scholarly journals Acyl-CoA reductase and acyl-CoA: fatty alcohol acyl transferase in the microsomal preparation from the bovine meibomian gland.

1988 ◽  
Vol 27 (4) ◽  
pp. 404-411
Author(s):  
P E Kolattukudy ◽  
L Rogers
Keyword(s):  
Fatty Alcohol ◽  
Meibomian Gland ◽  
Acyl Transferase ◽  
Microsomal Preparation ◽  
Coa Reductase

scholarly journals 3-Hydroxy-3-methylglutaryl-coenzyme A reductase. A comparison of the modulation in vitro by phosphorylation and dephosphorylation to modulation of enzyme activity by feeding cholesterol- or cholestyramine-supplemented diets

1980 ◽  
Vol 185 (2) ◽  
pp. 435-441 ◽  
Author(s):  
Konstantinos A. Mitropoulos ◽  
Brian L. Knight ◽  
Bernard E. A. Reeves
Keyword(s):  
Microsomal Fraction ◽  
Coenzyme A ◽  
Maximal Activity ◽  
Kinetic Properties ◽  
Standard Diet ◽  
Microsomal Preparation ◽  
Phosphoprotein Phosphatase ◽  
Coa Reductase ◽  
Hydroxymethylglutaryl Coa Reductase ◽  
Coenzyme A Reductase

The activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (hydroxymethylglutaryl-CoA reductase) was considerably inhibited during incubation with ATP+Mg2+. The inactivated enzyme was reactivated on further incubation with partially purified cytosolic phosphoprotein phosphatase. The inactivation was associated with a decrease in the apparent Km of the reductase for hydroxymethylglutaryl-CoA, and this was reversed on reactivation. The slight increase in activity observed during incubation of microsomal fraction without ATP was not associated with a change in apparent Km and, unlike the effect of the phosphatase, was not inhibited by NaF. Liver microsomal fraction from rats given cholesterol exhibited a low activity of hydroxymethylglutaryl-CoA reductase with a low apparent Km for hydroxymethylglutaryl-CoA. Mícrosomal fraction from rats fed cholestyramine exhibited a high activity with a high Km. To discover whether these changes had resulted from phosphorylation and dephosphorylation of the reductase, microsomal fraction from rats fed the supplemented diets and the standard diet were inactivated with ATP and reactivated with phosphoprotein phosphatase. Inactivation reduced the maximal activity of the reductase in each microsomal preparation and also reduced the apparent Km for hydroxymethylglutaryl-CoA. There was no difference between the preparations in the degree of inactivation produced by ATP. Treatment with phosphatase restored both the maximal activity and the apparent Km of each preparation, but never significantly increased the activity above that observed with untreated microsomal fraction. It is concluded that hydroxymethylglutaryl-CoA reductase in microsomal fraction prepared by standard procedures is almost entirely in the dephosphorylated form, and that the difference in kinetic properties in untreated microsomal fraction from rats fed the three diets cannot be explained by differences in the degree of phosphorylation of the enzyme.

scholarly journals The Effects of Boron Derivatives on Lipid Absorption from the Intestine and on Bile Lipids and Bile Acids of Sprague Dawley Rats

1995 ◽  
Vol 2 (2) ◽  
pp. 65-72 ◽  
Author(s):  
Iris H. Hall ◽  
David J. Reynolds ◽  
O. T. Wong ◽  
A. Sood ◽  
B. F. Spielvogel
Keyword(s):  
Bile Acids ◽  
Intestinal Mucosa ◽  
Enzyme Activities ◽  
Reductase Activity ◽  
Lipid Absorption ◽  
Small Intestinal Mucosa ◽  
Acyl Transferase ◽  
Hmg Coa Reductase ◽  
Small Intestinal ◽  
Coa Reductase

N,N-dimethyl-n-octadecylamine borane 1¯ at 8 mg/kg/day, tetrakis-u-(trimethylamine boranecarboxylato)-bis(trimethyl-carboxyborane)-dicopper(II) 2¯ at 2.5 mg/kg/day and trimethylamine-carboxyborane 3¯ at 8 mg/kg/day were evaluated for their effects on bile lipids, bile acids, small intestinal absorption of cholesterol and cholic acid and liver and small intestinal enzyme activities involved in lipid metabolism. The agent administered orally elevated rat bile excretion of lipids, e.g. cholesterol and phospholipids, and compounds 2¯ and 3¯ increased the bile flow rate. These agents altered the composition of the bile acids, but there was no significant increase in lithocholic acid which is most lithogenic agent in rats. The three agents did decrease cholesterol absorption from isolated in situ intestinal duodenum loops in the presence of drug. Hepatic and small intestinal mucosa enzyme activities, e.g. ATP-dependent citrate lyase, acyl CoA cholesterol acyl transferase, cholsterol-7-α -hydroxylase, sn glycerol-3-phosphate acyl transferase, phosphatidylate phosphohydrolase, and lipoprotein lipase, were reduced. However, the boron derivatives 1¯ and 3¯ decreased hepatic HMG-CoA reductase activity, the regulatory enzyme for cholesterol synthesis, but the compounds had no effects on small intestinal mucosa HMG-CoA reductase activity. There was no evidence of hepatic cell damage afforded by the drugs based on clinical chemistry values which would induce alterations in bile acid concentrations after treatment of the rat.

Covalent reaction of cerulenin at the active site of acyl-CoA reductase of Photobacterium phosphoreum

1989 ◽  
Vol 67 (2-3) ◽  
pp. 163-167 ◽  
Author(s):  
Lee Wall ◽  
Edward Meighen
Keyword(s):  
Active Site ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cysteine Residue ◽  
The Other ◽  
Photobacterium Phosphoreum ◽  
Acyl Transferase ◽  
Coa Reductase ◽  
Myristoyl Coa

Inhibition of bioluminescence in Photobacterium phosphoreum by cerulenin has been demonstrated to be due to a specific inactivation of the acyl-CoA reductase subunit of the fatty acid reductase complex required for synthesis of the aldehyde substrate for the luminescent reaction. In contrast, the activities of the other luminescence-related enzymes, acyl-protein synthetase, acyl-transferase, and luciferase, were unaffected by cerulenin. Myristoyl-CoA, but not NADPH, protected the acyl-CoA reductase against cerulenin inhibition. Cerulenin blocked the acylation of the reductase with myristoyl-CoA and the reaction with N-ethylmaleimide. A shift in mobility of the reductase polypeptide on sodium dodecyl sulfate – polyacrylamide gel electrophoresis occurred after reaction with cerulenin, a shift which could be blocked by reaction with N-ethylmaleimide. These results demonstrate that cerulenin blocks aldehyde synthesis by covalent reaction with the acyl-CoA reductase and indicate that the reaction may occur at a cysteine residue involved in the formation of the acyl–reductase intermediate.Key words: bioluminescence, cerulenin, acyl-CoA reductase.

Characterization of a Fatty Acyl-CoA Reductase fromMarinobacter aquaeoleiVT8: A Bacterial Enzyme Catalyzing the Reduction of Fatty Acyl-CoA to Fatty Alcohol

Biochemistry ◽  
2011 ◽  
Vol 50 (48) ◽  
pp. 10550-10558 ◽  
Author(s):  
Robert M. Willis ◽  
Bradley D. Wahlen ◽  
Lance C. Seefeldt ◽  
Brett M. Barney
Keyword(s):  
Fatty Alcohol ◽  
Fatty Acyl ◽  
Bacterial Enzyme ◽  
Coa Reductase

HMG-CoA reductase expression in human eyelid tissue and in a human meibomian gland epithelial cell line

2019 ◽  
Vol 257 (4) ◽  
pp. 785-790
Author(s):  
Kenneth G-J Ooi ◽  
Anupam Rao ◽  
Jonathan S-K Goh ◽  
Gary Gracie ◽  
Svetlana Cherepanoff ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Cell Line ◽  
Meibomian Gland ◽  
Epithelial Cell Line ◽  
Hmg Coa Reductase ◽  
Coa Reductase

scholarly journals A prokaryotic acyl-CoA reductase performing reduction of fatty acyl-CoA to fatty alcohol

FEBS Letters ◽  
2011 ◽  
Vol 585 (22) ◽  
pp. 3538-3543 ◽  
Author(s):  
Per Hofvander ◽  
Thuy T.P. Doan ◽  
Mats Hamberg
Keyword(s):  
Fatty Alcohol ◽  
Fatty Acyl ◽  
Coa Reductase

scholarly journals The Hypolipidemic Activity of Boronated Nucleosides in Male Mice and Rats

1996 ◽  
Vol 3 (4) ◽  
pp. 173-183 ◽  
Author(s):  
Bruce S. Burnham ◽  
Anup Sood ◽  
Jeno Tomasz ◽  
W. J. Powell ◽  
Bernard F. Spielvogel ◽  
...  
Keyword(s):  
Ldl Cholesterol ◽  
Hdl Cholesterol ◽  
Acyl Transferase ◽  
Male Mice ◽  
Hydroxylase Activity ◽  
Cholesterol Acyl Transferase ◽  
Hypolipidemic Agents ◽  
Cholesterol Levels ◽  
Tissue Lipids ◽  
Coa Reductase

The boronated nucleosides with varying bases and sugar moieties were shown to be potent hypolipidemic agents in rodents. The 3′– aminocynaoborane dideoxythymidine derivative caused reductions in serum cholesterol and triglyceride levels, tissue lipids, VLDL and LDL cholesterol levels while elevating HDL cholesterol levels in rodents. The agents suppressed rat hepatic acetyl CoA synthetase, HMG-CoA reductase, acyl-CoA cholesterol acyl transferase, phosphatidylate phosphohydrolase and lipoprotein lipase activities while elevating cholesterol-7α-hydroxylase activity from 25 to 100 μM.

Sign in / Sign up

Export Citation Format

Share Document