What is ACP biology?
The acyl carrier protein (ACP) is a cofactor of both fatty acid and polyketide biosynthesis machinery. It is one of the most abundant proteins in cells of E. coli.
What is the function of malonyl-CoA?
Malonyl-CoA has long been recognized as an important precursor of fatty acid biosynthesis in lipogenic tissues such as the liver and has an important role in regulating fatty acid oxidation in heart and skeletal muscle. Malonyl-CoA has also recently emerged as an important regulator of food intake and energy balance.
What is the difference between ACP and AP classes?
ACP vs. An ACP student is registered in an IU college course and a college grade is entered onto the student’s permanent college transcript upon course completion; an AP student is enrolled in a high school college-level class designed to prepare the student to take an examination.
What is beta-ketoacyl ACP synthase?
Beta-ketoacyl-ACP synthase. In molecular biology, Beta-ketoacyl-ACP synthase EC 2.3.1.41, is an enzyme involved in fatty acid synthesis. It results in the formation of acetoacetyl ACP . Beta-ketoacyl-ACP synthase is a highly conserved enzyme that is found in almost all life on earth as a domain in fatty acid synthase (FAS).
What is the function of beta ketoacyl synthase III?
Beta-ketoacyl-ACP synthase III, perhaps the most well known of this family of enzymes, catalyzes a Claisen condensation between acetyl CoA and malonyl ACP. The image below reveals how CoA fits in the active site as a substrate of synthase III.
What is the role of CoA in beta-ketoacyl-ACP synthase?
It typically uses malonyl-CoA as a carbon source to elongate ACP-bound acyl species, resulting in the formation of ACP-bound β-keto acyl species such as acetoacetyl – ACP. Beta-ketoacyl-ACP synthase is a highly conserved enzyme that is found in almost all life on earth as a domain in fatty acid synthase (FAS).
Where is beta-ketoacyl-ACP synthase found?
Beta-ketoacyl-ACP synthase. Type I is found in animals, fungi, and “lower eukaryotes .” Type II is found in prokaryotes, plastids, and mitochondria. Beta-ketoacyl-ACP synthase III, perhaps the most well known of this family of enzymes, catalyzes a Claisen condensation between acetyl CoA and malonyl ACP.