Acetyl Coenzyme A Carboxylase
نویسندگان
چکیده
منابع مشابه
Rat Mammary Acetyl Coenzyme A Carboxylase
The isolation of acetyl-CoA carboxylase from lactating rat mammary glands is described. A procedure was used which differs significantly from those employed by others who have isolated this enzyme from animal tissues. The purified enzyme catalyzes the carboxylation of 5.5 pmoles of acetylCoA per min per mg of protein under optimum assay conditions. Apparent K, values were determined for acetyl-...
متن کاملCharacterization of Maize Acetyl-Coenzyme A Carboxylase.
Maize (Zea mays L.) leaf acetyl-CoA carboxylase (ACCase) was purified about 500-fold by ammonium sulfate fractionation and gel filtration and blue Sepharose affinity and anion-exchange chromatography. Most ACCase activity (85%) recovered from the anion-exchange column was found in a highly purified fraction (specific activity 5.5 [mu]mol acid-stable product min-1 mg-1) that consisted primarily ...
متن کاملRegulation of Acetyl-Coenzyme A Carboxylase and Acetyl-Coenzyme A Synthetase in Spinach Chloroplasts
Acetyl-CoA Carboxylase, Acetyl-CoA Synthetase, Light Dependence o f Fatty Acid Synthesis in Chloroplasts In analogy to chloroplast fatty acid synthesis from acetate the key enzymes o f acetate fixation, acetyl-CoA synthetase and acetyl-CoA carboxylase, in rapidly Triton X-100 lysed spinach chloroplasts show an activation by light and deactivation in the dark. The stimulation o f acetyl-CoA carb...
متن کاملA gene encoding acetyl-coenzyme A carboxylase from Brassica napus.
ACCase (EC 6.4.1.2) is one of the key regulatory enzymes in fatty acid biosynthesis catalyzing the formation of malonyl-COA from acetyl-COA and bicarbonate in an ATPdependent reaction providing the substrate for fatty acid synthesis. ACCase from plants is proposed to be a dimer consisting of identical subunits of larger than 200 kD (Egli et al., 1993; Gomicki and Haselkom, 1993). To date the se...
متن کاملTissue distribution of acetyl-coenzyme a carboxylase in leaves.
Acetyl-CoA carboxylase [acetyl-CoA-carbon dioxide ligase (ADP forming), EC 6.4.1.2] is a biotin-containing enzyme catalyzing the formation of malonyl-CoA. The tissue distribution of this enzyme was determined for leaves of C(3)- and C(4)-plants. The mesophyll tissues of the C(3)-plants Pisum sativum and Allium porrum contained 90% of the leaf acetyl-CoA carboxylase activity, with the epidermal ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)81801-8