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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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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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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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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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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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Deficient acetyl CoA carboxylase activity in multiple carboxylase deficiency
Clinica Chimica Acta, 1981Multiple carboxylase deficiency has previously been characterized by deficient activity of three biotin-dependent enzymes: propionyl CoA carboxylase, pyruvate carboxylase and beta-methylcrotonyl CoA carboxylase. We have demonstrated that the activity of a fourth carboxylase, acetyl CoA carboxylase (ACC), is also deficient in fibroblasts from two ...
G L, Feldman, B, Wolf
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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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Acetyl-CoA carboxylase from rat adipose tissue
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1969Abstract Rat epididymal adipose tissue acetyl-CoA carboxylase activity has been shown to respond to various dietary treatments. Feeding a high dextrose diet increases the enzyme activity. In biotin-deficient rats the enzyme activity is reduced to less than a sixth of the levels found in control animals fed the deficient diet supplemented with biotin.
K, Dakshinamurti, P R, Desjardins
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