Results 131 to 140 of about 19,848 (176)

Malonyl-CoA metabolism in cardiac myocytes

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Hypothalamic malonyl-CoA and the control of food intake [PDF]

Physiology and Behavior, 2013
Fatty acid metabolism is implicated in the hypothalamic control of food intake. In this regard, malonyl-CoA, an intermediate in fatty acid synthesis, is emerging as a key player. Malonyl-CoA in the hypothalamus has been proposed as an anorectic mediator in the central control of feeding.
Andrew Butler, Timothy Moran, Su Gao
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Malonyl-CoA decarboxylase in rat brain mitochondria

International Journal of Biochemistry, 1979
Abstract 1. 1. Partial purification of malonyl-CoA decarboxylase (EC 4.1.1.9) from rat brain mitochondria and comparison of its size, K m , pH optimum, and immunological crossreactivity showed that the enzyme from the brain is quite similar to that in the other tissues, contrary to previous conclusions. 2. 2.
Y S, Kim, P E, Kolattukudy, A, Boos
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Malonyl-CoA, fuel sensing, and insulin resistance

American Journal of Physiology-Endocrinology and Metabolism, 1999
Malonyl-CoA is an allosteric inhibitor of carnitine palmitoyltransferase (CPT) I, the enzyme that controls the transfer of long-chain fatty acyl (LCFA)-CoAs into the mitochondria where they are oxidized. In rat skeletal muscle, the formation of malonyl-CoA is regulated acutely (in minutes) by changes in the activity of the β-isoform of acetyl-CoA ...
N B, Ruderman, A K, Saha, D, Vavvas, L A, Witters   +3 more
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A malonyl-CoA-binding protein from liver

Biochemical and Biophysical Research Communications, 1987
A soluble protein that binds malonyl-CoA without requiring cofactors has been purified from rat liver. Until saturated, it competes with fatty acid synthetase for free malonyl-CoA, temporarily reducing the rate of fatty acid synthesis at low levels of malonyl-CoA, as in fatty acid synthetase--coupled assays for acetyl-CoA carboxylase.
R E, Dugan, B R, Osterlund, R F, Drong, T L, Swenson   +3 more
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Liver malonyl-CoA decarboxylase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1973
Abstract 1. 1.Malonyl-CoA decarboxylase (CE 4.1.1.9) was purified 51-fold from beef liver homogenate, by acid extraction, ammonium sulphate fractionation, precipitation at pH 5.8 and gel chromatography on Sephadex G-200. The molecular weight was estimated to be 250 000. Phosphate is an activator of the enzyme.
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Muscle malonyl-CoA decreases during exercise

Journal of Applied Physiology, 1989
Malonyl-CoA, the inhibitor of carnitine acyltransferase I, is an important regulator of fatty acid oxidation and ketogenesis in the liver. Muscle carnitine acyltransferase I has previously been reported to be more sensitive to malonyl-CoA inhibition than is liver carnitine acyltransferase I.
W W, Winder, J, Arogyasami, R J, Barton, I M, Elayan, P R, Vehrs   +4 more
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Malonyl-CoA, a Key Signaling Molecule in Mammalian Cells

Annual Review of Nutrition, 2008
Malonyl-CoA can be formed within the mitochondria, peroxisomes, and cytosol of mammalian cells. Besides being an intermediate in the pathways of de novo fatty acid biosynthesis and fatty acid elongation, malonyl-CoA has an important signaling function through its allosteric inhibition of carnitine palmitoyltransferase 1, the enzyme that normally ...
David Saggerson
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Microsomal malonyl-CoA-sensitive carnitine acyltransferase

Biochemical Society Transactions, 2001
Liver microsomes contain two carnitine acyltransferase activities. One of these has properties closely corresponding to those of 88 kDa mitochondrial carnitine palmitoyltransferase-1 (CPT-1). Antisera against CPT-1 cross-react with an 88 kDa microsomal protein, suggesting that CPT-1 may be targeted to both microsomal and mitochondrial membranes ...
N M, Broadway, R J, Pease, G, Birdsey, N A, Turner, M, Shayeghi, E D, Saggerson   +5 more
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Malonyl-CoA inhibits proteolysis of carnitine palmitoyltransferase

Biochemical and Biophysical Research Communications, 1991
Incubation of isolated mitochondria in the presence of malonyl-CoA prevented proteolysis of the outer carnitine palmitoyltransferase by Nagarse and trypsin. Malonyl-CoA had no direct action on trypsin when present in a chromogenic assay system for proteolysis or when preincubated with the proteases in the absence of mitochondria. As reported previously,
K, Kashfi, G A, Cook
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