Sandbox Reserved 914: Difference between revisions

Line 7:

[[Image:pymol.png|300px|left|thumb|'''Figure 1:'''Three dimensional structure of Palmitoyl-Protein Thioesterase 1. The blue color represents the α-helices and the purple represents the β-sheets. The pink signifies random coil.]]

Palmitoyl-Protein Thioesterase 1 (PPT1) is a lysosomal enzyme that plays a role in the degradation of lipid-modified proteins<ref name="human">Palmitoyl-Protein Thioesterase 1 ~~Precursor - Homo Sapiens~~. N.p., 1 Oct. 1996.</ref>. PPT1 derives its catalytic power from its [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad], [http://en.wikipedia.org/wiki/Alpha/beta_hydrolase_fold α/β hydrolase fold], and hydrophobic groove in order to remove fatty acid acyl groups, typically [http://en.wikipedia.org/wiki/Palmitic_acid palmitate] from cysteine residues in proteins<ref name="human"/>. PPT1 is able to be modified by cofactor enzymes, which can induce biological changes<ref name="human"/>. Misregulation of PPT1 modifications can cause various diseases, including infantile neuronal ceroid lipofuscinosis<ref name="PPT"/>, kufs disease<ref name="PPT"/>, and late-infantile neuronal ceroid lipofuscinosis<ref name="PPT"/>. Within these diseases, the production of PPT1 is decreased or eliminated completely, which leads to fatty acid buildup primarily in neuronal cells, leading to slowed developmental progress<ref name="PPT"/>.

Palmitoyl-Protein Thioesterase 1 (PPT1) is a lysosomal enzyme that plays a role in the degradation of lipid-modified proteins<ref name="human">"Palmitoyl Protein Thioesterase 1." UniProt. N.p., 1 Oct. 1996. Web. 10 Apr. 2014.</ref>. PPT1 derives its catalytic power from its [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad], [http://en.wikipedia.org/wiki/Alpha/beta_hydrolase_fold α/β hydrolase fold], and hydrophobic groove in order to remove fatty acid acyl groups, typically [http://en.wikipedia.org/wiki/Palmitic_acid palmitate] from cysteine residues in proteins<ref name="human"/>. PPT1 is able to be modified by cofactor enzymes, which can induce biological changes<ref name="human"/>. Misregulation of PPT1 modifications can cause various diseases, including infantile neuronal ceroid lipofuscinosis<ref name="PPT"/>, kufs disease<ref name="PPT"/>, and late-infantile neuronal ceroid lipofuscinosis<ref name="PPT"/>. Within these diseases, the production of PPT1 is decreased or eliminated completely, which leads to fatty acid buildup primarily in neuronal cells, leading to slowed developmental progress<ref name="PPT"/>.

Sandbox Reserved 914: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 11:56, 22 April 2014 view source Nicole Green (talk \| contribs) 19 edits No edit summary ← Older edit		Revision as of 12:35, 22 April 2014 view source Audrey Wright (talk \| contribs) 48 edits No edit summary Newer edit →
Line 7:		Line 7:
	[[Image:pymol.png\|300px\|left\|thumb\|'''Figure 1:'''Three dimensional structure of Palmitoyl-Protein Thioesterase 1. The blue color represents the α-helices and the purple represents the β-sheets. The pink signifies random coil.]]		[[Image:pymol.png\|300px\|left\|thumb\|'''Figure 1:'''Three dimensional structure of Palmitoyl-Protein Thioesterase 1. The blue color represents the α-helices and the purple represents the β-sheets. The pink signifies random coil.]]

	Palmitoyl-Protein Thioesterase 1 (PPT1) is a lysosomal enzyme that plays a role in the degradation of lipid-modified proteins<ref name="human">Palmitoyl-Protein Thioesterase 1 ~~Precursor - Homo Sapiens~~. N.p., 1 Oct. 1996.</ref>. PPT1 derives its catalytic power from its [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad], [http://en.wikipedia.org/wiki/Alpha/beta_hydrolase_fold α/β hydrolase fold], and hydrophobic groove in order to remove fatty acid acyl groups, typically [http://en.wikipedia.org/wiki/Palmitic_acid palmitate] from cysteine residues in proteins<ref name="human"/>. PPT1 is able to be modified by cofactor enzymes, which can induce biological changes<ref name="human"/>. Misregulation of PPT1 modifications can cause various diseases, including infantile neuronal ceroid lipofuscinosis<ref name="PPT"/>, kufs disease<ref name="PPT"/>, and late-infantile neuronal ceroid lipofuscinosis<ref name="PPT"/>. Within these diseases, the production of PPT1 is decreased or eliminated completely, which leads to fatty acid buildup primarily in neuronal cells, leading to slowed developmental progress<ref name="PPT"/>.		Palmitoyl-Protein Thioesterase 1 (PPT1) is a lysosomal enzyme that plays a role in the degradation of lipid-modified proteins<ref name="human">"Palmitoyl Protein Thioesterase 1." UniProt. N.p., 1 Oct. 1996. Web. 10 Apr. 2014.</ref>. PPT1 derives its catalytic power from its [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad], [http://en.wikipedia.org/wiki/Alpha/beta_hydrolase_fold α/β hydrolase fold], and hydrophobic groove in order to remove fatty acid acyl groups, typically [http://en.wikipedia.org/wiki/Palmitic_acid palmitate] from cysteine residues in proteins<ref name="human"/>. PPT1 is able to be modified by cofactor enzymes, which can induce biological changes<ref name="human"/>. Misregulation of PPT1 modifications can cause various diseases, including infantile neuronal ceroid lipofuscinosis<ref name="PPT"/>, kufs disease<ref name="PPT"/>, and late-infantile neuronal ceroid lipofuscinosis<ref name="PPT"/>. Within these diseases, the production of PPT1 is decreased or eliminated completely, which leads to fatty acid buildup primarily in neuronal cells, leading to slowed developmental progress<ref name="PPT"/>.