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Regulation and structure of the heteromeric acetyl-CoA carboxylase
Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids, 2016The enzyme acetyl-CoA carboxylase (ACCase) catalyzes the committed step of the de novo fatty acid biosynthesis (FAS) pathway by converting acetyl-CoA to malonyl-CoA. Two forms of ACCase exist in nature, a homomeric and heteromic form. The heteromeric form of this enzyme requires four different subunits for activity: biotin carboxylase; biotin carboxyl ...
Jay J Thelen
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Regulation of Spinach Chloroplast Acetyl-CoA Carboxylase
Archives of Biochemistry and Biophysics, 1998We have investigated several factors which influence acetyl-CoA carboxylase (ACCase) activity in lysed spinach chloroplasts. (1) When assayed after rapid lysis of light-incubated chloroplasts, ACCase activity was 2-fold higher than activity from dark-incubated chloroplasts.
John B Ohlrogge
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Insights into the methodology of acetyl-CoA carboxylase inhibition
Acetyl-CoA carboxylase catalyzes the first committed and regulated step in fatty acid synthesis in all animals, plants and bacteria. In most Gram-positive and Gram-negative bacteria, the enzyme is composed of three proteins: biotin carboxylase, biotin carboxyl carrier protein and carboxyltransferase. The reaction consists of two half-reactions.
Mirela Tkalčić, Čavužić +2 more
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Regulation of acetyl-CoA carboxylase
Biochemical Society Transactions, 2006Acetyl-CoA carboxylase (ACC) catalyses the formation of malonyl-CoA, an essential substrate for fatty acid synthesis in lipogenic tissues and a key regulatory molecule in muscle, brain and other tissues. ACC contributes importantly to the overall control of energy metabolism and has provided an important model to explore mechanisms of enzyme control ...
R W, Brownsey +4 more
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Plant Molecular Biology, 1993
The acetyl-CoA carboxylase present in both wheat germ and total wheat leaf protein contains ca. 220 kDa subunits. It is the major biotin-dependent carboxylase present in wheat chloroplasts. Active acetyl-CoA carboxylase purified from wheat germ is a homodimer with an apparent molecular mass of ca. 500 kDa.
P, Gornicki, R, Haselkorn
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The acetyl-CoA carboxylase present in both wheat germ and total wheat leaf protein contains ca. 220 kDa subunits. It is the major biotin-dependent carboxylase present in wheat chloroplasts. Active acetyl-CoA carboxylase purified from wheat germ is a homodimer with an apparent molecular mass of ca. 500 kDa.
P, Gornicki, R, Haselkorn
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Effect of insulin on association of acetyl CoA carboxylase phosphatase and acetyl CoA carboxylase
Biochemical and Biophysical Research Communications, 1985Insulin promotes an association between acetyl CoA carboxylase and acetyl CoA carboxylase phosphatase. The association between rat epididymal fat tissue carboxylase and the phosphatase occurs in both a tissue culture system and in vivo and is accompanied by an increase in acetyl CoA carboxylase activity.
G R, Krakower, K H, Kim
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Archives of Biochemistry and Biophysics, 1971
Abstract A biotin carboxyl carrier protein (BCCP) from Escherichia coli has been purified and crystallized. The purified protein was found to be homogeneous by polyacrylamide gel electrophoresis and sedimentation in a synthetic boundary cell. BCCP has a sedimentation coefficient of 1.04 S, a diffusion coefficient ( D 20,w ) of 10.4 × 10 −7 cm 2 ...
A.M. Nervi +2 more
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Abstract A biotin carboxyl carrier protein (BCCP) from Escherichia coli has been purified and crystallized. The purified protein was found to be homogeneous by polyacrylamide gel electrophoresis and sedimentation in a synthetic boundary cell. BCCP has a sedimentation coefficient of 1.04 S, a diffusion coefficient ( D 20,w ) of 10.4 × 10 −7 cm 2 ...
A.M. Nervi +2 more
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Multi-subunit acetyl-CoA carboxylases
Progress in Lipid Research, 2002Acetyl-CoA carboxylase (ACC) catalyses the first committed step of fatty acid synthesis, the carboxylation of acetyl-CoA to malonyl-CoA. Two physically distinct types of enzymes are found in nature. Bacterial and most plant chloroplasts contain a multi-subunit ACC (MS-ACC) enzyme that is readily dissociated into its component proteins.
John E, Cronan, Grover L, Waldrop
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Inhibitors of Mammalian Acetyl-CoA Carboxylase
Recent Patents on Cardiovascular Drug Discovery, 2007Inhibition of acetyl-CoA carboxylase (ACC), with its resultant inhibition of fatty acid synthesis and stimulation of fatty acid oxidation, has the potential to favorably affect, in a concerted manner, a multitude of the cardiometabolic risk factors associated with diabetes, obesity, and the metabolic syndrome.
Jeffrey W, Corbett, James H, Harwood
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Regulation of Acetyl-CoA Carboxylase
1983Publisher Summary This chapter discusses the regulation of acetyl-CoA carboxylase. Acetyl-CoA carboxylase catalyzes the ATP-dependent carboxylation of acetyl-CoA in the formation of malonyl-CoA. Malonyl-CoA is then condensed to acetyl-CoA in the process of long-chain fatty acid synthesis.
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