mn2+ or Mg2+ was essential for activity. Mercaptoethanol stimulated phosphatidylinositol-inositol exchange and Hg2+ inhibited this activity. In the absence of CMP, no phosphatidylinositol-inositol exchange was observed. CDP (and to a smaller extent CTP) also supported phosphatidylinositol-inositol exchange and this appeared to occur via the generation of CMP during incubations. The apparent Km values of the phosphatidylinositol-inositol exchange enzyme for CMP and inositol were 0.4 mM and 11 microM, respectively. When CDPdiacylglycerol was present at a concentration optimal for CDPdiacylglycerol : inositol transferase activity, CMP-dependent phosphatidylinositol-inositol exchange activity was still observed. However, in the presence of Hg2+ CDPdiacylglycerol inhibited phosphatidylinositol-inositol exchange activity. Several properties of the phosphatidylinositol-inositol exchange enzyme resemble those of CDPdiacylglycerol : inositol transferase, but the two enzymes appear distinct on the basis of different degrees of inhibition by either Ca2+, Hg/+ or heat, and on the basis of different changes in activity during lung development.

Animals↗
PubMed1982

CMP-dependent incorporation of [14C]Glycerol 3-phosphate into phosphatidylglycerol and phosphatidylglycerol phosphate by rabbit lung microsomes.

Rabbit lung microsomes were found to catalyze CMP-dependent incorporation of [14C]glycerol 3-phosphate into a total lipid extract. The radioactively labeled products in the lipid extract were identified as phosphatidylglycerol and phosphatidylglycerol phosphate. CMP-dependent incorporation of [14C]glycerol 3-phosphate by lung microsomes proceeded optimally at pH 7.4 and required Mn2+. The apparent Km value for CMP in this reaction was calculated to be 0.19 mM. No other cytidine nucleotide could substitute completely for CMP in supporting [14C]glycerol 3-phosphate incorporation into lipid. Cytosine-beta-D-arabinofuranoside-5'-monophosphate-dependent incorporation of [14C]glycerol 3-phosphate was observed at pH 8.5 but not at pH 6.8 CMP-dependent incorporation of [14C]glycerol 3-phosphate by microsomes was inhibited by inositol. The optimal in vitro rates of CMP-dependent and CDP diacylglycerol-dependent incorporation of [14C]glycerol 3-phosphate into lipid were similar (approximately 1 nmol . mg-1 protein . h-1) and were not additive. Both CMP -dependent and CDP diacylglycerol-dependent incorporation of [14C]glycerol 3-phosphate by lung microsomes appeared to involve CDPdiacylglycerol:glycerol-3-phosphate phosphatidyltransferase. However, the specific activity of this enzyme in a particular subcellular fraction did not relate directly in the extent of CMP-dependent [14C]glycerol 3-phosphate incorporation in that fraction. Preincubation of lung microsomes with 5 mM CMP plus 3 mM phosphatidylinositol increased CMP-dependent incorporation of [14C]glycerol 3-phosphate. When lung microsomes were depleted specifically of phosphatidylinositol by incubating with a phosphatidylinositol-specific phospholipase C, CMP-dependent incorporation was diminished. The Mn2+ requirement for CMP-dependent incorporation of [14C] glycerol 3-phosphate, its phosphatidylinositol requirement and its inhibition by Triton X-100 (0.2%) were not features shared by CDPdiacylglycerol-dependent incorporation of [14C]glycerol 3-phosphate but were characteristics of the reverse reaction catalyzed by CDPdiacylglycerol: inositol phosphatidyltransferase. Together with the previous finding of a developmental increase in the CMP content of fetal rabbit lung, these observations are consistent with a role for CMP in the regulation of the phosphatidylinositol and phosphatidylglycerol content of lung surfactant during lung maturation.

Animals↗
PubMed1999

2-Chloroadenosine reverses hyperglycemia-induced inhibition of phosphoinositide synthesis in cultured human retinal pigment epithelial cells and prevents reduced nerve conduction velocity in diabetic rats.

The effect of the adenosine (AD) analog 2-chloroadenosine (C-AD) on glucose-induced inhibition of phosphoinositide synthesis was studied in human retinal pigment epithelial (RPE) cells by monitoring the level of the phosphatidylinositol (PI) synthase substrate, cytidine diphosphate diglyceride (CDP-DG). In high-aldose reductase (AR)-expressing RPE 91 cells, C-AD decreased CDP-DG at 5 mmol/L glucose and reversed the increase by 20 mmol/L glucose. AD deaminase (ADA), which inactivates endogenously released AD, potentiated the hyperglycemia-induced increase in CDP-DG. Theophylline, an AD-A1 and AD-A2 receptor antagonist, caused an increase in CDP-DG at 20 mmol/L glucose. C-AD did not alter CDP-DG in low-AR-expressing RPE 45 cells, but did decrease CDP-DG after cells were conditioned in 300 mmol/L glucose for 1 week (which induces AR). The mechanism by which AD regulates PI synthase in cells with high AR activity is unknown, but it is independent of Gi or Gs proteins, adenylate cyclase and phospholipase C (PLC) activation, myo-inositol (MI) uptake, or MI efflux. Administration of C-AD to streptozotocin-induced diabetic rats prevented the slowing of motor nerve conduction velocity (MNCV). Thus, AD derivatives, which reverse a glucose-induced deficit in phosphoinositide metabolism, might serve as a useful pharmacological tool to intervene in hyperglycemia-induced diabetic complications.

2-Chloroadenosine↗
PubMed1996

Regulation of cardiolipin biosynthesis in H9c2 cardiac myoblasts by cytidine 5'-triphosphate.

The regulation of cardiolipin biosynthesis by CTP in H9c2 cardiac myoblasts was investigated. H9c2 cells were incubated in the presence of cyclopentenylcytosine which is converted to cyclopentenylcytosine-triphosphate, a potent and specific inhibitor of CTP synthetase. Incubation of cells for 12 h with cyclopentenylcytosine reduced the cellular pool size of CTP to less than 10% of control cells but did not influence the pool size of other nucleotides. The de novo biosynthesis of phosphatidylcholine from [methyl-3H]choline, phosphatidylethanolamine from [1-3H]ethanolamine, and biosynthesis of all glycerol containing phospholipids from [U-14C]glycerol or [1,3-3H]glycerol were reduced approximately 50% after preincubation of the cells with cyclopentenylcytosine. In contrast, radioactive glycerol accumulated in phosphatidic acid, diacylglycerol, and triacylglycerol in cyclopentenylcytosine-treated cells compared with controls suggesting a re-routing of phospholipid biosynthesis away from CTP utilizing reactions toward neutral lipid synthesis. The de novo biosynthesis of all phospholipids was restored to control levels by addition of cytidine to the medium which elevated CTP levels. Cyclopentenylcytosine did not affect the in vitro enzyme activities involved in cardiolipin biosynthesis in these cells. In addition, the resynthesis of cardiolipin and most phospholipids from [1-14C]linoleic acid was not affected by cyclopentenylcytosine. Our findings indicate that the cellular CTP level may regulate cardiolipin biosynthesis in H9c2 cardiac myoblasts and support the notion that the cellular CTP level may be a universal signal/switch for all phospholipid biosynthesis in eukaryotic cells.

Animals↗
PubMed1999

Plant-exuded choline is used for rhizobial membrane lipid biosynthesis by phosphatidylcholine synthase.

Phosphatidylcholine is a major lipid of eukaryotic membranes, but found in only few prokaryotes. Enzymatic methylation of phosphatidylethanolamine by phospholipid N-methyltransferase was thought to be the only biosynthetic pathway to yield phosphatidylcholine in bacteria. However, mutants of the microsymbiotic soil bacterium Sinorhizobium (Rhizobium) meliloti, defective in phospholipid N-methyltransferase, form phosphatidylcholine in wild type amounts when choline is provided in the growth medium. Here we describe a second bacterial pathway for phosphatidylcholine biosynthesis involving the novel enzymatic activity, phosphatidylcholine synthase, that forms phosphatidylcholine directly from choline and CDP-diacylglycerol in cell-free extracts of S. meliloti. We further demonstrate that roots of host plants of S. meliloti exude choline and that the amounts of exuded choline are sufficient to allow for maximal phosphatidylcholine biosynthesis in S. meliloti via the novel pathway.

Choline↗
PubMed1982

CDP-diacylglycerol synthase activity in Clostridium perfringens.

CTP:phosphatidate cytidylyltransferase (CDP-diacylglycerol synthase; EC 2.7.7.41) was identified in the cell envelope fraction of the gram-positive anaerobe Clostridium perfringens. The association of this enzyme with the cell envelope fraction of cell extracts was demonstrated by glycerol density gradient centrifugation and by activity sedimenting with the 100,000 x g pellet. The enzyme exhibited a broad pH optimum between pH 6.5 and pH 7.5. Enzyme activity was dependent on magnesium (5 mM) or manganese (1 mM) ions. Activity was also dependent on the addition of the nonionic detergent Triton X-100 (5 mM). The apparent Km values for CTP and phosphatidic acid were 0.18 mM and 0.22 mM, respectively. Thioreactive agents inhibited activity, indicating that a sulfhydryl group is essential for activity. Maximal enzyme activity was observed at 50 degrees C.

Cell Membrane↗
PubMed1972

Biosynthesis of cardiolipin from phosphatidylglycerol in Staphylococcus aureus.

Cardiolipin (CL) synthetase from Staphylococcus aureus catalyzes the complete conversion of two molecules of phosphatidylglycerol (PG) to one molecule of CL and one molecule of glycerol. The fatty acids and phosphates of the two PG molecules can be quantitatively recovered in the CL. The enzyme is membrane-bound, shows a linear relationship with the product formed between 10 and 125 mug of membrane protein, has a pH optimum at 4.4, a temperature optimum between 37 and 45 C, a K(m) for PG of 2.1 x 10(-4)m, a V(max) of 200 nmoles of CL per min per mg of membrane protein, and does not require monovalent or divalent metals for activity. The enzyme has no nucleotide requirement and is not affected by prolonged dialysis, and treatment of the enzyme with charcoal has no effect on its activity. The enzyme has no phosphomonoesterase or phosphodiesterase activity, does not act on CL, is specific for PG, and CL and glycerol are the sole products of its activity. Other lipids do not stimulate or inhibit its activity. The enzyme is inhibited by organic solvents and some detergents. There is sufficient CL synthetase activity to account for CL synthesis during exponential growth. Inhibition of CL hydrolysis during growth results in an increase in CL that is balanced by a loss of PG. The activity of CL synthetase is not affected by cytidine diphosphate diglyceride but is inhibited competitively by the product, CL.

Acetates↗
PubMed1981

Characterization of a membrane-associated cytidine diphosphate-diacylglycerol-dependent phosphatidylserine synthase in bacilli.

The synthesis of phosphatidylserine in two gram-positive aerobic bacteria has been partially characterized. We have located a cytidine 5'-diphospho-diacylglycerol:L-serine O-phosphatidyltransferase (phosphatidylserine synthase) activity in the membrane fraction of Bacillus licheniformis and Bacillus subtilis. The activity was demonstrated to be membrane associated by differential centrifugation, sucrose gradient centrifugation, and detergent solubilization. The direct involvement of cytidine 5'-diphospho-diacylglycerol in the reaction was demonstrated by the conversion of the liponucleotide phosphatidyl moiety to phosphatidylserine. This activity is dependent on divalent metal ion (manganese being optimal) and is stimulated by nonionic detergent and its product phosphatidylserine. Based on studies with various combinations of products and substrates, the reaction appears to follow a sequential BiBi kinetic mechanism.

Bacillus↗
PubMed1991

Synthesis of CDP-diacylglycerol by rat liver rough microsomes as visualized by electron microscopic autoradiography: relationship to GTP-stimulated membrane fusion.

Using detergent-free conditions of incubation for the analysis of liponucleotide synthesis, we compared GTP-dependent formation of CDP-diacylglycerol (CDP-DG) and membrane fusion in RNA-depleted rough microsomes from rat liver. After incubation of stripped rough microsomes (SRM) in the presence of GTP and [5-3H]-CTP, radioactivity was recovered in lipid extracts and identified by thin-layer chromatography as a single spot which co-migrated with CDP-DG. The nucleotide requirement for CDP-DG synthesis and that for membrane fusion were observed to be identical. We next carried out an electron microscopic autoradiographic analysis on incubated membranes to determine the site of incorporation of [5-3H]-CTP. Silver grains were observed directly over the unilamellar membranes of natural vesicles. In confirmation of the biochemical data, quantitation of silver grain density indicated more grains over membranes incubated in the presence of GTP than over those incubated in the absence of this nucleotide. For membranes incubated in the presence of GTP, the grain density was similar over fused and unfused membranes in the same preparation. When SRM were incubated with the enzyme co-factors required for synthesis of phosphatidylinositol, a GTP-independent membrane fusion was observed by both transmission and freeze-fracture electron microscopy. Together with the biochemical and autoradiographic data, this suggests that phospholipid metabolism may be activated by GTP and lead to the fusion of RER membrane.

Animals↗
PubMed1975

Studies in cholestasis of pregnancy. III. Fatty acid composition of serum phosphoglycerides.

The influence of cholestasis of pregnancy (CP) on liver lipid synthesis as reflected by the composition of serum phosphoglycerides was studied in 28 pregnant women in the last trimester by means of gas-liquid-chromatography (GLC). All patients complained of pruritus and had immunologically detectable lipoprotein-X (LP-X) in serum. Twenty women with uncomplicated pregnancies served as a control series. In lecithin, low palmitic acid (16:0) and high oleic acid (18:1 (n-9)) were found which appear to be characteristic for CP. The increased oleic acid suggests an enhanced liver lecithin synthesis through the cytidine-diphosphate diglyceride pathway. Measurement of the concentrations of lecithin from the gas-liquid-chromatograms was made possible by the use of an internal standard fatty acid added, which gave a linear relation to direct determination of lecithin. For further studies of influences of cholestasis of pregnancy on the relative fatty acid composition, lecithin was chosen because differences between lecithin (PC) and phosphoglycerides (GPL) were found, evidently due to mutual variations among the three components in GPL (lecithin, cephalin and lysolecithin).

Cholestasis↗
PubMed1977

Studies in cholestasis of pregnancy. VI. Fatty acid composition of glycero-phospholipids before and after delivery.

Eight pregnant women, complaining of generalized pruritus with lipoprotein-X (LP-X) in their serum and diagnosed as cases of cholestasis of pregnancy (CP)--were studied during pregnancy and after delivery. Ten women with uncomplicated normal pregnancy served as controls. LP-X, liver function tests and relative fatty acid composition of serum lecithin (determined by gas-liquid chromatography, GLC) were followed. The fatty acid composition in liver and serum lecithin is determined by the synthesis pathways of lecithin in the liver. The faster and quantitatively dominating cytidine-diphosphate diglyceride pathway, pathway I, causes the appearance of lecithin with palmitic acid (16:0) in 1-position and oleic (18:1) or linoleic (18:2) acid in 2-position, while pathway II, with methylation of phosphatidyl-ethanolamine (cephalin) preferentially cases the appearance of lecithin with stearic acid (18:0) in 1-position and arachidonic acid (20:4) in 2-position. Pathway I is enchanced by oestrogenic and pathway II by cholestatic influence. During pregnancy women with CP were characterized in their serum lecithin fatty acid composition by a high palmitic (16:0) and a high oleic (18:1) acid content, in agreement with earlier studies. After delivery, in women with prior CP a decrease in palmitic (16:0) and linoleic (18:2) acids and an increase in stearic (18:0) acid, was interpreted as decreased influence on the major lecithin synthesis pathway I and an enhancement of pathway II. In addition, after delivery in the lactating mother, serum lecithin fatty acid composition data revealed an essential fatty acid (EFA) "consumption." It was earlier shown, that women with previous CP (when studied 8--21 months after delivery) had as judged from their serum lecithin fatty acid composition, a "basic metabolic defect," expressing presumably as estrogen enhanced pathway II of liver lecithin synthesis. In the present study, soon after delivery (on day 4--8) women with prior CP showed, however, less pathway II influence than women with a prior normal pregnancy. This was interpreted as a presistence of the cholestatic influence on liver lecithin synthesis pathways at this short time after delivery. Serum lecithin fatty acid composition appears to be a sensitive variable for the evaluation of metabolic influences in the liver.

Adult↗
PubMed1968

Cytidine triphosphate: phosphatidic acid cytidyltransferase in Escherichia coli.

An enzyme has been found in particulate fractions of Escherichia coli that catalyzes the incorporation of cytidine triphosphate (CTP) into lipid in the presence of exogenous phosphatidic acid and Mg(++). The product has been identified enzymatically and by chromatography as cytidine diphosphate diglyceride. The reaction is optimal at a pH of 6.5 and Mg(++) concentration of 5-10 mm. The apparent K(m) for CTP is 7 x 10(-4)M and for phosphatidic acid, 2 x 10(-3)M. The reaction rate falls off rapidly with time and ceases entirely after 1 hr as the result of inactivation of the system by Mg(++).

Cytosine Nucleotides↗
PubMed1993

Hydrolysis of short acyl chain inositol lipids by phospholipase C-delta 1.

We investigated the relationship between substrate aggregation and activation of phosphoinositide-specific phospholipase C-delta 1 (PLC-delta 1), isolated from bovine brain cytosol. The inositol lipids 1,2-dibutyryl-sn-glycero-3-phosphoinositol (di-C4-PI), 1,2-dihexanoyl-sn-glycero-3-phosphoinositol (di-C6-PI), and 1,2-dioctanoyl-sn-glycero-3-phosphoinositol (di-C8-PI) were prepared from synthetic cytidine diphosphate diglyceride analogs in a reaction with myo-inositol catalyzed by yeast phosphatidylinositol synthase. All three lipids served as substrates for PLC-delta 1 at concentrations significantly below their critical micelle concentration (cmc). Under these conditions, steps that might limit the reaction rate, such as membrane adsorption or penetration into the phospholipid surface, were eliminated. Below the cmc, the concentration of lipid substrate required to produce hydrolysis followed the order: di-C8-PI < di-C6-PI << di-C4-PI. Calcium was essential for hydrolysis of the short chain substrates at all lipid concentrations tested. The dependence of the reaction on calcium suggests that this ion activates PLC-delta 1 at a step other than adsorption to or penetration of the membrane surface. As the concentration of di-C8-PI was raised above the cmc, the reaction velocity increased 2-3-fold. These results are consistent with the idea that micellar or bilayer aggregates of phosphoinositol are not required for PLC-catalyzed hydrolysis, although the reaction rate is enhanced by micelle formation.

Animals↗
PubMed1977

Phenethyl alcohol inhibition of sn-glycerol 3-phosphate acylation in Escherichia coli.

In vivo and in vitro experiments were performed to determine how phenethyl alcohol (PEA) inhibits phospholipid synthesis in Escherichia coli. This drug drastically reduced the rate of incorporation of sn-glycerol 3-phosphate into the phospholipids of an sn-glycerol 3-phosphate auxotroph. PEA also reduced the rate of fatty acid incorporation into the phospholipids of a fatty acid auxotroph. The kinetics of PEA inhibition of the rate of incorporation of sn-glycerol 3-phosphate were almost identical to those of PEA inhibition of the rate of fatty acid incorporation into phospholipids. The in vivo experiments suggested that the rate-limiting step(s) in phospholipid biosynthesis inhibited by PEA is at the level of the acylation of sn-glycerol 3-phosphate or beyond this step. PEA inhibited the sn-glycerol 3-phosphate acyltransferase with either palmitoyl coenzyme A or palmitoyl-acyl carrier protein as the acyl donor. This drug, however, had no effect on the cytidine 5'-diphosphate-diglyceride:glycerol 3-phosphate phosphatidyl transferase, cytidine 5'-diphosphate-diglyceride:L-serine phosphatidyl transferase, and acyl coenzyme A:lysophatidic acid acyltransferase. The in vitro findings suggested that PEA inhibits phospholipid synthesis primarily at the level of sn-glycerol 3-phosphate acyltransferase.

Acylation↗