Sandbox Wabash28 - Revision history

Student at 01:56, 19 February 2016

Student — Fri, 19 Feb 2016 01:56:56 GMT

←Older revision		Revision as of 01:56, 19 February 2016
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	As before, His 57 again attacks a proton (this time from water) supported by Asp 102. The more nucleophilic water attacks the ester forming a second tetrahedral intermediate.		As before, His 57 again attacks a proton (this time from water) supported by Asp 102. The more nucleophilic water attacks the ester forming a second tetrahedral intermediate.

-	The protonated His 57 donates that proton to the Ser 195 oxygen making it a stable leaving group as the carbonyl reforms as a carboxylic acid. The N-terminus leaves the active site and trypsin is ready to repeat the process.	+	The protonated His 57 donates that proton to the Ser 195 oxygen making it a stable leaving group as the carbonyl reforms as a carboxylic acid. The N-terminus leaves the active site and trypsin is ready to repeat the process. <scene name='72/725339/Back_to_start/1'>Back to the Start</scene>

	== Function ==		== Function ==

Student at 01:40, 19 February 2016

Student — Fri, 19 Feb 2016 01:40:52 GMT

←Older revision		Revision as of 01:40, 19 February 2016
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	Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site contains two glycines and an aspartic acid. This binding site's glycines permit the bulkier lysine and arginine residues to nestle within the pocket and interact ionically with the aspartate residue thereby holding the peptide in place for hydrolysis. Trypsin is inactivated by the lysine-mimicking tosyl-L-lysine chloromethylketone as well as by enzymes trypsin activates within the body.		Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site contains two glycines and an aspartic acid. This binding site's glycines permit the bulkier lysine and arginine residues to nestle within the pocket and interact ionically with the aspartate residue thereby holding the peptide in place for hydrolysis. Trypsin is inactivated by the lysine-mimicking tosyl-L-lysine chloromethylketone as well as by enzymes trypsin activates within the body.

-	First, the substrate peptide binds to trypsin. Specifically, a lysine or arginine binds to the binding pocket's aspartate (Asp 189).	+	First, the substrate peptide binds to trypsin. Specifically, a lysine or arginine binds to the binding pocket's aspartate (Asp 189). <scene name='72/725339/Specificity_pocket/2'>Specificity Pocket</scene>

	Made more nucleophilic by a base attack from His 57 (a residue itself stabilized via hydrogen bonding with Asp 102), Ser 195 attacks the scissile bond at the carbonyl forming a tetrahedral intermediate. These three residues (Asp 102, His 57, and Ser 195) form a conserved active site among serine proteases called the catalytic triad. <scene name='72/725339/Ser_195_attack_peptide/1'>Catalytic Triad</scene>		Made more nucleophilic by a base attack from His 57 (a residue itself stabilized via hydrogen bonding with Asp 102), Ser 195 attacks the scissile bond at the carbonyl forming a tetrahedral intermediate. These three residues (Asp 102, His 57, and Ser 195) form a conserved active site among serine proteases called the catalytic triad. <scene name='72/725339/Ser_195_attack_peptide/1'>Catalytic Triad</scene>

Student at 01:19, 19 February 2016

Student — Fri, 19 Feb 2016 01:19:02 GMT

←Older revision		Revision as of 01:19, 19 February 2016
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	First, the substrate peptide binds to trypsin. Specifically, a lysine or arginine binds to the binding pocket's aspartate (Asp 189).		First, the substrate peptide binds to trypsin. Specifically, a lysine or arginine binds to the binding pocket's aspartate (Asp 189).

-	Made more nucleophilic by a base attack from His 57 (a residue itself stabilized via hydrogen bonding with Asp 102), Ser 195 attacks the scissile bond at the carbonyl forming a tetrahedral intermediate. These three residues (Asp 102, His 57, and Ser 195) form a conserved active site among serine proteases called the catalytic triad. <scene name='72/725339/~~Stick_substrate~~/1'>~~Ser 195~~</scene>	+	Made more nucleophilic by a base attack from His 57 (a residue itself stabilized via hydrogen bonding with Asp 102), Ser 195 attacks the scissile bond at the carbonyl forming a tetrahedral intermediate. These three residues (Asp 102, His 57, and Ser 195) form a conserved active site among serine proteases called the catalytic triad. <scene name='72/725339/Ser_195_attack_peptide/1'>Catalytic Triad</scene>

-	His 57 donates its proton to the forming amine making it a good leaving group. Simultaneously, the carbonyl reforms by kicking off the amine. The ester formed between Ser 195 and the N-terminus is known as the acyl-enzyme intermediate. The C-terminus leaves the active site and water enters.	+	His 57 donates its proton to the forming amine making it a good leaving group. Simultaneously, the carbonyl reforms by kicking off the amine. The ester formed between Ser 195 and the N-terminus is known as the acyl-enzyme intermediate. The C-terminus leaves the active site and water enters.

	As before, His 57 again attacks a proton (this time from water) supported by Asp 102. The more nucleophilic water attacks the ester forming a second tetrahedral intermediate.		As before, His 57 again attacks a proton (this time from water) supported by Asp 102. The more nucleophilic water attacks the ester forming a second tetrahedral intermediate.

Student: /* Mechanism of Trypsin (By: Brady Boles, Justin Miller, and Anthony Douglas) */

Student — Thu, 18 Feb 2016 21:42:13 GMT

Mechanism of Trypsin (By: Brady Boles, Justin Miller, and Anthony Douglas)

←Older revision		Revision as of 21:42, 18 February 2016
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	==Mechanism of Trypsin (By: Brady Boles, Justin Miller, and Anthony Douglas)==		==Mechanism of Trypsin (By: Brady Boles, Justin Miller, and Anthony Douglas)==
	<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
-	Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site ~~(catalytic triad)~~ contains two glycines and an aspartic acid. It is inactivated by tosyl-l-lysine chloromethylketone ~~and also~~ by enzymes trypsin activates ~~itself~~.	+	Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site contains two glycines and an aspartic acid. This binding site's glycines permit the bulkier lysine and arginine residues to nestle within the pocket and interact ionically with the aspartate residue thereby holding the peptide in place for hydrolysis. Trypsin is inactivated by the lysine-mimicking tosyl-L-lysine chloromethylketone as well as by enzymes trypsin activates within the body.

		+	First, the substrate peptide binds to trypsin. Specifically, a lysine or arginine binds to the binding pocket's aspartate (Asp 189).
		+
		+	Made more nucleophilic by a base attack from His 57 (a residue itself stabilized via hydrogen bonding with Asp 102), Ser 195 attacks the scissile bond at the carbonyl forming a tetrahedral intermediate. These three residues (Asp 102, His 57, and Ser 195) form a conserved active site among serine proteases called the catalytic triad. <scene name='72/725339/Stick_substrate/1'>Ser 195</scene>
		+
		+	His 57 donates its proton to the forming amine making it a good leaving group. Simultaneously, the carbonyl reforms by kicking off the amine. The ester formed between Ser 195 and the N-terminus is known as the acyl-enzyme intermediate. The C-terminus leaves the active site and water enters.
		+
		+	As before, His 57 again attacks a proton (this time from water) supported by Asp 102. The more nucleophilic water attacks the ester forming a second tetrahedral intermediate.
		+
		+	The protonated His 57 donates that proton to the Ser 195 oxygen making it a stable leaving group as the carbonyl reforms as a carboxylic acid. The N-terminus leaves the active site and trypsin is ready to repeat the process.

-	Serine 195 attacks the scissile bond carbonyl. Ser 195 becomes nucleophilic by base attack from His 57. His 57 will stabilize as a base from aspartic acid and hydrogen bonding. The tetrahedral intermediate collapses back into a carbonyl. <scene name='72/725339/Stick_substrate/1'>Ser 195</scene>
	== Function ==		== Function ==

Student at 06:40, 15 February 2016

Student — Mon, 15 Feb 2016 06:40:51 GMT

←Older revision		Revision as of 06:40, 15 February 2016
Line 4:		Line 4:


-	Serine 195 attacks the scissile bond carbonyl. Ser 195 becomes nucleophilic by base attack from His 57. His 57 will stabilize as a base from aspartic acid and hydrogen bonding. The tetrahedral intermediate collapses back into a carbonyl.	+	Serine 195 attacks the scissile bond carbonyl. Ser 195 becomes nucleophilic by base attack from His 57. His 57 will stabilize as a base from aspartic acid and hydrogen bonding. The tetrahedral intermediate collapses back into a carbonyl. <scene name='72/725339/Stick_substrate/1'>Ser 195</scene>
	== Function ==		== Function ==

Student at 06:19, 15 February 2016

Student — Mon, 15 Feb 2016 06:19:15 GMT

←Older revision		Revision as of 06:19, 15 February 2016
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	</StructureSection>		</StructureSection>
	== References ==		== References ==
-	~~<references/>~~	+	1.↑ Radisky ES, Lee JM, Lu CJ, Koshland DE Jr. Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates. Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277

Student at 06:01, 15 February 2016

Student — Mon, 15 Feb 2016 06:01:17 GMT

←Older revision		Revision as of 06:01, 15 February 2016
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-	==Mechanism of Trypsin==	+	==Mechanism of Trypsin (By: Brady Boles, Justin Miller, and Anthony Douglas)==
	<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
	Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site (catalytic triad) contains two glycines and an aspartic acid. It is inactivated by tosyl-l-lysine chloromethylketone and also by enzymes trypsin activates itself.		Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site (catalytic triad) contains two glycines and an aspartic acid. It is inactivated by tosyl-l-lysine chloromethylketone and also by enzymes trypsin activates itself.

Student at 00:14, 15 February 2016

Student — Mon, 15 Feb 2016 00:14:16 GMT

←Older revision		Revision as of 00:14, 15 February 2016
Line 1:		Line 1:
-	==Mechanism of Trypsin ~~(Andrew Powell, Bilal Jawed, Mazin Hakim)~~==	+	==Mechanism of Trypsin==
	<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
	Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site (catalytic triad) contains two glycines and an aspartic acid. It is inactivated by tosyl-l-lysine chloromethylketone and also by enzymes trypsin activates itself.		Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site (catalytic triad) contains two glycines and an aspartic acid. It is inactivated by tosyl-l-lysine chloromethylketone and also by enzymes trypsin activates itself.

Student at 00:13, 15 February 2016

Student — Mon, 15 Feb 2016 00:13:33 GMT

←Older revision		Revision as of 00:13, 15 February 2016
Line 1:		Line 1:
-	==Mechanism of Trypsin==	+	==Mechanism of Trypsin (Andrew Powell, Bilal Jawed, Mazin Hakim)==
	<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
	Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site (catalytic triad) contains two glycines and an aspartic acid. It is inactivated by tosyl-l-lysine chloromethylketone and also by enzymes trypsin activates itself.		Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site (catalytic triad) contains two glycines and an aspartic acid. It is inactivated by tosyl-l-lysine chloromethylketone and also by enzymes trypsin activates itself.

Student: New page: ==Mechanism of Trypsin== Trypsin is a digestive enzyme synthesized by the pancreas and ...

Student — Fri, 12 Feb 2016 16:55:49 GMT

New page: ==Mechanism of Trypsin== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> Trypsin is a digestive enzyme synthesized by the pancreas and ...

New page

==Mechanism of Trypsin==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site (catalytic triad) contains two glycines and an aspartic acid. It is inactivated by tosyl-l-lysine chloromethylketone and also by enzymes trypsin activates itself.

Serine 195 attacks the scissile bond carbonyl. Ser 195 becomes nucleophilic by base attack from His 57. His 57 will stabilize as a base from aspartic acid and hydrogen bonding. The tetrahedral intermediate collapses back into a carbonyl.
== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>