BIOSYNTHESIS OF LIPIDS IN PLANTS: II. INCORPORATION OF GLYCEROPHOSPHATE-32P INTO PHOSPHATIDES BY CELL-FREE PREPARATIONS FROM SPINACH LEAVES

1966 ◽  
Vol 44 (4) ◽  
pp. 459-467 ◽  
Author(s):  
P. S. Sastry ◽  
M. Kates
Keyword(s):  
Adenosine Triphosphate ◽  
Lysophosphatidic Acid ◽  
Coenzyme A ◽  
Phosphatidyl Inositol ◽  
Phosphatidyl Glycerol ◽  
Enzyme Systems ◽  
Microsome Fraction ◽  
Chloroplast Fraction ◽  
Phosphatide Acid ◽  
Spinach Leaves

Cell-free homogenates of spinach leaves incorporated glycerophosphate-32P into phosphatides when supplied with adenosine triphosphate, Mg++and coenzyme A (CoA). Most of the activity of the homogenate was associated with the microsome fraction sedimented at 104,000 × g, but some activity was also present in the chloroplast fraction. In all systems, most of the32P incorporated appeared in phosphatide acid (+ lysophosphatidic acid), with small to trace amounts in phosphatidyl glycerol and phosphatidyl inositol. Coenzyme A and adenosine triphosphate + Mg++were obligatory cofactors for the incorporation of α-glycerophosphate-32P but acetate + bicarbonate, cytidine triphosphate, or light were not essential. The results demonstrate the presence of acyl-CoA:L-glycerol-3-phosphate O-acyltransferase in the microsome fraction of spinach leaves and also indicate the existence of enzyme systems catalyzing the conversion of phosphatidic acid to phosphatidyl inositol and phosphatidyl glycerol.

BIOSYNTHESIS OF LIPIDS IN PLANTS: I. INCORPORATION OF ORTHOPHOSPHATE-32P AND GLYCEROPHOSPHATE-32P INTO PHOSPHATIDES OF CHLORELLA VULGARIS DURING PHOTOSYNTHESIS

1965 ◽  
Vol 43 (9) ◽  
pp. 1445-1453 ◽  
Author(s):  
P. S. Sastry ◽  
M. Kates
Keyword(s):  
Chlorella Vulgaris ◽  
Phosphatidyl Ethanolamine ◽  
Phosphatidyl Inositol ◽  
Biosynthetic Pathways ◽  
Bacterial Cells ◽  
Phosphatidyl Glycerol ◽  
Kinetics Of

The kinetics of incorporation of 32P from orthophosphate-32P or DL-α-glycerophosphate-32P into the phosphatides of Chlorella vulgaris during photosynthesis was studied. Rapid labelling of phosphatidyl glycerol was observed with both precursors, followed by lower rates of incorporation into lecithin, phosphatidyl ethanolamine, and phosphatidyl inositol. The results are discussed in the light of biosynthetic pathways known for animal and bacterial cells.

The role of adenosine triphosphate citrate lyase in the metabolism of acetyl coenzyme a and function of blood platelets in diabetes mellitus

Metabolism ◽  
2004 ◽  
Vol 53 (1) ◽  
pp. 66-72 ◽  
Author(s):  
Anna Michno ◽  
Anna Skibowska ◽  
Anna Raszeja-Specht ◽  
Justyna Ćwikowska ◽  
Andrzej Szutowicz
Keyword(s):  
Diabetes Mellitus ◽  
Adenosine Triphosphate ◽  
Coenzyme A ◽  
Blood Platelets ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Citrate Lyase ◽  
And Function

scholarly journals CGI-58/ABHD5 is a coenzyme A-dependent lysophosphatidic acid acyltransferase

2009 ◽  
Vol 51 (4) ◽  
pp. 709-719 ◽  
Author(s):  
Gabriela Montero-Moran ◽  
Jorge M. Caviglia ◽  
Derek McMahon ◽  
Alexis Rothenberg ◽  
Vidya Subramanian ◽  
...  
Keyword(s):  
Lysophosphatidic Acid ◽  
Coenzyme A ◽  
Lysophosphatidic Acid Acyltransferase

The occurrence of Δ3-trans-hexadecenoic acid in phosphatidyl glycerol from spinach leaves

1964 ◽  
Vol 20 (9) ◽  
pp. 511-512 ◽  
Author(s):  
F. Haverkate ◽  
J. de Gier ◽  
L. L. M. van Deenen
Keyword(s):  
Hexadecenoic Acid ◽  
Phosphatidyl Glycerol ◽  
Spinach Leaves

Solubilization of microsomal-associated phosphatidylserine synthase and phosphatidylinositol synthase from Saccharomyces cerevisiae

1981 ◽  
Vol 27 (11) ◽  
pp. 1140-1149 ◽  
Author(s):  
George M. Carman ◽  
Jonathan Matas
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Specific Activity ◽  
Phosphatidyl Inositol ◽  
Maximum Activity ◽  
Enzymatic Activities ◽  
Ph Optimum ◽  
Phosphatidylserine Synthase ◽  
Phosphatidylinositol Synthase ◽  
Microsome Fraction ◽  
Triton X

Membrane-associated cytidine 5′-diphospho-1,2-diacyl-sn-glycerol (CDP-diacylglycerol):L-serine O-phosphatidyltransferase (phosphatidylserine synthase, EC 2.7.8.8.) and CDP-diacylglycerol: myo-inositol phosphatidyltransferase (phosphatidyl-inositol synthase, EC 2.7.8.11) were solubilized from the microsomal fraction of Saccharomyces cerevisiae. A variety of detergents were examined for their ability to release phosphatidylserine synthase and phosphatidylinositol synthase activities from the microsome fraction. Both enzymes were solubilized from the microsome fraction with Renex 690 in yields over 80% with increases in specific activity of 1.6-fold. Both solubilized enzymatic activities were dependent on manganese ions and Triton X-100 for maximum activity. The pH optimum for each reaction was 8.0. The apparent Km values for CDP-diacylglycerol and serine for the phosphatidylserine synthase reaction were 0.1 and 0.25 mM, respectively. The apparent Km values for CDP-diacylglycerol and inositol for the phosphatidylinositol synthase reaction were 70 μM and 0.1 mM, respectively. Thiore-active agents inhibited both enzymatic activities. Both solubilized enzymatic activities were thermally inactivated at temperatures above 30 °C.

scholarly journals The hydrolysis of phosphatidylinositol by lysosomal enzymes of rat liver and brain

1978 ◽  
Vol 176 (2) ◽  
pp. 475-484 ◽  
Author(s):  
R F Irvine ◽  
N Hemington ◽  
R M C Dawson
Keyword(s):  
Phospholipase C ◽  
Rat Liver ◽  
Gel Filtration ◽  
Phosphatidyl Inositol ◽  
Temperature Stability ◽  
Enzyme Systems ◽  
Phosphatidic Acid Phosphatase ◽  
Bivalent Metals ◽  
Hydrolysis Of ◽  
Marked Specificity

1. Lysosomes from rat liver contain two enzymic systems for hydrolysing phosphatidyl-inositol: a deacylation via lysophosphatidylinositol producing glycerophosphoinositol and non-esterified fatty acid, and a phospholipase C-like cleavage into inositol 1-phosphate and diaclygycerol. 2. The separate enzyme systems involved can be distinguished by gel filtration, differential temperature-stability and the inhibitory action of detergents. 3. The enzyme systems both have pH optima at 4.8 and their attack on a pure phosphatidylinositol substrate is inhibited by many bivalent metals including Ca2+ and Mg2+, and cationic drugs. 4. Whereas the deacylation system will attack other glycerophospholipids, the phospholipase C shows a marked specificity towards phosphatidylinositol, although it will also slowly attach phosphatidylcholine with the liberation of phosphocholine. 5. Gel filtration and temperature-stability distinguish the phospholipase C from lysosomal phosphatidic acid phosphatase, but not from sphingomyelinase. 6. Evidence is presented that an EDTA-insensitive phospholipase C degrading phosphatidylinositol is present in rat brain.

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