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.

3-Hydroxy-3-methylglutaryl coenzyme A reductase activity in beef adrenal cortex

1978 ◽  
Vol 56 (10) ◽  
pp. 958-962 ◽  
Author(s):  
B. Preiss ◽  
L. Tan ◽  
J.-G. Lehoux
Keyword(s):  
Adrenal Cortex ◽  
Sucrose Gradient ◽  
Microsomal Fraction ◽  
Coenzyme A ◽  
Reductase Activity ◽  
Zona Glomerulosa ◽  
Zona Fasciculata ◽  
Hmg Coa Reductase ◽  
Coa Reductase ◽  
Coenzyme A Reductase

3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) activity (mevalonate:NADP+ oxidoreductase (CoA-acylating) EC 1.1.1.34) was demonstrated in beef adrenal cortex. Most of the HMG-CoA reductase activity is in the microsomal fraction while a small percentage of the activity is associated with the mitochondria, Mitochondria purified on a linear sucrose gradient are enriched in HMG-CoA reductase and cytochrome c oxidase activities. The reductase present in microsomal preparations from the whole adrenal cortex has an apparent Km of 5.6 × 10−5 M for (R,S)-HMG-CoA. Reductase activities found in the microsomal fractions from the zona glomerulosa, the zona fasciculata, and the zona reticularis were 1.32, 7.37, and 9.74 nmol mevalonate formed per milligram protein in 30 min respectively.

scholarly journals A new method for assaying rat liver microsomal 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity and its application in a study of the effect of dietary cholesterol on this effect of dietary cholesterol on this enzyme

1977 ◽  
Vol 164 (3) ◽  
pp. 501-508 ◽  
Author(s):  
Y A Baqir ◽  
R Booth
Keyword(s):  
Rat Liver ◽  
Cholesterol Ester ◽  
Time Course ◽  
Coenzyme A ◽  
Reductase Activity ◽  
Dietary Cholesterol ◽  
New Method ◽  
Coa Reductase ◽  
Microsomal Cholesterol ◽  
Coenzyme A Reductase

A new method suitable for measuring rat liver 3-hydroxy-3-methylglutaryl-CoA reductase activity is described and its advantages over methods previously available are discussed. An accurate time course was measured for the inhibition of liver microsomal 3-hydroxy-3-methylglutaryl-CoA reductase activity by dietary cholesterol; this enzyme was affected 1 1/4 h after the rats began to consume a cholesterol-rich diet. In this experiment there was no correlation between concentrations of microsomal cholesterol ester and the activity of 3-hydroxy-3-methylglutary-CoA reductase.

scholarly journals Genome Sequence of the Fungal Strain 14919 Producing 3-Hydroxy-3-Methylglutaryl–Coenzyme A Reductase Inhibitor FR901512

2017 ◽  
Vol 5 (14) ◽  
Author(s):  
Hiroya Itoh ◽  
Makoto Matsui ◽  
Toshitaka Kumagai ◽  
Masanori Arita ◽  
Masayuki Machida ◽  
...  
Keyword(s):  
Soil Sample ◽  
Genome Sequence ◽  
Reductase Inhibitor ◽  
Coenzyme A ◽  
Fungal Strain ◽  
Hmg Coa Reductase ◽  
Chiba Prefecture ◽  
Hmg Coa Reductase Inhibitor ◽  
Coa Reductase ◽  
Coenzyme A Reductase

ABSTRACT Fungal strain 14919 was originally isolated from a soil sample collected at Mt. Kiyosumi, Chiba Prefecture, Japan. It produces FR901512, a potent and strong 3-hydroxy-3-methylglutaryl–coenzyme A (HMG-CoA) reductase inhibitor. The genome sequence of fungal strain 14919 was determined and annotated to improve the productivity of FR901512.

scholarly journals Activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in brains of adult and 7-day-old rats

1976 ◽  
Vol 154 (2) ◽  
pp. 559-560 ◽  
Author(s):  
M M. Sudjic ◽  
R Booth
Keyword(s):  
Rat Brain ◽  
Coenzyme A ◽  
Reductase Activity ◽  
Cholesterol Biosynthesis ◽  
Adult Brain ◽  
Adult Rat ◽  
Adult Rat Brain ◽  
Old Rats ◽  
Coa Reductase ◽  
Coenzyme A Reductase

Rat brain contains 3-hydroxy-3-methylglutaryl-CoA reductase activity, but this enzyme is far more active in 7-day-old brain than in adult brain. This difference may partly explain why cholesterol biosynthesis is more rapid in growing than in adult rat brain.

scholarly journals 3-hydroxy-3-methylglutaryl coenzyme A reductase of human lymphocytes: Kinetic properties

FEBS Letters ◽  
1978 ◽  
Vol 86 (2) ◽  
pp. 225-229 ◽  
Author(s):  
M. Laporte ◽  
M. Astruc ◽  
C. Tabacik ◽  
B. Descomps ◽  
A.Crastes de Paulet
Keyword(s):  
Coenzyme A ◽  
Human Lymphocytes ◽  
Kinetic Properties ◽  
Coenzyme A Reductase

scholarly journals Characteristics of rat liver microsomal 3-hydroxy-3-methylglutaryl-coenzyme A reductase

1986 ◽  
Vol 233 (1) ◽  
pp. 167-172 ◽  
Author(s):  
G C Ness ◽  
C E Sample ◽  
M Smith ◽  
L C Pendleton ◽  
D C Eichler
Keyword(s):  
Rat Liver ◽  
Coenzyme A ◽  
Rabbit Antiserum ◽  
Single Band ◽  
Coa Reductase ◽  
Coenzyme A Reductase

A procedure for the preparation of rat liver microsomal fractions essentially devoid of contaminating lysosomes is described. When this preparation was examined by immunoblotting with a rabbit antiserum to rat 3-hydroxy-3-methylglutaryl-CoA reductase, a single band corresponding to an Mr of 100000 was observed. No evidence was found for glycosylation of rat liver-3-hydroxy-3-methylglutaryl-CoA reductase. Native rat liver microsomal 3-hydroxy-3-methylglutaryl-CoA reductase differs from the purified proteolytically modified species in that it displays allosteric kinetics towards NADPH.

scholarly journals Enhanced Production of a Plant Monoterpene by Overexpression of the 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Catalytic Domain in Saccharomyces cerevisiae

2010 ◽  
Vol 76 (19) ◽  
pp. 6449-6454 ◽  
Author(s):  
Juan Rico ◽  
Ester Pardo ◽  
Margarita Orejas
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Coenzyme A ◽  
Catalytic Domain ◽  
Laboratory Strain ◽  
Strain Engineering ◽  
Enhanced Production ◽  
Wine Strain ◽  
Coa Reductase ◽  
Rate Limiting ◽  
Coenzyme A Reductase

ABSTRACT Linalool production was evaluated in different Saccharomyces cerevisiae strains expressing the Clarkia breweri linalool synthase gene (LIS). The wine strain T73 was shown to produce higher levels of linalool than conventional laboratory strains (i.e., almost three times the amount). The performance of this strain was further enhanced by manipulating the endogenous mevalonate (MVA) pathway: deregulated overexpression of the rate-limiting 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) doubled linalool production. In a haploid laboratory strain, engineering of this key step also improved linalool yield.

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