Sandbox Reserved 434
From Proteopedia
(Difference between revisions)
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==Introduction== | ==Introduction== | ||
| - | + | Vanin 1, otherwise known as pantetheinase, is an enzyme found throughout the body in various tissues including the liver and kidneys. As an ectoenzyme—any enzyme found on the outside or outer surface of a cell—pantethiense is anchored to the cell wall by a glycosylphosphatidylinositol (GPI) linker, allowing for the it to carry out its enzymatic purpose of hydrolyzing pantetheine to pantothenic acid and cysteamine [1]. The two protein subunits possess dense regions of <scene name='48/483891/Secondary_structure/1'>beta strands and alpha helices</scene> which create binding sites for three types of ligands, the non-polar <scene name='48/483891/Rrv/1'>RRV ligand</scene>, a di(hydroxyethyl)ether compound <scene name='48/483891/Peg/1'>PEG</scene>, and <scene name='48/483891/Nag/1'>NAG</scene> (N-acetyl-d-glucosamine) ligands. The identification of the associated binding sites has led to the investigation of active-site inhibitors (see Additional Features). | |
| - | Vanin 1, otherwise known as pantetheinase, is an enzyme found throughout the body in various tissues including the liver and kidneys. As an ectoenzyme—any enzyme found on the outside or outer surface of a cell—pantethiense is anchored to the cell wall by a glycosylphosphatidylinositol (GPI) linker, allowing for the it to carry out its enzymatic purpose of hydrolyzing pantetheine to pantothenic acid and cysteamine [1]. | + | |
The importance of vanin 1 lies in the products of the enzymatic reaction. Pantothenic acid (vitamin B12) plays a significant role in the maintenance of the nervous system and brain. The compound is also involved in DNA synthesis, as well as fatty acid and amino acid metabolism [2]. Cysteamine—a product of the degradation of the amino acid cysteine—is used to form coenzyme A, a compound that plays a key role in the citric acid cycle and the synthesis of fatty acids. A lack of these biomolecules can lead to significant physiological issues (see Additional Features). | The importance of vanin 1 lies in the products of the enzymatic reaction. Pantothenic acid (vitamin B12) plays a significant role in the maintenance of the nervous system and brain. The compound is also involved in DNA synthesis, as well as fatty acid and amino acid metabolism [2]. Cysteamine—a product of the degradation of the amino acid cysteine—is used to form coenzyme A, a compound that plays a key role in the citric acid cycle and the synthesis of fatty acids. A lack of these biomolecules can lead to significant physiological issues (see Additional Features). | ||
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4CYG has three types ligands involved in the structure. There are two <scene name='48/483891/Rrv/1'>RRV</scene> ((2r)-2,4-dihydroxy-n-[(3s)-3-hydroxy-4-phenylbutyl]-3,3-dimethylbutanamide) ligands, two <scene name='48/483891/Peg/1'>PEG</scene> (di(hydroxyethyl) ether) ligands, and eight <scene name='48/483891/Nag/1'>NAG</scene> (N-acetyl-d-glucosamine) ligands. | 4CYG has three types ligands involved in the structure. There are two <scene name='48/483891/Rrv/1'>RRV</scene> ((2r)-2,4-dihydroxy-n-[(3s)-3-hydroxy-4-phenylbutyl]-3,3-dimethylbutanamide) ligands, two <scene name='48/483891/Peg/1'>PEG</scene> (di(hydroxyethyl) ether) ligands, and eight <scene name='48/483891/Nag/1'>NAG</scene> (N-acetyl-d-glucosamine) ligands. | ||
| + | ==Binding Interactions== | ||
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| - | ==Binding Interactions== | ||
4CYG is a key protein that is involved in the breakdown of pantetheine to panthothenic acid and cysteamine. These proteins are associated with many metabolic diseases like type 2 diabetes. Understanding the binding interaction would give insight into treating these diseases more effectively. 4CYG has three <scene name='48/483891/Binding_site/1'>Catalytic Residues</scene> (Glu79, Lys178 and Cys211) that represents the active site of the enzyme. The purple amino acids represent the three amino acids directly involved in the binding interactions. The active site is located in the center of the enzyme in between the two sub-units. It was discovered that Glu79 and Lys178 were responsible for orienting and activating Cys211 to catalyze the reaction. The substrate forms a covalent bond with Cys211 producing the transition state.[1] | 4CYG is a key protein that is involved in the breakdown of pantetheine to panthothenic acid and cysteamine. These proteins are associated with many metabolic diseases like type 2 diabetes. Understanding the binding interaction would give insight into treating these diseases more effectively. 4CYG has three <scene name='48/483891/Binding_site/1'>Catalytic Residues</scene> (Glu79, Lys178 and Cys211) that represents the active site of the enzyme. The purple amino acids represent the three amino acids directly involved in the binding interactions. The active site is located in the center of the enzyme in between the two sub-units. It was discovered that Glu79 and Lys178 were responsible for orienting and activating Cys211 to catalyze the reaction. The substrate forms a covalent bond with Cys211 producing the transition state.[1] | ||
Revision as of 03:13, 11 April 2016
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
Pantetheinase (4CYG)[1]
by [Luke Schnitzler, Patrick Tonne, Owen O'Connor, Tyler Russell, Nicholas Sant]
Student Projects for UMass Chemistry 423 Spring 2016
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